| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01028435001 |
| Family | GT47 |
| Protein Properties | Length: 1319 Molecular Weight: 145385 Isoelectric Point: 8.5183 |
| Chromosome | Chromosome/Scaffold: 7 Start: 7494452 End: 7501710 |
| Description | Subtilase family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT47 | 235 | 456 | 0 |
| QFAVDRPEWKIMGGKDHFLVAGRITWDFRRLTDLESDWGNKLLFLPAAKNMSMLVVESSPWNANDFGIPYPTYFHPAKDTDVLIWQDRMRKLERKWLFSF AGAPRPGNTKSIRGQIIDQCRTSKVGKLLECDFGESKCHSPSSIMQMFQSSLFCLQPQGDSYTRRSAFDSMLAGCIPVFFHPGSAYTQYTWHLPKNFSSY SVFIPEDDIRKRNVSIEERLGQ | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1319 Download |
| MNGIAGATSP EAPRGKNTPT TDTRGPAHVA KMRLAATSAI YTLTHILLLG WNLMRRRPTT 60 TILPEQMDKG MPKNQQTRLC FLASLSALFW VLLLYFHFVV LGNSNVDESV QLTTIPVATQ 120 SHITSVITSP PEVTNLAKSP YPELNKETSL AQSKLDNYPF MRALRTVENK SDPCGGRYIY 180 VHDLPPRFNE DMLKECKSLS LWTNMCTFTS NAGLGPPLEN VEGVFSNTGW YATNQFAVDR 240 PEWKIMGGKD HFLVAGRITW DFRRLTDLES DWGNKLLFLP AAKNMSMLVV ESSPWNANDF 300 GIPYPTYFHP AKDTDVLIWQ DRMRKLERKW LFSFAGAPRP GNTKSIRGQI IDQCRTSKVG 360 KLLECDFGES KCHSPSSIMQ MFQSSLFCLQ PQGDSYTRRS AFDSMLAGCI PVFFHPGSAY 420 TQYTWHLPKN FSSYSVFIPE DDIRKRNVSI EERLGQIPPE QVKAMREEVI SLIPRLIYAD 480 PRSKLETLKD AFDVAVQAVI GKVTKLRKDI IGGQTDDNFV EENSWKYDLL EEGQREVGPH 540 EWDPFFSKPK DQNGDSGACI QLQALPLCSH SSMEAKAQLL FSVLFLFLVF VHAQSLQTYI 600 IQLHPHGATA SSFSSKVQWH LSFLERIMFS EDDPSSRLLY SYHSAMEGFA AQLSETELES 660 LRKLGEVIAV RPDTRLQLHT TYSYKFLGLS PASRGGWFQS GFGHGTIVGV LDTGVWPESP 720 SFSDHGMPPV PKKWRGVCQE GQDFNSSNCN RKLIGARFFS KGHRVASISP SSDTVVEYVS 780 ARDSHGHGTH TSSTAGGASV PMASVLVCWF SGCYSSDILA AMDVAIRDGV DILSLSLGGF 840 PIPLFDDSIA IGSFRAMEHG ISVICAAGNN GPIQSSVANE APWITTVGAS TLDRRFPAIV 900 RMGNGKRLYG ESMYPGKHNP YAGKELELVY VTGGDSGSEF CFKGSLPRAK VLGKMVVCDR 960 GVNGRAEKGE AVKEAGGAAM ILANTDINLE EDSVDAHVLP ASLIGFAESV QLKSYMNSSR 1020 TPTARIEFGG TVIGKSRAPA VAQFSSRGPS LTNPTILKPD IIAPGVNIIA AWPQNLGPSG 1080 LPEDSRRVNF TVMSGTSMAC PHISGIAALI HSANPTWTPA AIKSAMITTA DVTDHTGKPI 1140 MDSNKPAGVF AMGAGQVNPE KAIDPGLIYD IKPDEYITHL CTLGYTRSEI SAITHRNVSC 1200 HELVQKNKGF SLNYPSISVI FRHGMMSRMI KRRLTNVGVP NSIYSVEVVA PEGVKVRVKP 1260 HHLIFKHINQ SLSYRVWFIS RKRTGEEKTR FAQGHLTWVH SHHTSYKVRS PISVTWAK* 1320 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd07474 | Peptidases_S8_subtilisin_Vpr-like | 4.0e-12 | 812 | 899 | 91 | + Peptidase S8 family domain in Vpr-like proteins. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. | ||
| cd07474 | Peptidases_S8_subtilisin_Vpr-like | 2.0e-29 | 1021 | 1162 | 146 | + Peptidase S8 family domain in Vpr-like proteins. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. | ||
| cd04852 | Peptidases_S8_3 | 4.0e-34 | 1055 | 1131 | 77 | + Peptidase S8 family domain, uncharacterized subfamily 3. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. | ||
| pfam03016 | Exostosin | 8.0e-48 | 173 | 457 | 331 | + Exostosin family. The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear. | ||
| cd04852 | Peptidases_S8_3 | 5.0e-86 | 676 | 892 | 239 | + Peptidase S8 family domain, uncharacterized subfamily 3. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004252 | serine-type endopeptidase activity |
| GO:0006508 | proteolysis |
| GO:0016020 | membrane |
| GO:0042802 | identical protein binding |
| GO:0043086 | negative regulation of catalytic activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI37197.1 | 0 | 1 | 1318 | 1 | 1318 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_563701.1 | 0 | 581 | 1315 | 6 | 771 | SDD1 (STOMATAL DENSITY AND DISTRIBUTION); serine-type endopeptidase [Arabidopsis thaliana] |
| RefSeq | XP_002269766.1 | 0 | 47 | 1318 | 52 | 1413 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002301847.1 | 0 | 646 | 1316 | 1 | 691 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002526537.1 | 0 | 573 | 1316 | 1 | 766 | Cucumisin precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3i74_B | 0 | 680 | 1312 | 1 | 640 | C Chain C, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 In Complex With A Chloromethylketone Inhibitor |
| PDB | 3i74_A | 0 | 680 | 1312 | 1 | 640 | C Chain C, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 In Complex With A Chloromethylketone Inhibitor |
| PDB | 3i6s_B | 0 | 680 | 1312 | 1 | 640 | A Chain A, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 |
| PDB | 3i6s_A | 0 | 680 | 1312 | 1 | 640 | A Chain A, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 |
| PDB | 3vta_B | 0 | 680 | 1315 | 1 | 618 | A Chain A, Crystal Structure Of Cucumisin, A Subtilisin-Like Endoprotease From Cucumis Melo L |
