ID A0A369S0B1_9METZ Unreviewed; 1415 AA.
AC A0A369S0B1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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};
GN ORFNames=TrispH2_007437 {ECO:0000313|EMBL:RDD40356.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD40356.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD40356.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD40356.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD40356.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDD40356.1}.
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DR EMBL; NOWV01000104; RDD40356.1; -; Genomic_DNA.
DR STRING; 287889.A0A369S0B1; -.
DR Proteomes; UP000253843; Unassembled WGS sequence.
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; cd05382; CAP_GAPR1-like; 1.
DR CDD; cd00041; CUB; 5.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.33.10; CAP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR014044; CAP_domain.
DR InterPro; IPR035940; CAP_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR034113; SCP_GAPR1-like.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR24251:SF37; CUB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00188; CAP; 1.
DR Pfam; PF00431; CUB; 5.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00090; TSP_1; 2.
DR PRINTS; PR00480; ASTACIN.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00042; CUB; 5.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00198; SCP; 1.
DR SMART; SM00209; TSP1; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF55797; PR-1-like; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 5.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 5.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50092; TSP1; 2.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000253843};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 26..1415
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5016484582"
FT DOMAIN 233..429
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 533..650
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 720..833
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 833..870
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 878..992
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1009..1121
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1146..1260
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 860..869
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1415 AA; 159142 MW; CC31414E6DF9B46F CRC64;
MMPLRYHFAG PTLFVILLVS GQISSNIIGD RDGEFHSLKL SRSKKVVHQS SPIQKFTKSE
GSNAEIGLSE LIKKLESESG LEKLLLKHEN YRALDADKLV RRENTAAKDS KRGKEEHDES
LMKLLSQKKL VKSEDKTELV EEIKSELMIE SLSKKGVKNL AKQTSVQQKS VKEINQKVNR
NSQGSLAAKQ ETYDNHKEKE PELFEGDIIL TPTVQHIVNA DPLKENKNSR SLRSMIQDVT
GLWNKRIIPY TIAKTVDDPT KLNLIQAILD IEAKSCLRFK PLEREEDYVL FQGSFSCYSH
IGRIGGRQIL GVGSDGSCKR GNLMHELLHV IGFWHEQSRL DRDSYIRVNY QNIRKGQEVN
FEKYTRGEVD SLNKPYDYGS IMHYELYAFS KNGHKTMEPL RDPGFVKIGQ RNGLSSGDVD
KVKTLYACNV NDTQGWSDWQ YYKACDFKCR KVIYRFCLNI SGCSNEPWYK TVNCSYSECP
DMDGVWSSWE NWSSCSRSCG KGGRRIRRRT CSNPPRQRNG KDCQGEELQS EECGATIPCV
GSTVTIHSPI DPITKKYYRS IDWLETLEVP RGYKIKIDFQ SIDIEKYDTE CSADYLNIYD
GASTRSKLIG SYCGNQIPDS IITSHNTALL HFSTDDSIER LGFKLVYRPI DMNDGQWSKW
SRWTKCSASC GFGVRQRSRS CTSPPPSNGG KECAGSSLQN KRCFLSLCIQ KANTKSGSSC
DTTFLTPTGI ISSQNYPSNY PNNNDCSYTI LVDPNSVVKL NWKHFDLEYE PNCPYDSLTI
FDKNSNGTTI TFPPLCGTAL PSFQYSMSNQ VIVSFLSDTS VTAKGFELHY STVSPPCNSN
PCQNGGTCEY NYTTGYTCHC IPNFSGINCE TLTTASYCNR IFTSISGAIA SKNYPSNYDN
LLDCNMTIQL PSNYKINLTW QDFAIEDDYQ CGFDSLTIYD VVGHSNQTKL GRFCERTPPP
NAIASTENTL ILQFHTDESE TRKGFLANYV GVPVTSDPTL VPTASSAICG TNIHQTSGEI
KSPGYPLKYS TFSFCVFKIF TSSNQRLKIN WIDFELEPSN GCMYDFVSIY DDSHMSAARL
LKACGKKFPP SILSSRSVLT FEFTTDGDTE MKGFHFRYEI TDIFNFPGIY FWFVLSRVTA
VSVDICNADY NSSAGIIMSP NYPGLYPLNI DCQYLIRAPA NHVITLVWNF MEIQASTTSN
CSKDWINVYD GETAQSLLLK SLCDTYIPSS ITSSSNRLLI VFHSDNYNQG RGFNASYYTT
DTIASAPINL LPYQQDCLNE HNRLRRIHGV PDLQWLTPLQ ISAEIWANQL IATGSMYPSD
TVHGENLYHG DFANPSTANV TQMVGIWYSE VANYDFSSPS FISAAKHFTQ LIWKSTTHIG
CGRSIIGNNV YLVAHYSPRG NFVGLFGQNV LPATS
//
