ID C4JLB2_UNCRE Unreviewed; 810 AA.
AC C4JLB2;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=UREG_03620 {ECO:0000313|EMBL:EEP78774.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP78774.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CH476616; EEP78774.1; -; Genomic_DNA.
DR RefSeq; XP_002544103.1; XM_002544057.1.
DR AlphaFoldDB; C4JLB2; -.
DR STRING; 336963.C4JLB2; -.
DR GeneID; 8443753; -.
DR KEGG; ure:UREG_03620; -.
DR VEuPathDB; FungiDB:UREG_03620; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_012773_0_0_1; -.
DR InParanoid; C4JLB2; -.
DR OMA; NCIHVFL; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000002058; 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:UP000002058};
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 22..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 509..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 687..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 92675 MW; 553BA8DFBB90B68D CRC64;
MGLLSKAAAY HPSTEFRTQD KIYIGVIGPV MCAAVLEWFL WIAAFIYCLY KVYVKADHWS
VKLMAVVMAV AFTALRGIFL PVMLVTLPLP YTITRHFPPR LVSFLQWFAF WTFAVLLIIP
WLFCVYRLVT NSLGRKKRIK EVLDVRTAPK TVIVMPVYKE EPPVLIKAIN SVVECDYPVE
CIHVFLSFDG DQVDELYLKV VEHLGVPINL KTYPQSIDVT YKGSRITISR FKHGGKRHCQ
KQTFRLVDKV YENYLRRNDN LFVLFIDSDC ILDRYCLQNF MYDMELKPGS KRNMLAMTGV
ITSTTEKTSL ITLLQDMEYI HGQLFERSVE SGCGAVTCLP GALTILRFSA FRKMAKYYFA
DKASQCTDIF DFGKCHLGED RWLTHLFMIG ARERYQIQMC TSAFCKTEAV QTFSSLLKQR
RRWFLGFITN EVCMLTDARL WFRYPILCLI RFMQNTIRTT ALLFFIMIIS IMTTSNRVEN
LPVGFIAVSL GLNYMLMFYF GLRLRRFKAW LYPMMFLLNP FFNWLYMVYG IFTAGRRTWG
GPRADAAEAD SNTTPAQAAE LAEEQGDELN VKVETFTAVP KPQESVPVHP SHGIEGRFAP
PELNSDGYYN NGNISGLSLP THVRHNPILP HIPLHPRDSF LSEFTNGSGN SICWPRRVES
IIADEEVDQE EVYITTEDQQ KMQLARQARS SNAAVDGVPF DSVSDQEKDS ISRALGPYTP
DRRSNVHERQ SQSGAYDRLS FDRARRPRVG QSPLRTSSAA EPEDEESGIG RAITTPDVAR
TRDSSAPEGE SGRRERRRLS KTPREPQDMV
//
