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
//