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CAZyme Information: MGYG000001518_03578
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Gorillibacterium timonense | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Gorillibacterium; Gorillibacterium timonense | |||||||||||
| CAZyme ID | MGYG000001518_03578 | |||||||||||
| CAZy Family | CBM50 | |||||||||||
| CAZyme Description | Gamma-D-glutamyl-L-diamino acid endopeptidase 1 | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1138257; End: 1139483 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd06229 | M14_Endopeptidase_I | 1.31e-115 | 157 | 393 | 1 | 238 | Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I. Peptidase M14-like domain of Gamma-D-glutamyl-L-diamino acid endopeptidase 1 (also known as Gamma-D-glutamyl-meso-diaminopimelate peptidase I, and Endopeptidase I (ENP1); EC 3.4.19.11). ENP1 is a member of the M14 family of metallocarboxypeptidases (MCPs), and is classified as belonging to subfamily C. However it has an exceptional type of activity of hydrolyzing the gamma-D-Glu-(L)meso-diaminopimelic acid (gamma-D-Glu-Dap) bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. ENP1 has a different substrate specificity and cellular role than MpaA (MpaA does not belong to this group). ENP1 hydrolyzes the gamma-D-Glu-Dap bond of MurNAc-tripeptide and MurNAc-tetrapeptide, as well as the amide bond of free tripeptide and tetrapeptide. ENP1 is active on spore cortex peptidoglycan, and is produced at stage IV of sporulation in forespore and spore integuments. |
| smart00631 | Zn_pept | 5.01e-48 | 127 | 382 | 17 | 273 | Zn_pept domain. |
| cd00596 | Peptidase_M14_like | 9.16e-38 | 157 | 382 | 1 | 205 | M14 family of metallocarboxypeptidases and related proteins. The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism. |
| pfam00246 | Peptidase_M14 | 1.64e-34 | 127 | 388 | 11 | 283 | Zinc carboxypeptidase. |
| cd03859 | M14_CPT | 5.59e-34 | 128 | 388 | 21 | 287 | Peptidase M14 Carboxypeptidase T subfamily. Peptidase M14-like domain of carboxypeptidase (CP) T (CPT), CPT belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPT has moderate similarity to CPA and CPB, and exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues like CPA and C-terminal positively charged residues like CPB. CPA and CPB are M14 family peptidases but do not belong to this CPT group. The substrate specificity difference between CPT and CPA and CPB is ascribed to a few amino acid substitutions at the substrate-binding pocket while the spatial organization of the binding site remains the same as in all Zn-CPs. CPT has increased thermal stability in presence of Ca2+ ions, and two disulfide bridges which give an additional stabilization factor. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BBH19109.1 | 9.42e-133 | 5 | 397 | 4 | 397 |
| QAV17934.1 | 6.89e-132 | 1 | 398 | 1 | 399 |
| QYR23328.1 | 1.64e-131 | 5 | 400 | 4 | 400 |
| BAD40552.1 | 8.89e-125 | 1 | 398 | 1 | 399 |
| SYX85282.1 | 2.04e-123 | 1 | 397 | 1 | 398 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7EQX_C | 1.32e-11 | 116 | 400 | 11 | 296 | ChainC, Carboxypeptidase B [Aedes aegypti],7EQX_D Chain D, Carboxypeptidase B [Aedes aegypti],7EQZ_A Chain A, Carboxypeptidase B [Aedes aegypti] |
| 4UIA_A | 1.97e-10 | 136 | 388 | 35 | 290 | Crystalstructure of 3a in complex with tafCPB [Sus scrofa],4UIB_A Crystal structure of 3p in complex with tafCPB [Sus scrofa],5LYD_A Crystal structure of 1 in complex with tafCPB [Sus scrofa],5LYF_A Crystal structure of 1 in complex with tafCPB [Sus scrofa],5LYI_A Crystal structure of 1 in complex with tafCPB [Sus scrofa],5LYL_A Crystal structure of 1 in complex with tafCPB [Sus scrofa] |
