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Database: UniProt
Entry: A0A0D1X7N7_9EURO
LinkDB: A0A0D1X7N7_9EURO
Original site: A0A0D1X7N7_9EURO 
ID   A0A0D1X7N7_9EURO        Unreviewed;      1763 AA.
AC   A0A0D1X7N7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=PV11_05845 {ECO:0000313|EMBL:KIV83856.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV83856.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV83856.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV83856.1,
RC   ECO:0000313|Proteomes:UP000053599};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-2015) 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: 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; KN846952; KIV83856.1; -; Genomic_DNA.
DR   STRING; 1016849.A0A0D1X7N7; -.
DR   HOGENOM; CLU_000192_0_0_1; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000053599; 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:0048315; P:conidium formation; IEA:UniProt.
DR   CDD; cd04190; Chitin_synth_C; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
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; PF00173; Cyt-b5; 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   Reference proteome {ECO:0000313|Proteomes:UP000053599};
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        724..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        760..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1021..1040
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1412..1435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1447..1466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1473..1496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1704..1761
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
SQ   SEQUENCE   1763 AA;  195548 MW;  E38BD9630F6B41C8 CRC64;
     MANRYSTYSN KSSQVGAARS AAQQSTQVST TTLLNALHTI YASGQTYELD SSTSIAVNTW
     LSAANPDAHG RTGGTVDADL ASRAWDHARR RAEDACVVLG SLHPSTPSLL QPFLQVIPVP
     TPNLAYTALS ALRPFLSCVT PANPTTYRHS SLSAKYTITL DGTITGFNLA LSGSGIDVQK
     GLLKVPAESG YRAFDVFYYL LTSASTPAER EFLDLKPASR YTLLSGSGTH NPPSYIPTAD
     DTAAAEDFRS ALKSIGIKGA SFRGLLSCLA GLLKLGETTG FLVDSDTLED MCEDVGALIG
     LEPDVLVNKC NSDDREVLIA GMYEALVDWV ISKANDAIAA ELRAGALTPD SSSGDEVSVT
     VVEIPGEALG KAVALRNVFD DTFGINAEMK EDGLEVAAAG SSVLKEMHLA VSQAEADLGI
     SGGPLSRERE HDRDRREGIL QKIGAEAESG GFLHTLLYPV NGEALNFGKR GRFDLGITLA
     SSRAWYQLSI HPTDDSPSTL SGLASPTSAW SAGAVSRQLR AWRLPEWANH RNRHLDFTAD
     FDVEEFVTRY SRLGCKDGMD GIESFLLERG WTNREVVIGR ERVWMRESAW WEAETILDLK
     PMPPSYSDEA AIGQHTNPFL SSYSVNAPDN ASAFFPPMGD GMSVLDSKDD LLDPVAANRA
     KSLAPTMART VQTIGGDYGL GPKGDPNKDQ YWDSDLGRFT GELDPEFGDP RNVESKKTSA
     GRQAWASLVW ALTWFIPSIF LRYIGRMKRP DVRMAWREKI VLVMLITLLN AFIVFYIVEF
     GRLLCPNFDK AWNDKEVGYH QGTNDYYVSI RGGVYDMTKF YKTQHSDTST QTDSTNMLPF
     AGLNLDAYFP VPLSVACPGL NVNTTVELQN NNTDAVVYST AVHYSGPQFQ TDSSSALYNI
     NWYSDTFLPK IKQYYKGDLV VTRGNVQSQA NDDDRIWVII DKKIYDLTNY FYTLTLMNNY
     PTYKFFPDEV SDLISGNPGS DITKQWGTTA AYQNSLNCMN NAFYVGKVDF RDTAKCQVNN
     YILLAFTIII CAVILVKFLA ALQLGSKRRP AAQDRFVICQ VPAYTEGEDH LRKSLDSLTA
     LQYDNKRKLI CVICDGMIVG GGNDRPTPKI VLDILGVDPK IDPPALPFRS VGNASEQLNY
     GKVYSGLYEC EGNVVPYIVV VKVGKESEQT KSKPGNRGKR DSQILLMQFL NRVHHRSPMS
     PLELEMFHQI NNIIGVDPEL YEYLLMVDAD TMVKEDSLNR LVAACANDAK IAGICGETSL
     ENEERSWWTM IQVYEYYISH HLAKSFESLF GSVTCLPGCF CMYRLRTADK GRPLIISDKV
     INEYSDCDVD TLHKKNLLSL GEDRYLTTLM TKHFPAMSYK FIPDAYAQTA APETWSVLLS
     QRRRWINSTI HNLAELVWLK DLCGFCCFSM RFVVFIDLFG TLILPATCVY LGYLIYRVAS
     GTGQFPLISI ILLAAVYGLQ AIIFIIKRQW QHVGWMLIYI IAYPIYSFVL PIYSFWNQDN
     FSWGNTRIVI GEKGDKKVVA IQDEGFDPRS IPLQRWDDYA AFNNLPGRRG NPGSYQEKGF
     EAGYTDDPAM MEMDDIHSTY SSVKPASTIL TGFPHMQQNP FMAPPRSPAP MGMNHRASTM
     TGLTQFKDQP VTVHGRNMSL MSLGSAARLK SPSPNHYYQD NQRSPYQSGY GGMQQSMSRP
     SLLGMANSRP ASTIMDFRTV PSAGPGDQEI VESIRLVLSE VDLETVTKKQ VRALVEQRLQ
     CEVPVGERRQ FLDKAIDNEL ANM
//
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