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Database: UniProt
Entry: K5W515_PHACS
LinkDB: K5W515_PHACS
Original site: K5W515_PHACS 
ID   K5W515_PHACS            Unreviewed;      1005 AA.
AC   K5W515;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   22-FEB-2023, entry version 45.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=PHACADRAFT_257626 {ECO:0000313|EMBL:EKM54034.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM54034.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM54034.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM54034.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
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; JH930473; EKM54034.1; -; Genomic_DNA.
DR   RefSeq; XP_007396739.1; XM_007396677.1.
DR   AlphaFoldDB; K5W515; -.
DR   STRING; 650164.K5W515; -.
DR   GeneID; 18916902; -.
DR   KEGG; pco:PHACADRAFT_257626; -.
DR   HOGENOM; CLU_002572_0_0_1; -.
DR   InParanoid; K5W515; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd04190; Chitin_synth_C; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF26; CHITIN SYNTHASE 7; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Transferase {ECO:0000313|EMBL:EKM54034.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        218..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        699..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        729..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        752..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          885..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..943
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..969
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  110491 MW;  76FEF0BF7FE7CC40 CRC64;
     MCTFIGFLTV GFQKVLCPGS AQTAGKFVRV GTRPDTLGVQ GWLVNVTKTP QVNGVNFGTL
     LESPGQDITT LFQRDASSYP ACNGLSFRAA AEAPCGNNAC TLPTLNQQTL SSLNMVNTSL
     IVGYDWSDVA QLQNYLVLDG AVLDMNSYMA LHPTPIPSDS VDAAIRQILT QMPGDSGRDG
     TRLFFFYPET RAAVPCLIQR YYAGNIDKIT PGCFASQLIL YAGLIVILSL VMVRFVMSCI
     FSWFISARLA GPPDTMSLNR SAISPAVMPE GANMSIDNPN GTAPWASGKK LTVPSKSMRS
     LASSNSTLLN DGTAPIVSLA QIGAELFAVC LVTCYSEGED SLRTTLDSIS TTTYSDARKL
     LFVVADGMIT GAGEKKSTPD ICVSVLEADP RFGNPVPMSY NAVGAGVKAE NRAMVYAGHY
     TVAGRRTPTI IVVKCGTERE AATDKKPGNR GKRDSQLILM NFFSRVTYND RMTPLDFDLF
     RKIHILMGVT PDFFEVCLMV DADTKVAPDS LKYLVNCMHH DQMIMGVCGE TRIANKRQSW
     VTAIQVFEYF ISHHMAKAFE SVFGGVSCLP GCFSMFRLKA RKSTGEDWVP LIIKPEIVKE
     YSQSIVTTLH EKNLLLLGED RFLTTILLRT FPNRKMMFLP QARCRTVVPD TFKILLSQRR
     RWINSTIHNL MELVLVRNLC GTFCFSMQFV VFMDLLGTVV LPIAITLTYS LIINMALDPP
     KTFEEAIPLV LLIAVLGLPA VLILITTRKV VYVFWMLIYL AALPVWNLIL PVYAFWHFDD
     FSWGETRKVE GEAKGEAHGD GGAAHSGPSI PLRRWEDWER SRLRKLRREE RRRREFERQH
     GSYMTANGEL LTVRSPVHSQ YGGSDTISVT SSEDEHWAAQ IGGYNENSAS YPPPPIGLMP
     QASVSGESVS ASELESMLEH GYDDRPQYRG ASQTPSPQRY QLSDRPGEYT PLSRTAASSP
     VSSTGPVDGL SSAAEPYRTH VKKRSGGGSG AKYGPLGPLD PGSRI
//
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