| 4Z65_A | 8.34e-10 | 136 | 388 | 33 | 288 | CarboxypeptidaseB with Sulphamoil Arginine [Sus scrofa],5J1Q_A Carboxypeptidase B with Sulphamoil Phenylalanine [Sus scrofa],5JC6_A Carboxypeptidase B with 2-nd zinc and acetate ion [Sus scrofa],5ZEQ_A Carboxypeptidase B in complex with DD28 [Sus scrofa] |
| 1Z5R_A | 8.46e-10 | 136 | 388 | 35 | 290 | CrystalStructure of Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1Z5R_B Crystal Structure of Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1Z5R_C Crystal Structure of Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1ZG7_A Crystal Structure of 2-(5-{[amino(imino)methyl]amino}-2-chlorophenyl)-3-sulfanylpropanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1ZG7_B Crystal Structure of 2-(5-{[amino(imino)methyl]amino}-2-chlorophenyl)-3-sulfanylpropanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1ZG7_C Crystal Structure of 2-(5-{[amino(imino)methyl]amino}-2-chlorophenyl)-3-sulfanylpropanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1ZG8_A Crystal Structure of (R)-2-(3-{[amino(imino)methyl]amino}phenyl)-3-sulfanylpropanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1ZG8_B Crystal Structure of (R)-2-(3-{[amino(imino)methyl]amino}phenyl)-3-sulfanylpropanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1ZG8_C Crystal Structure of (R)-2-(3-{[amino(imino)methyl]amino}phenyl)-3-sulfanylpropanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1ZG9_A Crystal Structure of 5-{[amino(imino)methyl]amino}-2-(sulfanylmethyl)pentanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1ZG9_B Crystal Structure of 5-{[amino(imino)methyl]amino}-2-(sulfanylmethyl)pentanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],1ZG9_C Crystal Structure of 5-{[amino(imino)methyl]amino}-2-(sulfanylmethyl)pentanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B [Sus scrofa],2JEW_A Chain A, CARBOXYPEPTIDASE B [Sus scrofa],2PIY_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B (S)-2-(3-Aminomethyl-phenyl)-3-{hydroxy-[(R)-2-methyl-1-(3-phenyl-propane-1-sulfonylamino)-propyl]-phosphinoyl}-propionic acid {ZK 528} COMPLEX [Sus scrofa],2PIY_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B (S)-2-(3-Aminomethyl-phenyl)-3-{hydroxy-[(R)-2-methyl-1-(3-phenyl-propane-1-sulfonylamino)-propyl]-phosphinoyl}-propionic acid {ZK 528} COMPLEX [Sus scrofa],2PIY_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B (S)-2-(3-Aminomethyl-phenyl)-3-{hydroxy-[(R)-2-methyl-1-(3-phenyl-propane-1-sulfonylamino)-propyl]-phosphinoyl}-propionic acid {ZK 528} COMPLEX [Sus scrofa],2PIZ_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Guanidino-phenyl)-3-[hydroxy-(3-phenyl-propyl)-phosphinoyl]-propionic acid COMPLEX [Sus scrofa],2PIZ_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Guanidino-phenyl)-3-[hydroxy-(3-phenyl-propyl)-phosphinoyl]-propionic acid COMPLEX [Sus scrofa],2PIZ_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Guanidino-phenyl)-3-[hydroxy-(3-phenyl-propyl)-phosphinoyl]-propionic acid COMPLEX [Sus scrofa],2PJ0_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B [((R)-1-Benzyloxycarbonylamino-2-methyl-propyl)-hydroxy-phosphinoyloxy]-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],2PJ0_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B [((R)-1-Benzyloxycarbonylamino-2-methyl-propyl)-hydroxy-phosphinoyloxy]-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],2PJ0_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B [((R)-1-Benzyloxycarbonylamino-2-methyl-propyl)-hydroxy-phosphinoyloxy]-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],2PJ1_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B (3-Aminomethyl-phenyl)-[((R)-1-benzyloxycarbonylamino-2-methyl-propyl)-hydroxy-phosphinoyloxy]-acetic acid COMPLEX [Sus scrofa],2PJ1_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B (3-Aminomethyl-phenyl)-[((R)-1-benzyloxycarbonylamino-2-methyl-propyl)-hydroxy-phosphinoyloxy]-acetic acid COMPLEX [Sus scrofa],2PJ1_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B (3-Aminomethyl-phenyl)-[((R)-1-benzyloxycarbonylamino-2-methyl-propyl)-hydroxy-phosphinoyloxy]-acetic acid COMPLEX [Sus scrofa],2PJ2_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-[((R)-1-benzyloxycarbonylamino-2-methyl-propyl)-hydroxy-phosphinoyl]-propionic acid COMPLEX [Sus scrofa],2PJ2_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-[((R)-1-benzyloxycarbonylamino-2-methyl-propyl)-hydroxy-phosphinoyl]-propionic acid COMPLEX [Sus scrofa],2PJ2_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-[((R)-1-benzyloxycarbonylamino-2-methyl-propyl)-hydroxy-phosphinoyl]-propionic acid COMPLEX [Sus scrofa],2PJ3_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B (3-Guanidino-phenyl)-{hydroxy-[(R)-2-methyl-1-(3-phenyl-propionylamino)-propyl]-phosphinoyloxy}-acetic acid COMPLEX [Sus scrofa],2PJ3_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B (3-Guanidino-phenyl)-{hydroxy-[(R)-2-methyl-1-(3-phenyl-propionylamino)-propyl]-phosphinoyloxy}-acetic acid COMPLEX [Sus scrofa],2PJ3_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B (3-Guanidino-phenyl)-{hydroxy-[(R)-2-methyl-1-(3-phenyl-propionylamino)-propyl]-phosphinoyloxy}-acetic acid COMPLEX [Sus scrofa],2PJ4_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B [((R)-Benzyloxycarbonylamino-cyclohexyl-methyl)-hydroxy-phosphinoyloxy]-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],2PJ4_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B [((R)-Benzyloxycarbonylamino-cyclohexyl-methyl)-hydroxy-phosphinoyloxy]-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],2PJ5_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B [((R)-1-Benzyloxycarbonylamino-hexyl)-hydroxy-phosphinoyloxy]-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],2PJ5_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B [((R)-1-Benzyloxycarbonylamino-hexyl)-hydroxy-phosphinoyloxy]-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],2PJ5_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B [((R)-1-Benzyloxycarbonylamino-hexyl)-hydroxy-phosphinoyloxy]-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],2PJ6_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-{hydroxy-[(R)-2-methyl-1-(2-phenyl-ethanesulfonylamino)-propyl]-phosphinoyl}-propionic acid COMPLEX [Sus scrofa],2PJ7_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-[((R)-1-benzenesulfonylamino-2-methyl-propyl)-hydroxy-phosphinoyl]-propionic acid COMPLEX [Sus scrofa],2PJ7_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-[((R)-1-benzenesulfonylamino-2-methyl-propyl)-hydroxy-phosphinoyl]-propionic acid COMPLEX [Sus scrofa],2PJ7_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-[((R)-1-benzenesulfonylamino-2-methyl-propyl)-hydroxy-phosphinoyl]-propionic acid COMPLEX [Sus scrofa],2PJ8_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-{[(R)-1-(biphenyl-4-sulfonylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-propionic acid COMPLEX [Sus scrofa],2PJ8_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-{[(R)-1-(biphenyl-4-sulfonylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-propionic acid COMPLEX [Sus scrofa],2PJ8_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-{[(R)-1-(biphenyl-4-sulfonylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-propionic acid COMPLEX [Sus scrofa],2PJ9_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-{[(R)-1-(benzo[1,2,5]thiadiazole-4-sulfonylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-propionic acid COMPLEX [Sus scrofa],2PJA_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 