ID M7SH37_EUTLA Unreviewed; 566 AA.
AC M7SH37;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=UCREL1_9469 {ECO:0000313|EMBL:EMR63578.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR63578.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer.
CC {ECO:0000256|ARBA:ARBA00024009}.
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; KB707201; EMR63578.1; -; Genomic_DNA.
DR RefSeq; XP_007797321.1; XM_007799130.1.
DR AlphaFoldDB; M7SH37; -.
DR STRING; 1287681.M7SH37; -.
DR KEGG; ela:UCREL1_9469; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_013022_2_1_1; -.
DR OMA; WGKTRIA; -.
DR OrthoDB; 2103951at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMR63578.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 377..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 566 AA; 64300 MW; 22D63F9D7148B1A5 CRC64;
MIVNISIWSL KNLIFKPKFI IPENPETMVL LMPCYNESYE ECSKSLDSLV NQVHIDQHKK
AIMVICDGKV RGPGMEKSTG GYLNEDILVD QTERRMIKEA YVAWDGQMMD IEISKGNYKG
VPFFCIVKQQ NQGKRDSLIV IRSFVYKFNV RHERPKVIFT PEFFAEMSDW MVNEAGIDNI
DHLIGMDADT VFADDCISHL LVESRHPKTI GVCGYVAVDF SSRPWNIWSI YQSAEYTIAQ
GLRRLHQSLV THKVSCLPGC CQLLRVCDET CGDRIIIDLF GYHPKVTDGM LKQIRATASE
DRNHVCLMLM EFTHAQTRQA LKAKAFTDVP HSLSVFLSQR RRWTLGATGN DLMLLTSSPL
RFNLFERVVA LSNVTTWTLN FFVIASLACM VNAFIHQPLW VTMAFASVMF VPLSYYLVMA
MWLPENRFQR YQFLVGLAVF VTCGPFINIS VTLYAIFYMD NFSWGKTRQV IAEDPEEEGA
AEGEVVEKIV EPPAPGLPAP SDDIAAIASG HRCNSIPDLE NQLDQVHQPY IAPAGRRRVD
SILCAELEKL PDIDKLPDIR RWRTSG
//
