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Database: UniProt
Entry: A0A195DCU8_9HYME
LinkDB: A0A195DCU8_9HYME
Original site: A0A195DCU8_9HYME 
ID   A0A195DCU8_9HYME        Unreviewed;      1775 AA.
AC   A0A195DCU8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Chitin-binding type-2 domain-containing protein {ECO:0000259|PROSITE:PS50940};
GN   ORFNames=ALC57_17310 {ECO:0000313|EMBL:KYN10703.1};
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:KYN10703.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN10703.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN10703.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN10703.1};
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; KQ980989; KYN10703.1; -; Genomic_DNA.
DR   RefSeq; XP_018375034.1; XM_018519532.1.
DR   STRING; 471704.A0A195DCU8; -.
DR   GeneID; 108768877; -.
DR   OrthoDB; 3062189at2759; -.
DR   Proteomes; UP000078492; 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:SF31; FI18007P1; 1.
DR   PANTHER; PTHR22933; UNCHARACTERIZED; 1.
DR   Pfam; PF01607; CBM_14; 1.
DR   SMART; SM00494; ChtBD2; 2.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 2.
DR   PROSITE; PS50940; CHIT_BIND_II; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1775
FT                   /note="Chitin-binding type-2 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008270385"
FT   DOMAIN          43..106
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          1708..1772
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   REGION          134..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..1254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1275..1312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1330..1368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1500..1566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..259
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..792
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..819
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..835
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..865
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..980
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..1007
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1019..1036
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1081..1113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1128..1144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1170..1184
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1185..1254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1330..1357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1520..1566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1775 AA;  197228 MW;  3F3B0D6E662B7BEF CRC64;
     MNLALHGFLL QIFVSILDFR HGRLLCSAGE PGYLDFDNLP ETNFSCQGKV IGGYYADVEA
     GCQMFHVCTI GQKDEIMDIK FLCLNGTVFD QETRVCERVD EVDCSKSERF YNLNLELYGN
     NAVTLSLNGD DEDDLTIDPV EDHQSRTTSA RPSTTSTTST TTSRPSKSST TSASGSFQHP
     AGYPQHYQPQ PPFPQVHTSQ SKSLYDDKNG GYHHQYIFHN GGERASNQAT SYQLFSNQGA
     VSSTTVPPAP PPPPPPQIHQ IRYSSTVGPP PQIIHSEPST VTPLFATSST IQTLLNANSP
     AGLINPIFHN HGIASTTEHF SVHSNNPRET TDYRDDDQEQ DIRALEAIQS VNKGKISKLT
     ISPVPSQQES SRTVQTKTSQ TSQQRISGNF LPTPATIETT MRSFYPTPRP SPKPPQSLQS
     VTHQVTQHIH VPQLKPHQIT INLPPPDIQR IVQNPSPLLP SQSRVIVTAK ASVSDESGRP
     LNTTQLVTLP LPTIPASYDD YKEGDESFDP FYRDVPKIRK NRQNAMENIR FLRAKRSLEQ
     PYNFVYEVNS HQDFKVIRKS EPRKNEDNAI NKESTHVQVN LEDFRSLKES LIKFRDILFS
     DNVNEDSSHS DAEENRNNTE RIGINSKTFD TISVKQVQDN AIKKVDYLED LKTEASKHFN
     LNKNTDEEEE DEKASHEDST PNVKIKSEKS LDEKKHIKDT SELEIYIEST TAHSRKNESQ
     GDVIDLIILD SNNNSKVKAT SAKTDAPIEI IIEETKSDTY NASKIDGKVA HEGQIAGSLI
     KDDPEKRSNS VAGERRQLTI PHKTIKRNGA KDGERKSGPR RKSSRPRSSK RRISSRIRQQ
     RMENIEPTET IQQKERTTTA TTVIDTTTVT STSTTTTTST TTVTPSITAF EKKVAEQIDS
     NIFGDSESQT FKELDTRAIG HRDAIYSKSL QDGKSYDSSR SKDIERSFDR QIVEEHTRSS
     ELRADQIEEE KRETELPDYT QTTEGKDTTE NPSNANEARS TEVAQVSEEK SSIEEEDSYR
     EYEFPDDDEA DTNEGELEEN SQDRSSKISS DEVATSREGN LEEESAYDED ASEKSSTEIS
     DEEQSSTANY NEDVNSEELN EYQDITESSA ESTRSIQEDY REYPESTEGS TMDYTNPEEY
     TDSQEDIAAS TEDGEDSTEG VLKFTDELPL SDDNEDEETT EESLTSNEND AHDYVDDNYE
     PENYKTEIAT KLDEFEEDKS EEKNDGEKKD TSAKDPDRTK NIEKSDDSIE VEMQTDHVAG
     VTKIKDLEEI ASLTTTSSTT TPTLTTTTSS TTASTTTTSS TMASSTTTSS TTASSTTASI
     MVTSTTTDST ITASSSTPIT TTTARSTTIT RRPKTTTPRA TPPKIFKPTG NKRIYAYIPP
     TTTPNPVVIK PRLSLYNPKP AKPIKSYNEL APKPTIRKLI LPTRTSTTTT TEGVTITTTE
     ILNTENPEIT TEPVTITTAA STAAVSTTAP LTTAATMATA MTTAATTTAA TTTAAMTTMA
     ATTTTTESSR SEENGLESKL ETNEYISLDS LAKNNQTNKD DQLPSSSEQN TSANSSENTD
     PGMTTMKIET FTPYPLFKLS TLAPSIERTT KEIEVIPQET TEDIDTLVPT TIPPTTLLFE
     KSEYAEIAPS TEKYLEITET TIASTSKVYQ QETSLVSSVP PVPERATSVS VLTTVLPKAE
     DSDPGASMEA AILKSSSRKL VKPRKHASFN CLEKEMYRFY GDFRDCRLFH YCSPGFTSRQ
     VLDFRFVCEE GTAFDEVTQS CRHEVRNRKC RNRSW
//
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