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Database: UniProt
Entry: A0A183QD99_9TREM
LinkDB: A0A183QD99_9TREM
Original site: A0A183QD99_9TREM 
ID   A0A183QD99_9TREM        Unreviewed;      1481 AA.
AC   A0A183QD99;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Hemicentin-1 {ECO:0008006|Google:ProtNLM};
OS   Schistosoma rodhaini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000160301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SROB_0000160301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) 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   STRING; 6188.A0A183QD99; -.
DR   WBParaSite; SROB_0000160301-mRNA-1; SROB_0000160301-mRNA-1; SROB_0000160301.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 5.
DR   Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 6.
DR   InterPro; IPR026823; cEGF.
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; IPR006605; G2_nidogen/fibulin_G2F.
DR   InterPro; IPR009017; GFP.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR22906:SF43; COMPLEMENT FACTOR PROPERDIN-RELATED; 1.
DR   PANTHER; PTHR22906; PROPERDIN; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF07645; EGF_CA; 4.
DR   Pfam; PF07474; G2F; 1.
DR   Pfam; PF13927; Ig_3; 3.
DR   Pfam; PF00090; TSP_1; 5.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 5.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00209; TSP1; 6.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF54511; GFP-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 6.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS50993; NIDOGEN_G2; 1.
DR   PROSITE; PS50092; TSP1; 6.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          36..124
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          129..213
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          278..358
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          742..989
FT                   /note="Nidogen G2 beta-barrel"
FT                   /evidence="ECO:0000259|PROSITE:PS50993"
FT   DOMAIN          1126..1166
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1187..1225
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
SQ   SEQUENCE   1481 AA;  164296 MW;  1E707C04C1DC6EA4 CRC64;
     MIWLFVMPED EGELTCIAKN TAGEDRITFR VSVQVPPRVS LPISTIGYEG KSVTMNCEAD
     GRPKPEIIWE FKGQPMTSHL GDRVRFETPT KVTIHDLIPS DGGTYSCIAR XXXXEMAMDS
     TFLTIFTKPE FERTPNQTTE AYEARWIQFR CIANGHPKPE IRWMHNGNII PSNPSKNGVG
     SLVLGPLRTD QAGQYTCVAK NDAGNVEYDF ELKVKTRPKV HVYQSDEPPR ESDTTRLRCE
     VSGDADSVAK DTGTYQCIAA NPVGEDLGEL RLVVESKPYL VNHPNNMTAQ IGSVVVMECL
     AEGQPKPTIT WYKDKQQIIL HGHRSLVNNG SLRIVGVSSD DDGLYHCVAS SSLGEDFSPP
     AFLQVQLDGR WSDWSQWSEC SQTCGHGTQS RTRTCTNPAP KYGGAHCTEE NTEIRPCLVK
     FCPTDGEWGS WTPWSACTAT CGVGLSQRRR RCDSPPPSNG GRPCVGEAVE DVMCEGLPPC
     PVSGSWSPWS PWSDCSSTCG TGGTQNRKRT CDNPTPSNGG KSCPGQDLMV RACNRGPCPI
     NGGWGTWSPW SHCSHSCGGG QRRRTRICDN PVPAYGGEDC PPTGSTETSE CQSEPCPIHG
     DWSNWSSWSA CSRTCGVGLQ TRERECTQPQ PQFGGRLCRG SAKEIRTCET QKRGSSQFCP
     NNEPGLISAW SEWSSWSECE PDCSLVGQVT EKSGIKRRER TCTVLSPENE STHGCPGPAE
     EIQDCTLEYK LDKCQDTLRS VNKGLLTGTI RGQLNNQDIG TIYLNANWST SASNLSTNYE
     FHLTNVPIER SQCLQALTEI YLPGIWYAAK EVSGASNGHT IMGSLNGITW ESIGQFADGN
     TIQMSQRVLR SNDSIVSPSS ESIVHLTTDI YLSGSCTLSL IDSKTTTTSP EVELHDFHEN
     LVQLSPQKGS LHSHSSRAFT VYNLEREKSQ MEPYSWISTI QISPERRQTY LTQELHVNGI
     ENKANLQTGQ IEFQAESIMK KPIGPDVCPS GFELNQARIT GTNIRLQRRR DYCKDVDECA
     FPNLNKCDHV CKNTVPYYTC ACHKGYRLSV DGHSCIDIDE CAIGGNNETI CSYGQRYIDE
     CLSGAYQCGE NERCVNIPGS FRCQPACPQG YRAIGTPESN IIECVDIDEC AIGISQCPIG
     SKCINEPGTY SCRCLNGHEA GTQGCDNRRD LLCNEGFQWN REKGCIDIDE CNPSFGSSPC
     QYNCVNTYGA YRCECPIGYE IDRKTNLCRD IDECNLSNPC RSDEVCLNLP GNYTCVQQRC
     PKNYVYDKKS RSCRIRCIDS KLNCPYGAMF ADTVEYLVVQ QSNCYYQLLD KAPNTPVQHR
     TEDGVVYLTP NWARNNNNNT NQTRERTLLS AHIEAATNPT YQQIKYDEPG QLYYLFFRVS
     CYENDSSTSS SSSSSASSSS LSTMESLQTT ISSGHKSTVM TSVPSSSITS SMINNEYSID
     NQAWSNNTSW DMNSHNQTNK KYKLVFQHSF YVYISISKYP F
//
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