ID   CHSD_EMENI     STANDARD;      PRT;  1184 AA.
AC   P78611; Q00744;
DT   15-JUL-1999 (Rel. 38, Created)
DT   16-OCT-2001 (Rel. 40, Last sequence update)
DT   25-JAN-2005 (Rel. 46, Last annotation update)
DE   Chitin synthase D (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl
DE   transferase D) (Class-V chitin synthase D).
GN   Name=chsD; Synonyms=chsE;
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiales; Trichocomaceae; Emericella.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 89;
RX   MEDLINE=96285568; PubMed=8709948; DOI=10.1007/s004380050188;
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   MEDLINE=97188530; 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.
RC   STRAIN=FGSC 4;
RX   MEDLINE=96406387; 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).
CC   -!- FUNCTION: Plays a major role in cell wall biogenesis.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-
CC       beta-D-glucosaminyl)}(N) = UDP + {(1,4)-(N-acetyl-beta-D-
CC       glucosaminyl)}(N+1).
CC   -!- SUBCELLULAR LOCATION: Plasma membrane-bound.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. Class V
CC       subfamily.
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DR   EMBL; D83246; BAA11866.2; -.
DR   EMBL; U52362; AAA97482.1; -.
DR   InterPro; IPR004835; Chitin_synth_fng.
DR   InterPro; IPR001199; Cyt_B5.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
KW   Cell wall; Glycosyltransferase; Multigene family; Transferase;
KW   Transmembrane.
FT   TRANSMEM    221    241       Potential.
FT   TRANSMEM    476    496       Potential.
FT   TRANSMEM   1039   1059       Potential.
FT   TRANSMEM   1073   1093       Potential.
FT   TRANSMEM   1097   1117       Potential.
SQ   SEQUENCE   1184 AA;  133505 MW;  D6157184F154EDE5 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
     QSHNGSGNVS 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 WRDFEKGMSM LTVLHDARTA NDIY
//