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Database: UniProt
Entry: A0A163JA50_ABSGL
LinkDB: A0A163JA50_ABSGL
Original site: A0A163JA50_ABSGL 
ID   A0A163JA50_ABSGL        Unreviewed;      1128 AA.
AC   A0A163JA50;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   Name=ABSGL_03520.1 scaffold 4609 {ECO:0000313|EMBL:SAL97993.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL97993.1};
RN   [1] {ECO:0000313|EMBL:SAL97993.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL97993.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC         D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC         UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223; EC=2.4.1.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00000319};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; LT552047; SAL97993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163JA50; -.
DR   STRING; 4829.A0A163JA50; -.
DR   InParanoid; A0A163JA50; -.
DR   OMA; GANARDC; -.
DR   OrthoDB; 1515176at2759; -.
DR   Proteomes; UP000078561; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF26; CHITIN SYNTHASE 7; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        554..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        787..814
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          250..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..315
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..377
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1128 AA;  126010 MW;  23C348FC4670E10D CRC64;
     MNAVLEELDR RNGKPIGIIN FCSYRKTIVG VLVIRDTVCH VILGGYCLAP KRFVCELNTG
     GLHERQPSGN NPGILDNWWD LAADYTHHPL MARSISTVDA SYNKHRRLTT TLDPLAVETP
     TAERNQIELG ERHADDILAN RMTVDEDAQK RVAVVKGKCD CGWTCHYQGL LWRFWTTKMN
     KDRCNSCLTS NGEWNSRLTT TPKNSESNLF LSGATFHVAG FEISRPSSMA HPQRSSGYAP
     ALRGYSTDPR VMQQHRQSSQ SPPQRSSMHP PQQRPPPGSY NMENMGRPRP PPHRQSTHHP
     LPQPPGQPRH STMQPQPPPH HHQQQQSRNI DGRQSRDYIY QQQQQQQQQY RPPPPRMMNR
     PGPRPVGGPP PSSANYHSQP PQPGEGGAYR RNTVARTRSL SRPERQRPKQ GMFRTPSQQR
     RMMIGSGRPG PAGATMMHHY QRPRMNPNQP MSNRLQQQLQ QQKLQQQHEA LLSQSPPGGG
     GRPPPRSGGA PMDPRQQKKL QQQMEEEEKP DVLTNWWSWL AFLATCCIPN WFIRVCLRKP
     NPLTQQAWRE KLTLCYIILL LCGALAFVTY GLTVTLCPNH ETNLAYSAMV QGQRKPMWRS
     DVRVLGRVYD LDDMKRFFGS KGLNFTNDYE NMDISSIFNG DTTGACTAFD TQTPSSLGDC
     TLYSPYGGSI KQSDGQCFSV NELKQYNSKG YLAFDWVDLR PNGVDSLGDT DLVVLGDSVL
     NLTNYLNGNN DFFGAKVKTA LDSSRGNDAS YSLLFTPEGK NARRCILDRY SVGIMEVDTG
     GCIASQMIMT IMLVVIIAMI VVRYSMALLF QWVIASKLVK PGGRSNWLAW RSIKGGNDDP
     ANHVPGPYNN YGPMNTYSGG NGGSSASIGS GFSSRGTPVS EQSSATDLGG RGIQTDIVST
     ELYACMLVTC YSEGEEGLRI TMDSLARTTY SKKHKIFFVI CDGLITGAGE SKSTPDIVVD
     MMDLDPTMKN PTPSSYLAIA DGEKQLNMAK VYAGHYRGVP CITIVKCGTE EEKNAPKAGN
     RGKRDSQLIL MSFFQRVLFN DRLSELDYEM FWKMTWLMKG VTPDKFEVVL MVDADTKVLP
     DALTFMIAAM ANDITIMGLC GETRIANKRA SCKLSQNDTL TGRWAYLI
//
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