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Database: UniProt
Entry: A0A151J6G7_9HYME
LinkDB: A0A151J6G7_9HYME
Original site: A0A151J6G7_9HYME 
ID   A0A151J6G7_9HYME        Unreviewed;      1530 AA.
AC   A0A151J6G7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Collagen alpha-2(IV) chain {ECO:0000313|EMBL:KYN18809.1};
DE   Flags: Fragment;
GN   ORFNames=ALC57_08885 {ECO:0000313|EMBL:KYN18809.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN18809.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN18809.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN18809.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN18809.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ979854; KYN18809.1; -; Genomic_DNA.
DR   STRING; 471704.A0A151J6G7; -.
DR   Proteomes; UP000078492; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 7.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR37456:SF3; COLLAGEN ALPHA-1(XXV) CHAIN; 1.
DR   PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR   Pfam; PF01607; CBM_14; 6.
DR   Pfam; PF01391; Collagen; 4.
DR   SMART; SM00494; ChtBD2; 7.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 6.
DR   PROSITE; PS50940; CHIT_BIND_II; 7.
PE   4: Predicted;
KW   Collagen {ECO:0000313|EMBL:KYN18809.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078492}.
FT   DOMAIN          15..79
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          160..222
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          701..761
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          909..968
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          1097..1159
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          1355..1415
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          1439..1500
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   REGION          71..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          968..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1159..1348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..256
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..387
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..506
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..621
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..687
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KYN18809.1"
SQ   SEQUENCE   1530 AA;  156482 MW;  5CF1D88E247FEDF2 CRC64;
     YYEYNRDQYR QSNAPFKCTE EGYHPDPRDC RVYYRCVDWG NGSPLTTFKF ECGVGTVFSK
     DKGDVCTYPE DSGRPECGSS ENELDSNVQD PPSPTWTTTI RTTMWSQSTM IQSPITKPST
     ITTEAATTIK KPETTILPPL TNRPPIDEPE DNVVNCQNGY QKCIQEGFLA DTCDCRKFYR
     CVNEGYGKFT KYEFKCGVGT VWDPEIQACN HAWAVTRKDC KQNLESSPGS PGSPGYPGTP
     GSPGSPGYPG TSPGSPGTPG SPGSSGSPGY PGTSGSPGSP GYPGTPGSPG TPGSPGSPGS
     PGYPGTPGSP GSPGYPGTPG SPGTPGSPAS PGSPGYPGTP SSPGSPGYPG TSPGSPGTPG
     SPGSPGSPGY PGTPGSPGSP GYPGSPGTPG SPGSSGSPGY PGTPGSPGSP GYPGTSPGSS
     GTPGSPGSPG TPGYPGTPGS PGSPGSPGSP GTPGYPGTPS FPGTPGYPGT PGSPGSPGYP
     GISPGSPGTP GSPGSPGTPG SPGTPGSPGT PGSSGSPGSP GYPGTPGSPG TPGSPASPGT
     PGSPGSPGYP GTPGSPGSPG SPGSPGSPGT PGSPGSPGYP GTSPGSPGTP GSPGTPGSPG
     SPGYPGTPGS PGSPGSPGTP GSPGTPGSTG SPGSPGYPGT PGSPGSSGYP GRPGSPGTPG
     SPGSPGTPGY PGTPGSPSSP NIPGSPGNPD SPNSSVNQPS TGICTVEGFF SDPQDCRKFY
     RCVDNGMSSF IKYDFQCGAG TVWDSSIQSC NHAYAVPHCN KANGAITDKP DTSLNEINST
     IGPDTSKLPS QSSESSTFPS TKPDIQSSAQ PDSTTGNSIA PSQTTSTSYL PPSSTYSSST
     MQVTESVSYV PPASQMTTTS VSYLPPSTTT NGISESTPES VSYLPPDTSS TTTLPSSASS
     AASSPQNEKY KCTKEGFFPD PDNCKKFYRC VQDQSGYQKY EFECSPGTAW DQLIQTCNYI
     DKVASCSSGS NEIDQGLGSS TPTSELPAMS SSTTVSSQTI ATTSPIPIST ESTTTVSTSS
     ETSDKTESSS TTSTITSVSS SENPASEKPE EVQMPGSSTE ISSESSSEST SESNEGSSSS
     TSESHAPDCA TQKPSNAIVC NNEGFYPHPT RCDKFYRCVN NGNGFNVYHF DCPPGTIFDS
     SISVCNYPES VYPAKDCTTG NTSTSVESTT QSGTPEQSTS EATATVAAHG TTQQTEESTI
     TTTELGTSTS EESASTSTES TTSNSLPESS ESMIESTTES TTATTETAID SSTSEQSSEA
     TTEAAPSTES GMSTTESQEQ STESQEQSTT EESQEQSTTE SKEPSTTETQ EQSTTELQEQ
     STIESQEQTT ESSESTTAEQ GAPCSIGNLT DDQITLVCPS GFRRHPKHCN LFYQCTSEGN
     MEIKILVLSC PENTIFDEKK IQCLSESESS QPCMGTKTSA RFYRRLEDHA LSPVKVSSNQ
     LCPQEGHFPY RQGCSNTFYK CKRDVRNSLQ GYLYKCPENF VYWSVSRRCE RVTRLPMCSH
     LSYRDKIDWN DRWQIPTEDF NLSARMLHFS
//
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