ID   A0A1I8PHV6_STOCA        Unreviewed;      1239 AA.
AC   A0A1I8PHV6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Chitin-binding type-2 domain-containing protein {ECO:0000259|PROSITE:PS50940};
GN   Name=106092742 {ECO:0000313|EnsemblMetazoa:SCAU008228-PB};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU008228-PB, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU008228-PB}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU008228-PB};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   RefSeq; XP_013115115.1; XM_013259661.1.
DR   AlphaFoldDB; A0A1I8PHV6; -.
DR   STRING; 35570.A0A1I8PHV6; -.
DR   EnsemblMetazoa; SCAU008228-RB; SCAU008228-PB; SCAU008228.
DR   KEGG; scac:106092742; -.
DR   VEuPathDB; VectorBase:SCAU008228; -.
DR   OrthoDB; 3204540at2759; -.
DR   Proteomes; UP000095300; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   PANTHER; PTHR22933:SF18; CHITIN-BINDING TYPE-2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22933; UNCHARACTERIZED; 1.
DR   Pfam; PF01607; CBM_14; 1.
DR   SMART; SM00494; ChtBD2; 1.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 1.
PE   4: Predicted;
FT   DOMAIN          927..986
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   REGION          93..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1142..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1066
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1097
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1239 AA;  138893 MW;  12801D280A9383D6 CRC64;
     MSVIQPQNKS SYVGDNVTLM LAEDSELSAS ERTRRLIPYM AFYVPIQELP INQQYTSVQT
     PKHVARPSAT GSSGSHSIQL PPQYVHLKST AVSGVGSGTE SGPTSYLQSS PAAPHYQASA
     GDAYHTLTRG GTQQIQPQYQ LPPTPIKHHS DNSGSNKYPD RHLLSHGLPG PSAPNTANLA
     GVKLNPIRHK TVQHFPPLTS QSAATSQLST SAYEAPSSTS SEKYQHHGIA YRPRTKQSKI
     NLTPFTPANS VPGNFVPIVY TPVNSNNNNY NNIVLTSQGA ASVDTINSYN VPTNTFNGGA
     KQQQIAIEYS HPLVQSITET PLQSYRPPQQ PHHQVHHDIP KQQDQQYLSV TSPASQQTGS
     ETGTSGGSTH QQNTQTTGAV GTYTQQIEEL QLQHQNRPKQ LQKFTLIRSK QQQADQPYGT
     KFTHFTPSKI ENLFDFEQHQ EQDGQVEQPT RYNDKQQYYP YHQQQKEQQH TVFLTKPKYR
     ESVHQQPTHI IVLSPTAATN DALSQAHSGK YALASGPIRQ PSYTRPEQSS VSSPGQQEIQ
     NIEASSTPVQ SNSQLPFEEQ ILTIPVHNLF SDLRNYQHIH YAPSSPSQPL VSSLNYNKIG
     GQSAQQYSDV SVNDPKQALD DEQNETYKKN IQQQRKQTLR PPPQAFIEVM TTAAPFHQPI
     IQENYVSTSR PLHKPKHNAG SQTPKEEKNP NYPTIRQPNP MARPLVTVTS TPHTMIMDSA
     PKYVYVEEEF GQKLSAGSIK LKPVDKYGHN KQTGTKQLHN LQHLAQRPPT AVDEPADVAA
     TLQQHQQHTP PPETSHHILA DPNELPDIRT SSLAEILHKL QESNHLPHTL TPDNIDNSIK
     TLIRILNNLK QTQTIVPYPS QYYEKSPPFS PEYDYTSGGD VVEQSLHKVQ DANLIPPSVP
     GPNKHPGPST GRPGIDYPNY SEIPQTSFDC SEQRYKGFFG DPETNCQVWH YCDLNGGKAS
     FLCPNGTIFS QIALTCDWWF NVKCATTAQL YVLNERLYKY ILPFTPKFPE DYSGPLVDKY
     LAMKFHEMEE KMRLERKQAL ENQQENEQNH ELPLEDTKEE TRLEDTTKST MPIQKPVESS
     MQKHDSINSQ VSEQSSERNL LIDDEVDDIS HRGSMDTFEV TTLETDTTKD LPFSLKPIIV
     SSTAGPAGCD EEEQQQHQQH DDAKRRTDQE LETNKTEANN KPQKEIIAKI FEKHISPSIA
     NTKTDLMKIT VEKVDVIEIK PDGNTDHLIR KMIQNNDNK
//