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Database: UniProt
Entry: A0A139H2Y6_9PEZI
LinkDB: A0A139H2Y6_9PEZI
Original site: A0A139H2Y6_9PEZI 
ID   A0A139H2Y6_9PEZI        Unreviewed;      1850 AA.
AC   A0A139H2Y6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   31-JUL-2019, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXS96728.1};
GN   ORFNames=AC578_154 {ECO:0000313|EMBL:KXS96728.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS96728.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS96728.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS96728.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana
RT   suggests a link between parallel evolutionary changes in
RT   Pseudocercospora fijiensis and Pseudocercospora eumusae and increased
RT   virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXS96728.1}.
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DR   EMBL; LFZN01000165; KXS96728.1; -; Genomic_DNA.
DR   EnsemblFungi; KXS96728; KXS96728; AC578_154.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000070133; 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; 3.40.850.10; -; 2.
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; 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; 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   ECO:0000256|SAAS:SAAS01194079};
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00875240};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070133};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00874053};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS01033784};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00874078};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    880    898       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    918    937       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1194   1213       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1583   1606       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1618   1637       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1649   1669       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    775       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   DOMAIN      945   1004       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
FT   NP_BIND      95    102       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION      586    640       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    612    631       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1850 AA;  206120 MW;  3222475EFEB885F1 CRC64;
     MTSVPTNQQN LAALPAHSMS DTHITSHIAS RFHSHLPITT LSSQGYISVN TYTSSTKGPN
     GAKEGSAMGA AEELASRMWT RLGARQENQA AVFLGESGTG KTTIRSHLLS SLLAYSSTPL
     SKKLSFAAFV FDTLTTTKSV TTPTASKAGL FFELQYDTTS SLHPTLIGGK VLDHRLERSR
     VASLPPGERN FHVLYYLLAG TSPAEKEHLG LELGTHSGVA NRTSMGGSAK RWRYLGHPSQ
     LKVGINDAEG FQHFKTALRK LEFPREEIAH LCEILAAILH IGQLEFMTSQ ATTPAPDESG
     GYGTEGGEEI TVVKNKDTLA AVAAFLGVSD KVLEQSLGYR TKILHRERVT IMLDPKGARE
     NADELARTLY SLLVALVMEK INQRTCAIEE SVANTIAIVD FPGFAQTSST GSVLDQLLNN
     AANESLYNFC LQSFFERKAD LLETEEVQVP ATSYFDNVDA VKGLLKSGNG LLSILDDQMR
     RGRSDMQLLE SLRKRFEGKN PAIEVASSTI TLPGNNFATP NASAGFTVKH FAGEVEYPVE
     GLLEENGEVI SGDLMNLVNS STSPFVAELF GQEALNKVLH PKDRNAVTQA SVASKPSRMP
     SMAKRKGGRP QRQRRGVFDD DADRSSDEGT KSFSRLPKPG LDAQQGAAAQ FLSSLENITK
     SLTLTNTNSY FFFCLKPNDR RIANQFDSKC VRTQIQTLGI AEICQRLKNA DFSIFMPFGE
     FLGTAEGDVS VVGTEREKSE MILDDKSWPS NEARVGSTGV FLSERCWRQI TRAPELGEVP
     VPYGDDGYGN SGMLTPIDAK KGFGDSKVQL LQTPGSGYLD DKAAGYFGSR DLDAKSEAGA
     SAFREGDMFR NLETRSQMLE KGNEIKAAEI EEKPLSGSRL RWLILVYFFT WWVPDFAVRY
     IGRMPRKDIR MAWREKLAIN LIIWLSCAFV VFFMVGFPRI ICPTQHVYSL EELSSYNGKG
     SHKAYIAIRG VVFDLSAFMP AHYPSIVPES ALKKYAGTDS TNLFPVQVSA MCQGRNESGI
     DPAVQLSYVT YNYSGSTNAI SATDPNAQYH DFRWATNDSR PAWFIEQMIF LQGHYWKGNV
     GYSPQYLKTL ADKSNYIAYI NGRVYDFTDY IAGGRAPQYP PGVDRPSTAP NSNFMDDRVV
     DLFQQRSGQD VTKYWLALNL DSGLRARMQT CMNNLFYVGN VDTRSSPQCQ FAKYILLAIS
     LLLVSVICFK FLAALQFGKK NVPENLDKFI ICTVPAYTED EDSLRRAIDS AARMRYDDKR
     KLLFIVCDGM IIGQGNDRPT PRIVLDILGV PETVDPEPLS FESLGEGLKQ HNMGKVYSGL
     YEVQGHIVPF IVIVKVGKPS EVSRPGNRGK RDSQMILMRF LNRVHYNMPM TPLELEMHHQ
     IRNVIGVNPT FYEFLLQIDA DTVVAPDSAT RFVSAFVNDT KLIAVCGETA LTNAKASMIT
     MMQVYEYYIS HNLTKAFESL FGSVTCLPGC FSMYRIRAAE TGKPLFVSRE IVNDYSEVRV
     DTLHMKNLLH LGEDRYLTTL LMKYHSKYKT KYIMRAHAWT IAPDSWTVFM SQRRRWINST
     VHNLIEVIPL SQLCGFCCFS MRFVVFLDLL STIVQPVIVG YIIYLIVEVA RNPSTVPITA
     FILLGAIYGL QAIIFILRRK WEMVGWMIIY MLATPVFSFF LPLIAFWHMD DFSWGNTRMV
     TGEKGKQVIV SDEGKFDPDS IPKKKWEEYQ AELWDAQTQR EDTRSEISGI SYATKSWHPA
     ASEYGYQSQH HMSQLTVPHM HPNASRMSLA YSDNGMGMPR ALSAADIDMA DLPSDDAILA
     EIRQILSTAD LMSVTKKSIK AELERRFGVN MDAKRQYIGS ATEAILSGQL
//
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