ID W9PVW0_FUSOX Unreviewed; 2302 AA.
AC W9PVW0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=FOVG_07124 {ECO:0000313|EMBL:EXA46407.1};
OS Fusarium oxysporum f. sp. pisi HDV247.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1080344 {ECO:0000313|EMBL:EXA46407.1};
RN [1] {ECO:0000313|EMBL:EXA46407.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HDV247 {ECO:0000313|EMBL:EXA46407.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum HDV247.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXA46407.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HDV247 {ECO:0000313|EMBL:EXA46407.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "Annotation of the Genome Sequence of Fusarium oxysporum HDV247.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; JH650971; EXA46407.1; -; Genomic_DNA.
DR HOGENOM; CLU_000192_0_0_1; -.
DR Proteomes; UP000030751; Unassembled WGS sequence.
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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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 InterPro; IPR007219; Transcription_factor_dom_fun.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF13; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF04082; Fungal_trans; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 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 684..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1010
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1380..1401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1413..1434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1441..1464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 750..810
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 1529..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1677..1703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2302 AA; 258247 MW; 21AEAF4F6F74B517 CRC64;
MSNFGHASPR ARSIHRTNVT LLNAIHASYL HSKPYQLDAR TSVVVNAWHT SSQAGPIVDT
LLGEKVWEHA RRRLENNCIL LQSLHPSTPS LFIPFLDTLP FAVPSSILTS LRALQPFLYC
VTPHNPSTSR HAALALTLDM TPEGRVSNAS LSMPAKGIDI TSGLLGIAPE VGYRAFDVFY
YLLTSVSTQA ERDFLSLKPA SHYSILAASG TYQPSSHLAA ADDGAAADDF RQAIREIGIK
GSTQRKLIAT LAGLLTLGNT LDQNVPRSDV VEVCEEASIM FGMEPEVLVN LSHSDRRAFM
SKVYEALINW VIVKANVAIA SQTVHPRRGT ESPLTAGAGD ESIRIIIIDM PDSSFGRVVA
METNFDESFG VNAEAIEDGI FTSSVDPLVW KDTKAMLDSS WYRKIMVAKS AAEETCEERQ
QSVMDSIIFL AEDDSFLKII LPYETSTTPG LHVLDLRDAL DSCRVWYHLC LYPGSNTMPG
SLASPLLTAP WSPSDVSVQL VSWRLRDWAN RSFTNPAYTV DFGIDEFLQR YSVIHSYLSS
KDDICNWALE RGWHNTNVAV GQERVWMSEE AWQQAEGMLD MKLALIRQQR SQSQLGFRNE
LFPSPRPVSV FSSGYGSRDH FLLGTYLDRE GNIPVTGGQL GTKEPLIEIS PTDAPQNHTI
LVSKDPELAK TTRIETKHVD MSRRLWVCFV WALTFWIPSP LLLHLGRMTR PDVRQAWREK
LALFSIIIFL NALILFWMIG LGKLLCPNSD KAWNRKEVAT HQGEDEFWVS IHGKVYDISD
FWKRQHSDTA IETTTANMQP LAGYDMDEYF VPPLNMACKG LGIAETTRLR ANTTAEYTTA
LHTSGYYCLD SKSALSKDDW YWTNFEPGIK EYYHGELVYS DSKFKGEAEQ GRMWAKYGNK
IYDLTNYFYT QSLYKNDAKY KFLNERVTKL WEDNPGKNIK EELDIMLEDS STNKTKHDNI
VASWRCIQAI SYKGISDFRE SAKCQVNNWL LLAFTVMVCA IILVKFLAAL RFGSKRRPSP
QDKFVICQIP AYTEEEESLR RAIDSLTCLK YDNKRKLMCL ICDGIAVGQG NDRPTSKLVL
EILGSDPKLD PPARAFKSIG SGSDQLNYGK VYSGLYECDG NIVPYIVIVK VGKESEQTRP
KPGNRGKRDS QLLLLSFLNR VYHDSPMNPL ELDMFHHIND VIGVDPRMYE FLLMVDADTA
VQEDALNHLV AACANNTKIA GICGETRLEN DEKSWWTMIQ IYEYFISHNL AKAFESLFGS
VTCLPGCFTM YRLRTFDGKK PLIVSNAVLR DYSVCDVETL HLKNLLSLGE DRYLTTLMIK
HFPSMWLKFL PEAQCQTVAP ESWKVLLSQR RRWINSTIHN LVELMRLENM CGVCCFSMRV
VVFADLFGTI IFPATCVYLV YLMYRVITNT GEFPMISIIL LAATYGLQAL LFLLKRQWQH
IGWMVIYLMA LPVYSFFLPL YSFWNQDNFS WGNTRVVIGE KGDKQVVAID DEGFDPASIP
LQRLVDYAVV NSLPNRCYQE TLRHSFYSSD PGTSSIRNSY LPGQSTGMLG NQPPIGVDGD
SQQHGSWNRL SMMTGGMISY SGQNDRPKAS FGLNESGRER DTTRTQSGLG LTTPRALGES
GLSNDVISAS IKWTLGKADL DSITKRQVRA IVERRLDTDL SGEQLVFFSR ELDRQLGEME
SSVGAPCTPR SPPPPRKKRG PNRDLQARLA HCEKLLEECE AAHKQQPPSS SSSTREPSVG
PKPTVPGKLV PGDGVVNFTD SPRWAALHEE LGAMHELVDV DRSKVSPPPP DDSWNDDGLL
PDADTESDFR FLPSQIFHLW KVFLNRVHPV TKIIHAPSTQ LHVVEAACTS GSGLSVRTQA
LLFSIYNAAL FTLSNDECLE FMGRPKRQVA QSCAKALRVH LRRTNFLRSA SLTTLQAVVL
YLFSLQGHHD THATWIFSGI CVRIAQKMGL HRDGESLGLP PFETEMRRRL WWRIYMLDAR
CGLKSGLGPS MMPSAGDSKM PTNLNDSEMH PNSTIYFQDR YGPSEMAVSF LIYSMGKFLA
ESPSVEASVI QHEIDMATTV PQARANQLAE LPKLAKEVEN RLTHIMDRFA DPSTPNIYEL
AGHIKAQILS RVRIMASMPP TKLSLSSQPL QPADKLFLVA VRVVEQSVGE YEAMERIGFL
WYMKMHFQLD LFAFMVSQLS RQPAGDMVEK AWELVSKVYQ YHEELFDASE KSNLALATAT
TSAWETKHGP IFTRSVHHVQ APAYIQRLGT MVAVDYAALN MASVTLSDVV GDVDGDPAPP
WDDLSLAFLD PSGAGLQFPG MF
//
