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
//