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Database: UniProt
Entry: M1WG40_CLAP2
LinkDB: M1WG40_CLAP2
Original site: M1WG40_CLAP2 
ID   M1WG40_CLAP2            Unreviewed;      1868 AA.
AC   M1WG40;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   31-JUL-2019, entry version 37.
DE   SubName: Full=Probable chitin synthase {ECO:0000313|EMBL:CCE31454.1};
GN   ORFNames=CPUR_05307 {ECO:0000313|EMBL:CCE31454.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE31454.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE31454.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE31454.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K.,
RA   Calie P.J., Fleetwood D.J., Haws D.C., Moore N., Oeser B.,
RA   Panaccione D.G., Schweri K.K., Voisey C.R., Farman M.L.,
RA   Jaromczyk J.W., Roe B.A., O'Sullivan D.M., Scott B., Tudzynski P.,
RA   An Z., Arnaoudova E.G., Bullock C.T., Charlton N.D., Chen L., Cox M.,
RA   Dinkins R.D., Florea S., Glenn A.E., Gordon A., Gueldener U.,
RA   Harris D.R., Hollin W., Jaromczyk J., Johnson R.D., Khan A.K.,
RA   Leistner E., Leuchtmann A., Li C., Liu J., Liu J., Liu M., Mace W.,
RA   Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K., Steiner U.,
RA   Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of
RT   the Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00782}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCE31454.1}.
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DR   EMBL; CAGA01000031; CCE31454.1; -; Genomic_DNA.
DR   STRING; 5111.M1WG40; -.
DR   EnsemblFungi; CCE31454; CCE31454; CPUR_05307.
DR   OrthoDB; 20724at2759; -.
DR   PhylomeDB; M1WG40; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0003774; F:motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
DR   CDD; cd14879; MYSc_Myo17; 1.
DR   Gene3D; 3.10.120.10; -; 1.
DR   Gene3D; 3.90.550.10; -; 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; IPR036037; MYSc_Myo17.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   SMART; SM01117; Cyt-b5; 2.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 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   Complete proteome {ECO:0000313|Proteomes:UP000016801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016801};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    892    911       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    932    951       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1205   1224       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1600   1620       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1626   1648       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1655   1678       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    784       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   DOMAIN      955   1016       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
FT   NP_BIND     105    112       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION        1     26       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      592    642       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      784    808       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1868 AA;  207158 MW;  12F952109C5662FF CRC64;
     MASTLPPLGG GSGGAHTQPS LPSLPAHLQS DTQITAHLAS RFHVSHPTAE LSSHALVCLN
     TYTSSSKGPD GGKPGSAMAG AEDMAERAWL RLGHRSENQA IVFLGESGSG KSTVRSHLLT
     ALLDKSSTPL SNKLSMAAYV FDTLTTTKTA TTPTASKSGL YYELQYDTSA TTNPILLGGK
     LLDHRLERSR IADVPTGERN FHILYYILAG TSSAEKTHLG LDDGVDGSKR WKYLGHPTQL
     KVGINDAEGF QLFKTALKKL EFPRSDVAEI CQILAAILHI GQLEFESTNN TSATGDDSGG
     FSHDGGNTST TVKNKDVLAI IAAFLGVSVG ELQSTLGYKT KTVHKERVTI LLDPVGARGH
     ANELARTLYS LLVAWILESV NQKVCAPEEQ IVNTISIVDF PGFAQQSATR STLDQLLNNA
     ATEAIYNLAL HNFFDRKAEM LESEEVSVAP TSYFDNSDAV KGLLKSGNGL LSILDDQTRR
     SRTDMQLLES LRKRFEGKNP AIEVGSATAK LPGSNFLTEN AMASFTVRHF AGEVDYPIKG
     LIEENGEVVS VDLLNLFNST KSEFVGRLFG QDVLQTVPHP NEKKTVMQAT ISSKPMRAPS
     VMSRKGGRGR GLPSQRRPQA PPLFDAGNNN VPDEAKSPKA SKVANKASID QGASGQFLSS
     LDNLQKAVTD PGTNTYFVFC LKPNDRRIAN QFDSKCVRTQ VQTFGIAEIS QRLRSADFSL
     FLPFGEFLGM ADSDTILVGS ERERAEMTIE ERRWPSNEAQ VGSTGVFLSE RRWMEVAHLS
     EGYSGSGGLA RYPQTSSDGY GNEGATPGDR DAFAASKEQL LSRGDTPLMY GEKGRPGYFD
     SDDARSEAGV SALGGGDMFK NFDTREQMAE RGNEKNLQEI EEYRDSPSRK RWVLTVFFLT
     WFIPDFLIRW LGRMPRKDVR MAWREKVAIN MLIWLMCLVA VFFIVVFPML ICPKQNVFTA
     AELSGHDGKD GNSAYVSIRG HVIDLGSFVN THYPPEPLVS KKSILNYAGK DVSALFPVQV
     SALCQGVDGS VNPQVTLDYK NTNMSGTPTL INSQDLNSRY HDFRYYTNDT RDDWYLEQLL
     YLKGNWGKGA IGYSPEYVSK LAGKNQKIAI IGSKVYDLSS YMDNRRLLRA KPGEQVNDDP
     KLADFLDSKV TDLFRTKAGQ DITKIWNALL LSPGVKARMQ TCLDHLFYVG NVDTRNSVRC
     QFAEYLILAV SIMLVSIIAF KFFAALQFGG KNVPENLDKF VMCQIPAYTE DEESLRRAID
     SAARMRYDDK RKLLVVVCDG MIIGQGNDRA TPRIVLDILG VSETVDPEPL SFESLGEGMK
     QHNMGKVYSG LYEVQGHIVP FLVIVKIGKP SEVARPGNRG KRDSQMILMR FLNRVHYNLA
     MSPLELEMYH QIRNIIGVNP TFYEFMFQID ADTVVAPDSA TRMVSAFIDD TRLIAVCGET
     ALTNAKSSFI TMIQVYEYYI SHNLSKAFES LFGSVTCLPG CFSMYRIRAA ETGKPLFVSR
     EVVEAYSTIR VDTLHMKNLL HLGEDRYLTT LLLKFHSKYK TKYLFNAHAW TIAPDSWQVF
     LSQRRRWINS TVHNLMELIP MAQLCGFCCF SMRFVVFIDL LSTVVQPVTI AYIAYLIVLV
     GTKGTVVPVT AFILIGAIYG LQAIIFILRR KWEMVGWMIL YVLAIPVFSF GLPLYAFWHM
     DDFNWGNTRV VAGEQGKKVV ISDEGKFDPD SIPRKKWEEY QAELWETQTS RDDTRSEVSG
     FSYGTKAQAA VSEYGLPSRP TSTTGFMAHH NPYESRNNSR MSLAPSELGQ LHMSQYGGSQ
     FFNPDDMVGL PSDDALLAEI RDILKTADLM TVTKKGIKQE LERRFDVPLD AKRAYINSAT
     EALLSGQL
//
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