(data stored in SCRATCH zone)

SWISSPROT: Q758F2_ASHGO

ID   Q758F2_ASHGO            Unreviewed;       884 AA.
AC   Q758F2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 104.
DE   RecName: Full=Chitin synthase {ECO:0000256|RuleBase:RU366040};
DE            EC=2.4.1.16 {ECO:0000256|RuleBase:RU366040};
GN   ORFNames=AGOS_AEL190W {ECO:0000313|EMBL:AAS52495.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52495.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52495.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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-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|RuleBase:RU366040};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU366040};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU366040}.
CC   -!- SIMILARITY: Belongs to the chitin synthase family.
CC       {ECO:0000256|RuleBase:RU366040}.
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DR   EMBL; AE016818; AAS52495.1; -; Genomic_DNA.
DR   RefSeq; NP_984671.1; NM_210024.1.
DR   STRING; 33169.AAS52495; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblFungi; AAS52495; AAS52495; AGOS_AEL190W.
DR   GeneID; 4620855; -.
DR   KEGG; ago:AGOS_AEL190W; -.
DR   HOGENOM; HOG000162144; -.
DR   InParanoid; Q758F2; -.
DR   KO; K00698; -.
DR   OMA; QHGIAKN; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006031; P:chitin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IEA:EnsemblFungi.
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;
DR   PRODOM; Q758F2.
DR   SWISS-2DPAGE; Q758F2.
KW   Cell membrane {ECO:0000256|RuleBase:RU366040};
KW   Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU366040};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU366040};
KW   Membrane {ECO:0000256|RuleBase:RU366040};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|RuleBase:RU366040};
KW   Transmembrane {ECO:0000256|RuleBase:RU366040};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU366040}.
FT   TRANSMEM        579..600
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366040"
FT   TRANSMEM        612..631
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366040"
FT   TRANSMEM        643..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366040"
FT   TRANSMEM        679..700
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366040"
FT   TRANSMEM        712..731
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366040"
FT   TRANSMEM        812..831
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366040"
FT   TRANSMEM        843..866
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366040"
FT   DOMAIN          168..232
FT                   /note="Chitin_synth_1N"
FT                   /evidence="ECO:0000259|Pfam:PF08407"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..147
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   884 AA;  100100 MW;  87F134DAFA93A99F CRC64;
     MVANPFLSEE SDRAGGPMHG ERAIPPLPRS PGRLAPSRAA TRYSPQRPER GGLAERAHLA
     PNRYEANLSL SPSRNMHTVL DMGFEASDSD SDSERSPVAP SSHGGRTHGG RPSMGSAYSP
     RKADDDGSSS VLSGATIGQT NFQLNHPQKR YIRRGKSEVR RTPPLAKQKN ILKLDNPIPR
     GLLDILPRRD SPEFTEMRYI ACTVEPDMYV EQGYSLRMAE MDRECQVVVC VTMYNEDKYA
     LARTLHSIQR NISHLCRRKK SQVWGKNGWK KVQVIIVSDG RNKINSGSLD YLSALGVYQE
     DMAKSTVNGE PVRAHIFELT TQVSINDQLN YKSENIVPCQ MVFCLKEENQ KKINSHRWLF
     NAFCRVLDPT VVMLVDVGTR LNDTAVYHLW KAFDMDSNVA GAAGQVKTMK GKYGCKLLNP
     LVASQNFEYK MSNILDKPLE SMFGYISVLP GALSAYRYRA LQNNEDGTGP LYSYFLGESI
     EGRNCNVFTA NMYLAEDRIL CWELVAKRDA KWVLKYVKEA QGETDVPEEP PEFISQRRRW
     LNGAMFAALY AQLHFFQIWG TKHSLRRKIF FHIEFLYQFF QMFFSWFSIS NFFLTFYYLA
     GSMIGVLKNG KAVFTFFKYL IICDLAAIFI ISMGNSPQGA NHLFIISMFL LSVCSTYALV
     CGITFAAKTL TAISTPSAAF SNIMVSLLST YGLYILSSFL YLDPWHIFTS SIQYFLMLPS
     FVCTLQIFAF CNTHDVSWGT KGASQGSKPK SEAMVTQGPD GKQIVEGTEW PQDIDNKYQE
     IKSRLKSDEV VEIKVDPIQK QADHYRDVRT RIVMLWMLSN LILIMMITQI YSPEETSNNK
     YLVFVLGSVA GLAAFRFLGS FSFLVIKYTR MIVKWKRKSA QIAK
//

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