ID A0A177DH97_ALTAL Unreviewed; 857 AA.
AC A0A177DH97;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=AA0117_g4644 {ECO:0000313|EMBL:RYN77860.1}, CC77DRAFT_1031975
GN {ECO:0000313|EMBL:OAG19173.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG19173.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG19173.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG19173.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000291422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL bioRxiv 0:0-0(2019).
RN [3] {ECO:0000313|EMBL:RYN77860.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN77860.1};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL J. ISSAAS 0:0-0(2019).
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; KV441481; OAG19173.1; -; Genomic_DNA.
DR EMBL; PDXD01000008; RYN77860.1; -; Genomic_DNA.
DR RefSeq; XP_018384594.1; XM_018526702.1.
DR STRING; 5599.A0A177DH97; -.
DR GeneID; 29112296; -.
DR KEGG; aalt:CC77DRAFT_1031975; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1031975; -.
DR OMA; NCIHVFL; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR Proteomes; UP000291422; 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:SF41; 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:UP000077248};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 493..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 526..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 693..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 96986 MW; 2E01854F4916F975 CRC64;
MVWQEMMGLA ARAVVARAEV DGSIPDITDP WPAKDIAYVA IIGGLMLAAL LEWFLWVAAF
LYCIVKVFQK AETISVRILS IFFGILFFAL RAIFLPIMVV TLPLPSQVTK YFPQEMVDFL
QWFAFWSFAG LLTVPWLFCV YQLVTHSVGR SRRIKSVLDE SSAPKVVIIM PCYKEIPEIL
LRTCDSLVDC EYPPSCLHIF LSFDGDQEDE LYLNTIEKLG VPLTLDTYPK SIDVIYRSCR
ITISRFPHGG KRHCQKRTFK LIDKIYSEYL KRNDNLFVLF IDSDCILDKT CIQNFMYEME
LKPGSKKNML AQTGVITSTT EKNSLITLLQ DMEYVHGQLF ERSVESGCGA VTCLPGALTM
LRFSAFRRMA KYYFADKAEQ CDDLFDYGKC HLGEDRWLTH LFMIGAKERY QIQMNTGAFC
KTEAVQTYQS LLKQRRRWFL GFITNEVCML TDIRLWKRYP ILLIVRFMQN TIRTTALLFF
ILCISLITTS QKVANLPVGF IAISLGLNWL LMLYFGAKLG RYKIMLYPLM FIVNPFFNWV
YMVYGIFTAG QRTWGGPRAD AGSADNKTTP QEAIEAAEAT GDDLNVVPET FKAAAEAHKH
RPAPIPLQPG ENIEGRFAAA ERLPNGWYQQ GNDSGLTLPN TMPRNPNVPH VPLHPRSSMD
SFASQETSAA NSIYMPRRVE SFMDPEDARI YHKTQQTQKP AGGAFYEEPR SGPYEVGAGA
SKGMYSESVD SIDDDSVYQS KGPQRPAQMR TNSDLAHAPV RTSPLSNQQT GLESPKPSYN
RTNSMEQRQG RSPLARQYVH TAPGDGIELQ APQQSSLMRD VSPAPLGQPT MPASNHGRSE
STDSKKRKRL SKQQPRK
//
