ID A0A0C2IDG7_THEKT Unreviewed; 642 AA.
AC A0A0C2IDG7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 10 {ECO:0000313|EMBL:KII63383.1};
GN ORFNames=RF11_02191 {ECO:0000313|EMBL:KII63383.1};
OS Thelohanellus kitauei (Myxosporean).
OC Eukaryota; Metazoa; Cnidaria; Myxozoa; Myxosporea; Bivalvulida;
OC Platysporina; Myxobolidae; Thelohanellus.
OX NCBI_TaxID=669202 {ECO:0000313|EMBL:KII63383.1, ECO:0000313|Proteomes:UP000031668};
RN [1] {ECO:0000313|EMBL:KII63383.1, ECO:0000313|Proteomes:UP000031668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuqing {ECO:0000313|EMBL:KII63383.1};
RX PubMed=25381665; DOI=10.1093/gbe/evu247;
RA Yang Y., Xiong J., Zhou Z., Huo F., Miao W., Ran C., Liu Y., Zhang J.,
RA Feng J., Wang M., Wang M., Wang L., Yao B.;
RT "The genome of the myxosporean Thelohanellus kitauei shows adaptations to
RT nutrient acquisition within its fish host.";
RL Genome Biol. Evol. 6:3182-3198(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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:KII63383.1}.
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DR EMBL; JWZT01004669; KII63383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2IDG7; -.
DR EnsemblMetazoa; KII63383; KII63383; RF11_02191.
DR Proteomes; UP000031668; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR PANTHER; PTHR45702:SF2; KUZBANIAN, ISOFORM A; 1.
DR Pfam; PF13574; Reprolysin_2; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 4: Predicted;
KW Integrin {ECO:0000313|EMBL:KII63383.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000031668};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 595..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..384
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 386..473
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 642 AA; 72758 MW; 0F091BDFAF43AE65 CRC64;
MKMIHSESNQ VSEDPGRQFN MLPVYKPEST YPFFLILSNK SYDFSHKDNF YTDELAKNTN
LEINKLKDGM HGKNKSNKSM AIDDIFDDCI SLQNAKNFNV ERSTQFSRGH HICPNCTTYK
SSIDDFTNTI DKGEIMGKNS TKFTEYKSEK AEIVSASGHF KKDEIQSPRT NPKYCELDLW
LHEDYVKHHR SQALALVQLS KAIQLLNNLL KTHFKNKDGE PMLQYHIKRV RVFGSGHTLD
KVKKSPITLL ETINDISQRT DTCATGVYVS EDWDGILGLA KLGSRKSGLC NKKSGYVVTS
IFRNWRVSAR VHRTTTIHEL GHHLGAQHDP EDSHANCSSY LGYVMSAIST QADRPINFMF
SPCSLEDMEK LMYLPNRRTC LKESISGLCG NGIIEIGEEC DSGFTDDPCC GKPHDADACK
LRGECSPSQG SCCNRHCKFR PNKFICTKKT DCSESSHCMG NSSICPPPIS INENRFCFNK
RAVCYQGTCT KSVCEKLKKV KCDCDGENSC RICCKKSNSS TEKCQPVYFQ HEKTFKNLPP
GFGCENKKMI GVCQTDGKCH IILTVSPIIN ALQSLISGPY RENLKNQIFD YLESFVWVFG
LVISLFSIIS RLLYVDKQKI YKAELSYAYL GFLDRCNDLW SY
//
