Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10431347g0010 |
Family | GH19 |
Protein Properties | Length: 626 Molecular Weight: 68726.6 Isoelectric Point: 8.5404 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH19 | 37 | 219 | 0 |
PSSCKGKSFYNYNSFIAAADSFPTFGGTGSSADARREVAAFLANVVDTSQEFCYIAQSNAQPSCNQSSSKYPCANGDRYYARGPLRLTGNYNYEAAGKYL KLDLLGNPDKVSENSTISFQTAIWLWTNGSKSHTAIVSGQGFAATVKALNSSACNDDAKLKSMVANYKAYCNYFGVDPGSNLG |
Full Sequence |
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Protein Sequence Length: 626 Download |
METPQGFIAA FLLLLTMAVM EGVAVSAYRI LSGAPAPSSC KGKSFYNYNS FIAAADSFPT 60 FGGTGSSADA RREVAAFLAN VVDTSQEFCY IAQSNAQPSC NQSSSKYPCA NGDRYYARGP 120 LRLTGNYNYE AAGKYLKLDL LGNPDKVSEN STISFQTAIW LWTNGSKSHT AIVSGQGFAA 180 TVKALNSSAC NDDAKLKSMV ANYKAYCNYF GVDPGSNLGS CHSETTPWKT IPPRSRRKPE 240 SLNPILLGSI GGTALIFCLV LLICWLSARW RRRYSRAGEG EGEESRLVYF DYQMLREATK 300 GFDARNKLGQ GGFGEVYKGI LRDGTPVAVK KLFPRQSSQA VVEFHTEIEA ISGVLHRNIL 360 CLLGYCTHRQ KRFLVYEFMP KRSLDIHLFG DRGIFLKWEA RFQIITGIAR GLAYLHEHSR 420 VSVVHRDIKA GNILLDDNLH PKIADFGLAK LFPDDRTHIT TNVGGTIGYM APEYVVHGHL 480 TQKADVYSYG VLVLEILTGR KCMDTRLPSP ILLQWAWSLY ERNENINIVD PKLEVQGMSE 540 NERGQVLRVV LIAFLCVQGL SSQRPSMSMV LTMLTGDSEI LVAPSAPALI DCEHISVASS 600 ATPQTLSAAA SSSTSHATMS NSMCPR |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00219 | TyrKc | 5.0e-52 | 307 | 498 | 197 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam07714 | Pkinase_Tyr | 3.0e-52 | 307 | 499 | 199 | + Protein tyrosine kinase. | ||
pfam00182 | Glyco_hydro_19 | 9.0e-53 | 38 | 218 | 218 | + Chitinase class I. | ||
smart00221 | STYKc | 3.0e-53 | 307 | 498 | 197 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
cd00325 | chitinase_glyco_hydro_19 | 4.0e-64 | 29 | 219 | 223 | + Glycoside hydrolase family 19 chitinase domain. Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Family 19 chitinases are found primarily in plants (classes I, III, and IV), but some are found in bacteria. Class I and II chitinases are similar in their catalytic domains. Class I chitinases have an N-terminal cysteine-rich, chitin-binding domain which is separated from the catalytic domain by a proline and glycine-rich hinge region. Class II chitinases lack both the chitin-binding domain and the hinge region. Class IV chitinases are similar to class I chitinases but they are smaller in size due to certain deletions. Despite any significant sequence homology with lysozymes, structural analysis reveals that family 19 chitinases, together with family 46 chitosanases, are similar to several lysozymes including those from T4-phage and from goose. The structures reveal that the different enzyme groups arose from a common ancestor glycohydrolase antecedent to the procaryotic/eucaryotic divergence. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAE04238.2 | 0 | 277 | 591 | 55 | 372 | OSJNBa0011F23.11 [Oryza sativa (japonica cultivar-group)] |
EMBL | CAH67794.1 | 0 | 277 | 591 | 55 | 372 | OSIGBa0132E09-OSIGBa0108L24.8 [Oryza sativa (indica cultivar-group)] |
RefSeq | XP_002308093.1 | 0 | 289 | 590 | 9 | 309 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002324661.1 | 0 | 291 | 589 | 1 | 298 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002447257.1 | 0 | 282 | 612 | 60 | 391 | hypothetical protein SORBIDRAFT_06g031420 [Sorghum bicolor] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3ulz_A | 0 | 286 | 577 | 16 | 309 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 3uim_A | 0 | 286 | 577 | 16 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 286 | 577 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 286 | 577 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 286 | 577 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |