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Database: UniProt
Entry: A0A182SDI9_9DIPT
LinkDB: A0A182SDI9_9DIPT
Original site: A0A182SDI9_9DIPT 
ID   A0A182SDI9_9DIPT        Unreviewed;       528 AA.
AC   A0A182SDI9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:AMAM004612-PA};
OS   Anopheles maculatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; Anopheles maculatus group.
OX   NCBI_TaxID=74869 {ECO:0000313|EnsemblMetazoa:AMAM004612-PA, ECO:0000313|Proteomes:UP000075901};
RN   [1] {ECO:0000313|Proteomes:UP000075901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=maculatus3 {ECO:0000313|Proteomes:UP000075901};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles maculatus species B.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMAM004612-PA}
RP   IDENTIFICATION.
RC   STRAIN=maculatus3 {ECO:0000313|EnsemblMetazoa:AMAM004612-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; A0A182SDI9; -.
DR   EnsemblMetazoa; AMAM004612-RA; AMAM004612-PA; AMAM004612.
DR   VEuPathDB; VectorBase:AMAM004612; -.
DR   OrthoDB; 5474074at2759; -.
DR   Proteomes; UP000075901; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProt.
DR   CDD; cd00033; CCP; 3.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 4.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR19325:SF502; BETA-2-GLYCOPROTEIN 1; 1.
DR   PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00084; Sushi; 3.
DR   SMART; SM00032; CCP; 4.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50923; SUSHI; 4.
PE   4: Predicted;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00302};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT   DOMAIN          1..85
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          86..198
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          197..258
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          259..319
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          320..380
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          381..439
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          439..477
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        86..113
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT   DISULFID        199..242
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        322..365
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        351..378
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   528 AA;  57074 MW;  4699CE826D054417 CRC64;
     LYVISARKGY TVSLDVQELD LNADSDFLLI RDGESAHDKP IAKLTGTIES KPSRVIISTG
     NKLYLYFSTS LAQPAKGFSI RYVEGCTAVV NAANGTVTSP AYNLSPYPNN QECYFVIKNP
     SGKPLSMRFV DFDVHRSDLV QVFDGPSTSG VRLHAGNGFT DSNAPKITLT ASSGKMLLKF
     ITDALYNGKG WSAEFSADCP ELKPGIGAIA SSRDTAFGTV INFTCPVGQE FATGKNRITT
     VCQNGGNWSI SYIPDCQEVY CGPVPQIDNG FSFKTTNVTY RGIATYQCYA GFAFGSGLAT
     ETISCLADGT WERQPACMAS QCPPLPEVAH ANVTVLNGGG RSYGTIISYE CIPGYVRTGR
     PILICMSNGQ WSSPVPSCSR KQCYKIPEVQ NGYVVDKTRE YYYGDEARVQ CYKGYRLIGS
     HTVKCNEQQD FSNVPVCEDI DECQTSQCDA SSTECMNAAG SFHCKCKTGY TSSMECRPVV
     DLGLSNGGIS DDSVTVSSTA SGYEKGVSTQ LSFLSLSSLC CELLTWPF
//
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