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Database: UniProt
Entry: A0A0C3CC75_HEBCY
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ID   A0A0C3CC75_HEBCY        Unreviewed;      1902 AA.
AC   A0A0C3CC75;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-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=M413DRAFT_445249 {ECO:0000313|EMBL:KIM41201.1};
OS   Hebeloma cylindrosporum h7.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX   NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM41201.1, ECO:0000313|Proteomes:UP000053424};
RN   [1] {ECO:0000313|EMBL:KIM41201.1, ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RA   Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; KN831780; KIM41201.1; -; Genomic_DNA.
DR   STRING; 686832.A0A0C3CC75; -.
DR   HOGENOM; CLU_000192_0_2_1; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000053424; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd14879; MYSc_Myo17; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036037; MYSc_Myo17.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
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.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053424};
KW   Transferase {ECO:0000313|EMBL:KIM41201.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        910..929
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        950..969
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1209..1231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1607..1628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1634..1654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1666..1685
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..758
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1844..1899
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   REGION          637..659
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          764..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1820..1849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        808..823
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..855
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1902 AA;  214371 MW;  64CB518910F4D9EF CRC64;
     MNRQSSASMS VHQRLEAATD LSQLSSISDD IIVACLRERF MTDTIYTNIG TSSLVALNPH
     KYVSSNADSI LHKYAAEYRD SSDHQERLPP HIFQTANNAY YHMRRTTQDQ CLVFSGETGS
     GKSENRRLAI KSLLELSVSS PGKKGSKLAN QLPASEFVLE TFGNARTLFN PNASRFGKYT
     ELQFSDRGRL TGVKTLDYYL ERNRVSAVPS GERNFHIFYY LVAGASPEER QHLHLLDKTT
     YRYLGQRGTA AARPNGSRDD DALRFDQLKI ALKTIGFSKR HVAQTCQLVA AILHLGNLEF
     IIDRHRNEDA AVVRNVDVLE IVSDFLGIHP SALEAALSYK TKLVKKELCT VFLDPDGASD
     NRDDLAKTLY SLLFAWLNEH INQRLCKDDF STFIGLFDLP GPQNMSSRPN SLDQFCINFA
     NERLQNWIQK SLFEKHVNEY TLEGISRFVP QVPYFDNSEC IRLLQNTPGG LIHIMDDQAR
     RQPKKTDHTM VEAFSKRWGN HSSFKAGAVD RSGYPSFTVN HFNGAVTYSS EGFLDRNLDA
     INPDFVSLLR GAVDGLEGSG SINPFVKGLF SAKAIATQAH PRNEDTIVSA QQAVKPMRAP
     STRRKGPLKR MPTVKESIDI EENHTSPCVA GEFKAAMDTL LETIDETQPW YVFCINPNDS
     QLPNQLEGRS VKGQVKAVGL AEIARRSVNV FEVNMTPEEF CERYRDGLAG GGIAEGDVRE
     VIGQARTAFN LNEKDLVLGV HKVFLSQRGF HKFENQLRLH DVEEQKRNRV RDAEPDGGID
     PRHFNDPYAP YRSPNEELDA SPWNGNYDEA YGASNQHLPL NKSSPFQRAD LYEDDYEENK
     SGEDYEARSK FTSQRDDSVS HFGSESYAPS RNMFQNTDKR GLMEKEALAG EIQEGEVSEV
     LKESSARRRW VAICWMLTFW IPTPFLTYIG RMKRMDVRQA WREKLALNMI IWFICACAVF
     VIAVLGVVIC PTEHIYNSAE LASHSSTLSP NNVLTSIRGE VFDLTSVAET HRRVVGVVPV
     KSILKYGGQS ADGIFPVQVS ALCNGINGNV SPYVILDSKN NTDVNAQYHD FRVFTNDSRP
     DWYFERMVEM RYQARVGFVG QTPKEIRSAA SSGRSVAIYN GMIYDVTTYL TSPPAVRTPA
     GTVAPANTDV NFMHGSVLDL FKFNAGRDIT KQLDGLNIDR DILARQKVCL RNLFLVGKVD
     NRQSPQCLFA NYILLVLSVI MVAIIGFKFL ASINFSAARA PEDHDKFVIC QVPCYTEGDV
     SLRRTIDSLA QMKYDDKRKL LVVICDGMIV GSGNDRPTPR IVLDILGADP NLDPEPLSFM
     SLGEGAKQHN MGKVYSGLYE CAGHVVPYLV IVKMGKPTER ARPGNRGKRD SQMLLMHFLN
     KVHFNSPMNP LELEMYHQIK NVIGVNPSFY EYLFMVDADT TVDPLSVNRL ISAMIHDKKL
     LGACGETELA NAKQSLITMM QVYEYFISHH MAKAFESLFG SVTCLPGCFT LYRLRTPDTH
     KPLLIANQLI QDYSENRVDT LHMKNLLHLG EDRYLTTLLL KHFPRFKTQF IRDAHAYTVA
     PDDWKVLLSQ RRRWINSTVH NLGELIFLEQ LCGFCCFSMR FVVMIDLLST LTQPVTVAYI
     VYLVYLVAAL GKSIPTLSLV MIAAIYGLQA LVFIMRRKWD MIGWMIFYIL AIPAFSFFLP
     LYSFWKMDDF SWGQTRVVLG ESGKKMIVHD EGKFDPRSIP LKSWSDYENE LWDKESNHSI
     GSWVAPAKMK NEGYAESRTA SLYGRETYYE PQRSFSPAPS QLGMFPPPGY QSGRNTPQSP
     FMNTMQETGL LQPIASRPTT NYLDIPIPRT RTPDDDLLGS GGGGPSDIDI DRAVQDVLRS
     ADLNSVTKRE IRRQLEDHFG MDLSSRKASI NASIDRTLLN QN
//
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