Q8JIR2

PR
Gene name
Protein name
Zinc metalloproteinase/disintegrin-like HR1a
Names
Snake venom metalloproteinase, SVMP
Species
Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
KEGG Pathway
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

141-216 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8JIR2

Entry ID Method Resolution Chain Position Source
AF-Q8JIR2-F1 Predicted AlphaFoldDB

No variants for Q8JIR2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8JIR2

No associated diseases with Q8JIR2

6 regional properties for Q8JIR2

Type Name Position InterPro Accession
domain Peptidase M12B, ADAM/reprolysin 200 - 396 IPR001590
domain Disintegrin domain 404 - 490 IPR001762
domain Peptidase M12B, propeptide 47 - 150 IPR002870
domain ADAM, cysteine-rich domain 489 - 605 IPR006586
conserved_site Disintegrin, conserved site 444 - 463 IPR018358
domain Reprolysin domain, adamalysin-type 200 - 394 IPR034027

Functions

Description
EC Number
Subcellular Localization
  • Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

4 GO annotations of molecular function

Name Definition
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
metallopeptidase activity Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
toxin activity Interacting selectively with one or more biological molecules in another (target) organism, initiating pathogenesis (leading to an abnormal, generally detrimental state) in the target organism. The activity should refer to an evolved function of the active gene product, i.e. one that was selected for. Examples include the activity of botulinum toxin, and snake venom.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIQVLLVTIC LAVFPYQGSS IILGSGNVND YEVVYPRKVT AVPKGAVQPK YEDTMQYEFK
70 80 90 100 110 120
VNGEPVVLHL EKNKGLFSKD YSETHYSPDG REITTYPSVE DHCYYHGRIQ NDADSTASIS
130 140 150 160 170 180
ACNGLKGHFK LQGEMYLIEP LRFSDSEAHA VFKYENVEKE DEAPKMCGVT QTNWESDEPI
190 200 210 220 230 240
KKASKLVVTA EQQRYLNNFR FIELVIVADY RMFTKFNSNL NEVKTWVYEI VNTLNEIYRY
250 260 270 280 290 300
LYVRVALVAL EVWSNGDLSS VTLSAYDTLD SFGEWRKRDL LKRKSHDNAQ LLTAIDFNGT
310 320 330 340 350 360
IIGLAHVASM CDPKCSTGIV QDYSSRNLVV AVIMAHEMGH NLGIRHDREN CTCHANSCIM
370 380 390 400 410 420
SAVISDQPSK YFSNCSHVQY WNYINDDEPQ CILNEPLRTD IVSPPVCGNE LLEVGEECDC
430 440 450 460 470 480
GSPATCRYPC CDAATCKLHS WVECESGECC EQCRFRTAGT ECRARRSECD IAESCTGHSA
490 500 510 520 530 540
DCPTDRFHRN GQPCLHNFGY CYNGNCPIMY HQCYALWGAN ATVAKDSCFE DNQKGNDYGY
550 560 570 580 590 600
CRKENGRKIP CEPQDVKCGR LYCSLGNQLP CRFFYTPTDE NIGMVDTGTK CGDKKVCSNR
QCVDVNTAY