ID A0A095AJA5_SCHHA Unreviewed; 683 AA.
AC A0A095AJA5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Thimet oligopeptidase {ECO:0000313|EMBL:KGB34131.1};
GN ORFNames=MS3_02331 {ECO:0000313|EMBL:KGB34131.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB34131.1};
RN [1] {ECO:0000313|EMBL:KGB34131.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; KL250590; KGB34131.1; -; Genomic_DNA.
DR RefSeq; XP_012793900.1; XM_012938446.1.
DR AlphaFoldDB; A0A095AJA5; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 209..676
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 683 AA; 78433 MW; A39B3FCFB7D4E357 CRC64;
MFVTPGCFLK WSATVDDIVE RTSTLISHAV SVYDKVGSSE PASFKSVVLL MSLFEAGYQT
EKNAIDFLQH ISACKAIRDA SYDATRRLSD VKVELEMRKD VFEKFVSVQK NIDSSFPDEY
RRYVDRKVQL GRRNGLHLDD DKRKLIEALN KEENQLCIDF QRALNEENTL LEFTDEELTG
CPADFIDGLK KLPSGKREVS LKYPHYFPIM QKASNPETRR TLETAFNSRC VKENSPILKR
LMELRKERAT VLGFSTHADF MLDLYTTKTS ANISEFLNNL GNKLEKLRLK EITRLLELKK
EECDRLGYTF NNCLNPWDTR YYMNMVKERD YSVDEVALKK YFPLATVKSG ILRLYQQLLG
LRFERVSNAE VWHEEVEMYS VSDSQSDSLL GYFYLDLHPR EGKYGHAAVF GLQPGCRRLM
NSNNITVDEH SHSPSLVTSE RQLDISAMVT NFTAPDKETD QCFLFHHEVV TFFHEFGHLM
HHVCSHTETA LFSGTAVETD FVECPSQMLE NWVWNVDGLK ALLGTNDDPI PKDLLASLIN
SRIANAGLFY SRQILLASFD QAIHTTNWED DPLVTFTNLS KKWLGIQPIP DTFWPASFVH
LTCGYDARFY SYLLSRVYST DMFESRFQCA MDSGCLSKSV GRDYREKILR PGGSKDAADM
LKDFLGREPN DDAFFKLLNV NLP
//
