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Database: UniProt
Entry: W1QAA5_OGAPD
LinkDB: W1QAA5_OGAPD
Original site: W1QAA5_OGAPD 
ID   W1QAA5_OGAPD            Unreviewed;       954 AA.
AC   W1QAA5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   31-JUL-2019, entry version 28.
DE   RecName: Full=Chitin synthase {ECO:0000256|RuleBase:RU366040};
DE            EC=2.4.1.16 {ECO:0000256|RuleBase:RU366040};
GN   ORFNames=HPODL_01832 {ECO:0000313|EMBL:ESW97746.1};
OS   Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 /
OS   NRRL Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW97746.1, ECO:0000313|Proteomes:UP000008673};
RN   [1] {ECO:0000313|EMBL:ESW97746.1, ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RX   PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA   Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA   Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A.,
RA   Mardanov A.V., Skryabin K.G.;
RT   "Genome sequence and analysis of methylotrophic yeast Hansenula
RT   polymorpha DL1.";
RL   BMC Genomics 14:837-837(2013).
RN   [2] {ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RA   Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA   Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT   "Genome sequence of the methylotrophic yeast Hansenula polymorpha
RT   DL1.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a major role in cell wall biogenesis.
CC       {ECO:0000256|RuleBase:RU366040}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-
CC         alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1)
CC         + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593,
CC         Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16;
CC         Evidence={ECO:0000256|RuleBase:RU366040};
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU366040}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU366040}.
CC   -!- SIMILARITY: Belongs to the chitin synthase family.
CC       {ECO:0000256|RuleBase:RU366040}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ESW97746.1}.
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DR   EMBL; AEOI02000009; ESW97746.1; -; Genomic_DNA.
DR   RefSeq; XP_013933831.1; XM_014078356.1.
DR   STRING; 1005962.W1QAA5; -.
DR   EnsemblFungi; ESW97746; ESW97746; HPODL_01832.
DR   GeneID; 25771288; -.
DR   OrthoDB; 256142at2759; -.
DR   Proteomes; UP000008673; Chromosome VI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006031; P:chitin biosynthetic process; IEA:InterPro.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR004834; Chitin_synth_fun.
DR   InterPro; IPR013616; Chitin_synth_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF01644; Chitin_synth_1; 1.
DR   Pfam; PF08407; Chitin_synth_1N; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU366040};
KW   Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU366040};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008673};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU366040,
KW   ECO:0000313|EMBL:ESW97746.1};
KW   Membrane {ECO:0000256|RuleBase:RU366040};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008673};
KW   Transferase {ECO:0000256|RuleBase:RU366040,
KW   ECO:0000313|EMBL:ESW97746.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU366040};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU366040}.
FT   TRANSMEM    576    595       Helical. {ECO:0000256|RuleBase:RU366040}.
FT   TRANSMEM    607    631       Helical. {ECO:0000256|RuleBase:RU366040}.
FT   TRANSMEM    651    673       Helical. {ECO:0000256|RuleBase:RU366040}.
FT   TRANSMEM    685    707       Helical. {ECO:0000256|RuleBase:RU366040}.
FT   TRANSMEM    744    770       Helical. {ECO:0000256|RuleBase:RU366040}.
FT   TRANSMEM    863    882       Helical. {ECO:0000256|RuleBase:RU366040}.
FT   TRANSMEM    915    937       Helical. {ECO:0000256|RuleBase:RU366040}.
FT   DOMAIN      157    241       Chitin_synth_1N. {ECO:0000259|Pfam:
FT                                PF08407}.
FT   REGION        1     21       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION       62     93       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   954 AA;  108198 MW;  23A4D3B8A71281E4 CRC64;
     MVQNDNPFRL DDDDSVEGQS LHNNPFVQMV DDDIHQTSNH AQRSAFDLND YQDSYNETVS
     SPVRHSILRP PSNVYDATQS SFSSNSSFLG SEKLPSNSYT RPVIYQPSVP PMPYQQSFPV
     FQSFMRDGDE PVIEDLFFDK TENDGIEPLN VATSGDTKVQ LLDDKHYSFD FPVPKQLVAR
     IPFEDAKNLT EFTYLRYHAI TADPKDFTSG DLEKRHDIVN YPLRPNLYGV RRETELMIVC
     TMYNEDEVLL GRTLKGVFKN IKTIIRLAKT RGKKIVVVIV SDGRSKIHER SKALLTLLGC
     YQEGVIQEKV NGDDVNAHLF EYTTTFGIGQ FDYHRGDEGK GFTVPLVTEQ TVPVQMMFLL
     KEQNKQKINS HRWAFNFLCP NLNPKIVCLL DVGTEPGPDS IYKLWQAFKD PQVGGACGEI
     RAMLGKKMSP NDEGSLMQKL GRWVLRTSSD LKCVVLNPLT AAQNFEYKIS NILDKPMESA
     FGFVTVLPGA FSAYRYEALQ GDPLEAYFHG EDMKTNTEKP AGTLESNMYL AEDRILCFEL
     VAKKGASYVL RYVHDAFGVT DVPGNIAEFI NQRRRWLNGS FFAALYSVMH FYRIVRSKHS
     FGRKLVLLVE VVYQTVNIGL SWLSISFYFL VFRILTLGLA DTSVGFKAGN ILAVVFLWLY
     IAALALTFII SFGNKPKDAK RLYQLAFLLF SIVMAYMIFC VIMLTIASVH TIQSEIAAST
     KSKVLAYLEN SKFRDLTVAL SSTYALYVLG SLLFFEFFHL FGCSLQYIFL SPAYINVLSV
     FAFCNIHDIS WGTKGALKVE EVGKKEANKS ERSNELILSE ALQDPDELYL LANNNISKPE
     AVKKESTLKT SERNYALGRT YTVLAWLVSN FIILVLVLRT GGLDDYNDYK DSGTSTTTAT
     TKVKRNVDSK SSNRFMTFVL WCVCCLALVR FFGVLVYRLD TFFRKRRYHK HPVI
//
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