ID A0A3Q2DAQ9_CYPVA Unreviewed; 674 AA.
AC A0A3Q2DAQ9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000015798.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000015798.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
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DR Ensembl; ENSCVAT00000023947.1; ENSCVAP00000015783.1; ENSCVAG00000018708.1.
DR Ensembl; ENSCVAT00000031668.1; ENSCVAP00000015798.1; ENSCVAG00000018708.1.
DR GeneTree; ENSGT00950000183111; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR008974; TRAF-like.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF884; METALLOENDOPEPTIDASE; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00629; MAM; 1.
DR PRINTS; PR00480; ASTACIN.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS50060; MAM_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 19..674
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5041475419"
FT DOMAIN 55..251
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 258..432
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 284..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 674 AA; 75385 MW; C93265118A824A64 CRC64;
MRLLGYFCLV LNLAFSSALS LPSAEVEIVD VGENNTIEED LTLDDIREPP NIQRSSILPG
NDLWTSPIPY VLDKDLELNA KGFIMRAFEQ FRLKSCIDFK PKYSEDYYID IQKLDGCFSY
IGRQFANGQD LSIGSGCDSL AIVEHEILHA LGFYHEQSRF DRDDFVQIVP ANIITGTEHN
FRKVSSDEST THGTPYDYMS VMHYGKNAFS NGNGNGTTII TVDPRFQDVI GQRLEMSPSD
VEELNLLYNC NATISFIFYC GFSNGTMCQM SRCSQNGSNW EVVTQTPGGP SSDHTSLSSG
SGDNGQQTGY FIHGSTATGQ EGDSARLETE EVKPNRGCNV QCLQFYYFHS GNESDELNIW
IREFQDEQDT NGVLRLMSQI TGSPTSHWKI HHVSLNATKN FQVVFEVRKG AGNSTGGFSI
DDINLSETEC PHVVLQIDDL ENLLNTSNTV TIRYSPRQYS KDGHAYRIAA ILRKPSVGMF
VQLLSGDFDN ELQWPCLQRQ MIFQLLDQTP NKKLQMSKEL AFLSVETQVT SSGILAWNNP
RDNGTKVLYE NNEYIYGGPL WGYSRFATLE ELRSREFLKG GSAIFMFNFE DLTPLINGTT
LPCPQLRPIK TRNPTKNVDE GPCLPRILST AHPPATTDNK ISSTVHPATT TDNRNSSTII
PPPPATTDNR YSLI
//