3-{[(R)-1-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-2-(3-guanidino-phenyl)-propionic acid COMPLEX [Sus scrofa],2PJA_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 3-{[(R)-1-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-2-(3-guanidino-phenyl)-propionic acid COMPLEX [Sus scrofa],2PJA_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 3-{[(R)-1-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-2-(3-guanidino-phenyl)-propionic acid COMPLEX [Sus scrofa],2PJB_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-{[1-((S)-2-benzyloxycarbonylamino-3-phenyl-propane-1-sulfonylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-propionic acid COMPLEX [Sus scrofa],2PJB_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-{[1-((S)-2-benzyloxycarbonylamino-3-phenyl-propane-1-sulfonylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-propionic acid COMPLEX [Sus scrofa],2PJB_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-{[1-((S)-2-benzyloxycarbonylamino-3-phenyl-propane-1-sulfonylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-propionic acid COMPLEX [Sus scrofa],2PJC_A CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B ({(R)-1-[(S)-2-Benzyloxycarbonylamino-3-(4-hydroxy-phenyl)-propionylamino]-2-methyl-propyl}-hydroxy-phosphinoyloxy)-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],2PJC_B CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B ({(R)-1-[(S)-2-Benzyloxycarbonylamino-3-(4-hydroxy-phenyl)-propionylamino]-2-methyl-propyl}-hydroxy-phosphinoyloxy)-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],2PJC_C CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B ({(R)-1-[(S)-2-Benzyloxycarbonylamino-3-(4-hydroxy-phenyl)-propionylamino]-2-methyl-propyl}-hydroxy-phosphinoyloxy)-(3-guanidino-phenyl)-acetic acid COMPLEX [Sus scrofa],3WAB_A Carboxypeptidase B in complex with DD2 [Sus scrofa],3WC5_A Carboxypeptidase B in complex with DD9 [Sus scrofa],3WC6_A Carboxypeptidase B in complex with 2nd zinc [Sus scrofa],3WC7_A Carboxypeptidase B in complex with EF6265 [Sus scrofa],5LRG_A Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin B complex [Sus scrofa],5LRG_B Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin B complex [Sus scrofa],5LRG_C Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin B complex [Sus scrofa],5LRJ_A Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin C complex [Sus scrofa],5LRJ_B Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin C complex [Sus scrofa],5LRJ_C Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin C complex [Sus scrofa],5LRK_A Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin F complex [Sus scrofa],5LRK_B Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin F complex [Sus scrofa],5LRK_C Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin F complex [Sus scrofa] |
| 3GLJ_A | 1.31e-09 | 136 | 388 | 130 | 385 | Apolymorph of carboxypeptidase B zymogen structure [Sus scrofa] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q03415 | 1.12e-98 | 112 | 397 | 110 | 394 | Gamma-D-glutamyl-L-diamino acid endopeptidase 1 OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1 |
| P54497 | 2.36e-67 | 128 | 397 | 100 | 372 | Uncharacterized protein YqgT OS=Bacillus subtilis (strain 168) OX=224308 GN=yqgT PE=3 SV=1 |
| E5A0U8 | 1.42e-11 | 108 | 320 | 205 | 423 | Inactive metallocarboxypeptidase ECM14 OS=Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) OX=985895 GN=ECM14 PE=3 SV=1 |
| Q8R4H4 | 6.09e-11 | 134 | 337 | 163 | 351 | Carboxypeptidase A5 OS=Mus musculus OX=10090 GN=Cpa5 PE=2 SV=1 |
| P00732 | 3.17e-09 | 136 | 320 | 145 | 314 | Carboxypeptidase B OS=Bos taurus OX=9913 GN=CPB1 PE=1 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000051 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |