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Database: UniProt
Entry: CHSD_EMENI
LinkDB: CHSD_EMENI
Original site: CHSD_EMENI 
ID   CHSD_EMENI              Reviewed;        1194 AA.
AC   P78611; C8VMZ3; Q00744; Q5BD25;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 4.
DT   08-MAY-2019, entry version 115.
DE   RecName: Full=Chitin synthase D;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase D;
DE   AltName: Full=Class-V chitin synthase D;
GN   Name=chsD; Synonyms=chsE; ORFNames=AN1555;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FGSC 89;
RX   PubMed=8709948; DOI=10.1007/BF02172373;
RA   Motoyama T., Fujiwara M., Kojima N., Horiuchi H., Ohta A., Takagi M.;
RT   "The Aspergillus nidulans genes chsA and chsD encode chitin synthases
RT   which have redundant functions in conidia formation.";
RL   Mol. Gen. Genet. 251:442-450(1996).
RN   [2]
RP   ERRATUM.
RX   PubMed=9037115; DOI=10.1007/s004380050353;
RA   Motoyama T., Fujiwara M., Kojima N., Horiuchi H., Ohta A., Takagi M.;
RL   Mol. Gen. Genet. 253:520-528(1997).
RN   [3]
RP   SEQUENCE REVISION.
RA   Motoyama T., Fujiwara M., Kojima N., Horiuchi H., Ohta A., Takagi M.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=8810520; DOI=10.1006/fgbi.1996.0030;
RA   Specht C.A., Liu Y., Robbins P.W., Bulawa C.E., Iartchouk N.,
RA   Winter K.R., Riggle P.J., Rhodes J.C., Dodge C.L., Culp D.W.,
RA   Borgia P.T.;
RT   "The chsD and chsE genes of Aspergillus nidulans and their roles in
RT   chitin synthesis.";
RL   Fungal Genet. Biol. 20:153-167(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Plays a major role in cell wall biogenesis.
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   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. Class V
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA97482.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAA11866.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA64262.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; D83246; BAA11866.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; U52362; AAA97482.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AACD01000025; EAA64262.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF85100.1; -; Genomic_DNA.
DR   PIR; JC6079; JC6079.
DR   RefSeq; XP_659159.1; XM_654067.1.
DR   STRING; 162425.CADANIAP00008183; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblFungi; CBF85100; CBF85100; ANIA_01555.
DR   EnsemblFungi; EAA64262; EAA64262; AN1555.2.
DR   GeneID; 2875763; -.
DR   KEGG; ani:AN1555.2; -.
DR   HOGENOM; HOG000158449; -.
DR   InParanoid; P78611; -.
DR   KO; K00698; -.
DR   OMA; TELEFEM; -.
DR   OrthoDB; 134286at2759; -.
DR   BRENDA; 2.4.1.16; 517.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0030428; C:cell septum; IBA:GO_Central.
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; IMP:AspGD.
DR   GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IGI:AspGD.
DR   GO; GO:0006031; P:chitin biosynthetic process; IMP:AspGD.
DR   GO; GO:0048315; P:conidium formation; IGI:AspGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Complete proteome;
KW   Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   1194       Chitin synthase D.
FT                                /FTId=PRO_0000193693.
FT   TRANSMEM    221    241       Helical. {ECO:0000255}.
FT   TRANSMEM    476    496       Helical. {ECO:0000255}.
FT   TRANSMEM   1039   1059       Helical. {ECO:0000255}.
FT   TRANSMEM   1073   1093       Helical. {ECO:0000255}.
FT   TRANSMEM   1097   1117       Helical. {ECO:0000255}.
FT   CONFLICT    606    606       L -> S (in Ref. 1; BAA11866 and 4;
FT                                AAA97482). {ECO:0000305}.
SQ   SEQUENCE   1194 AA;  134864 MW;  5CFA527B791118B6 CRC64;
     MSLPQRPGKT SPRREETSAF REPSRRRRRE SDSLSNNDPT SPRHHRHHRS HSSRHQHDID
     EERAEEGGIR RKRSLVKPER GRMDPSHPNY LYRQKTQNMP TYNPMTGNEP LIHEEGEAET
     NSTPSMDSKR KDALYGAHGN VNKPMERVPT RHRSKKRKGS RKISKREAAA EKRRRKAMEQ
     VRPPSLWTTY CSVITFWAPD FVLKCFGMPQ KAQRSAWREK IGLISIILMI AAFVGFLTFG
     FTATVCGTPP TRLKINEIGS GYMIFHGQAY DLTKSTHPAA AGIPDMTNVL YDLPHKYGGQ
     DGSFFFQEVN GACKGLITRT ENSDIPTNSN GDLAWYFPCH AFNQDGSSEP NTTVSYYNGW
     ACHTSGSARK SFYSLKNSGD VYFTWEDTKN TSRKLAVYSG NVLDLNLLNW FDDTQVNYPT
     KFKDLRDNDD IRGVDLTYYF QTGEDKQIGK CLSQIIKVGS IDTDTVGCIA SQVVLYVSLI
     FILSIVIVKF AFALLFQWFL APRFAAQKTS MGAVDSKARN QQIEDWSNDI YRPGPRLADP
     VPGDRMSKRA SFLPTTSRFS SPYTVSNGGK QKPQWVTMAS QNSTTRLVPP ASGTTPSIYR
     QSHNGLGNVS VDNSRLNPSA SRTSLVQDSR YSTVIPDSEG IGSAGYVHEL VVPQPPPDWQ
     PYGFPLAHAM CLVTCYSEGE EGIRTTLDSI ALTDYPNSHK SIVVICDGII KGKGEEFSTP
     DIVLRMMRDP IIPPEEVEAF SYVAVATGSK RHNMAKVYAG FYDYGEHSII PVEKQQRVPM
     MIIVKCGTPA EATAAKPGNR GKRDSQIILM SFLQKVMFDE RMTELEYEMF NGLLHVTGIP
     PDFYEVVLMV DADTKVFPDS LTHMISAMVK DPEVMGLCGE TKIANKTDSW VTMIQVFEYF
     VSHHQSKAFE SVFGGVTCLP GCFSMYRIKA PKGGQNYWVP ILANPDIVEH YSENVVDTLH
     KKNLLLLGED RYLSTLMLRT FPKRKQIFVP QAVCKTVVPD KFMVLLSQRR RWINSTVHNL
     MELVLVRDLC GTFCFSMQFV IFVELVGTVV LPAAISFTIY VVVSSIIKQP VQIIPLVLLA
     LILGLPGVLV VVTAHRLVYV LWMLVYLISL PIWNFVLPTY AYWKFDDFSW GDTRKTAGEK
     DKGHEDGEGE FDSSKITMKR WRDFEKDRRL RMQAGWQLPV GGHPPMPYEP YPEY
//
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