ID A0A2J7PUQ8_9NEOP Unreviewed; 549 AA.
AC A0A2J7PUQ8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=Chitin-binding type-2 domain-containing protein {ECO:0000259|PROSITE:PS50940};
GN ORFNames=B7P43_G05267 {ECO:0000313|EMBL:PNF20067.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF20067.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF20067.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF20067.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNF20067.1}.
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DR EMBL; NEVH01021193; PNF20067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7PUQ8; -.
DR Proteomes; UP000235965; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10974; CE4_CDA_like_1; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR45985; -; 1.
DR PANTHER; PTHR45985:SF6; FI03450P; 1.
DR Pfam; PF01607; CBM_14; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Reference proteome {ECO:0000313|Proteomes:UP000235965};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..549
FT /note="Chitin-binding type-2 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014456165"
FT DOMAIN 52..114
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DISULFID 132..144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 139..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 151..166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 549 AA; 62395 MW; 9EE22F28504BCA40 CRC64;
MARCTRVALS LLCASACLHI VTGSTSQGVL NQFVKRVKRQ EETNKKEESF ETELCKDKDA
GEWFRLVAGE GDNCRDVIQC TSSGLQAIRC PAGLYFDIEK QTCDWKDAVK NCKLKNKERK
VKPLLYTDEP LCTEGSLACG DGNCVERGLF CNGEKDCADG SDENTCDNDN DPNRAPPCDP
AVCVLPDCFC SEDGTAIPGD LPAKDVPQMI TITFDDAINN NNIQLYKDIF NGNRKNPNGC
DIKATFFVSH KYTNYSAVQE THRKGHEIAV HSITHNDDEQ FWSNATVDDW AKEMAGTRII
IEKFANLTDN SVVGVRAPYL RVGGNNQFTM MEEQAFLYDS TITAPLSNPP LWPYTMYFRM
PHRCHGNLQH CPTRSHAVWE MVMNELDRRE DPQFDEYLPG CAMVDSCSNI LTGDQFYNFL
NHNFDRHYEK NRAPLGLYFH AAWLKNNPEF LDAFLYWVDE ILSNHNDVYF VTMTQVIQWI
QNPRTISEVK NFEPWREKCT VDGKPACWVP HSCKLTSKEL PGETINLQTC VRCPNNYPWV
NDPTGDGFF
//