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Database: UniProt
Entry: W6QJS5_PENRF
LinkDB: W6QJS5_PENRF
Original site: W6QJS5_PENRF 
ID   W6QJS5_PENRF            Unreviewed;      1762 AA.
AC   W6QJS5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=PROQFM164_S03g001198 {ECO:0000313|EMBL:CDM34474.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM34474.1};
RN   [1] {ECO:0000313|EMBL:CDM34474.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM34474.1};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
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; HG792017; CDM34474.1; -; Genomic_DNA.
DR   STRING; 1365484.W6QJS5; -.
DR   OMA; WILERGW; -.
DR   OrthoDB; 1331060at2759; -.
DR   GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 2.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF13; CHITIN SYNTHASE; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   SMART; SM01117; Cyt-b5; 2.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 2.
DR   SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51998; DEK_C; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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        720..740
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        756..777
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1017..1036
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1408..1431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1443..1462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1469..1492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1704..1760
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1762 AA;  196237 MW;  B436F5590244462E CRC64;
     MSNRYSVFST QSTGLSVGPR PQHGAQVSTT TLLNALHSFY TAGQPYQLDS ATSLVVNTWV
     TAATTLPDGR TGATVDRDLA IRAWEHARRR AEDGSVVLGA LHQSTPSLLE PFIAAIPVET
     PEVALIALSA IRPFLTAVTS FNPSYSLHSA LAATFNLSLQ GSVVGLSFAL STSGINVRKG
     LLDIQPETGY RAFDAFYYLL TSTSTAAERE FLDLKDPAEY TLLNRSNTYN PPHYLPTADD
     AAAAEDFRAS LKSIGIKGAA QRGLLSALAG LLKLGNAVGF EVDQEDLEEV CEDAGGLLGI
     DPEILLHKCS TDEREVLIAG LYEALVDWVI SKANEAIAAD IQIALENDSS NGGGAAQWST
     DDTVNLTVID IPRPALGKAI MMRGIFDDAL GLNAEMKDDG IPLPPIGASI ISEMNSAVAQ
     VEPDLNIMTG LAGREREHDL DKRQGVLEKV GVELEIDAFL RRVLFPNDTE GISVGKRGRF
     DLANTLNSSR VWYHLSIHPT DDMPEQLVSL GPTAWSAGAV SRQLRDWRLP EWANRRLKQL
     DFTADFDVEE FVSRYARLGC TEGQDGVENW IIERGWSNGD AVVGEQRVWM REGAWWEAES
     MLDLKPEETQ VNPFMYGPAL YETAFTPDGT PIHENSNLLS MPPSGAIAPS VIDGAKSIAP
     SAPFANAVNT GDYGLGRKGD DKKGDIAYYD EYGRYVGEFD PEFGDPKHIE KKTITLGRRL
     WTGFVWALTF WIPSFVLRYI GRMKRPDVRL AWREKLVLVF LILLFNAIVC FYIIAFGDLL
     CPNKDKVWNK KEVSWHTTDN NFYVGIHGRV YDISKFWRTQ HSDITGETTS STNMEQFGGE
     ILDAYFPPPL NRYCSSFVTS DTLALQHNDT SAIALSTAEH KSGAQATSTT SALHKSTWYE
     KKFLPKIGTY YKGDLVWTRD TIKKQADADS RYWVIKDQKV YDLTDYFYTL STMNNLDTYD
     WLPSTLTALF KDNMGEDVTD KWEDTTDFKN AQTCLDFVFY VGKVDFRESA RCTVNNWILL
     TFTILICAVI LVKFLAALQL GSKRRPTPQD KFVICMVPAY TEGENDLRKG LDSLTALQYD
     NKRKLIFVIC DGMIVGGGND RPTPKIVLDI LGVDPKMDPP ALPCKSLGQG SEQLNYGKVY
     SGLYEYEGNV VPYIVVVKVG KESEQRKSKP GNRGKRDTQV LLMQFLNRVH HRSPMSPLEL
     EMFHQINNVI GVDPELYEYC LMVDADTTVK EDSLNRLVAA CAADAKIAGI CGETSLQNEE
     RSWWTMIQVY EYYISHHLAK AFESLFGSVT CLPGCFTMYR LRTADKGRPL IISDKVIHDY
     ADNDVDTLHK KNLLSLGEDR YLTTIMTKHF PAMSYKFIPD AYASTAAPDT WSVLMSQRRR
     WINSTIHNLV ELAALEDLCG FCCFSMRFVV LVDLVGTLIL PATCVYLTYL IYRVASNTGP
     FPMISIIMLA GVYGLQAIIF IVKRQWQHIG WMIIYLLAYP IYNFVLPLYA FWKQDDFTWG
     TTRIVIGEKG DKRVIAVEDE PFDPRSIPLQ RWDDYAMANN LPGRRGEVSA SQEKVYATGR
     YDEMAMEMDD MHSQYSSVKP ASTILTGFPG QGRNHPYMPP QSPAPFVGGN VPGNRNSHMS
     NFSRYTDLPQ MSPRMGGHSA QASRHMSMGG LSAYQDNPMA SSRHSVGMMQ SSENLLGNAG
     SRSPLPQYPS RPASTAFDFR SASGPDEGAI TEAIRGCLAE VDLDTVTKKQ VRVLVEHRLQ
     TSLTGDKRAF LDRQIDQELA NM
//
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