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Database: UniProt
Entry: A0A0D1W5A1_9EURO
LinkDB: A0A0D1W5A1_9EURO
Original site: A0A0D1W5A1_9EURO 
ID   A0A0D1W5A1_9EURO        Unreviewed;      1875 AA.
AC   A0A0D1W5A1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   31-JUL-2019, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIV83855.1};
GN   ORFNames=PV11_05844 {ECO:0000313|EMBL:KIV83855.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV83855.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV83855.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV83855.1,
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.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN846952; KIV83855.1; -; Genomic_DNA.
DR   EnsemblFungi; KIV83855; KIV83855; PV11_05844.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000053599; 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; 3.90.550.10; -; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053599};
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:UP000053599};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    892    911       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    931    951       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1199   1221       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1597   1618       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1624   1645       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1652   1675       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    713       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   DOMAIN      955   1014       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
FT   NP_BIND      99    106       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION        1     22       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      597    650       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      804    830       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      859    879       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    608    648       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1875 AA;  207362 MW;  F203851B7BE0F35F CRC64;
     MAGRANLPAH AQASLPGLPS HLQSDTHLTA HLASRFHVSL PTAKLSSQAL ICLNTYTSST
     RGPNGETEGS AMGEAEDLAR RAWARLGSRA EDQAIVFYGE SGSGKTTVRS HLLSSFLSFS
     STPLSSKLSL AAFVFDTLTT TKTTTTQTAS KAGLFYELQY DASSSIPTLI GGKLLDHRLE
     RSRISHVPTG ERSFHVLYYL LAGTSAAEKS HLGLNGHTNV TTSGNGLGRS ASISQKRWRY
     LGHPTQMRVG INDAEGFQHF KTALRKLEFP RAEIAEICQV LAAILHIGQL EFGIGQATLT
     AAEESGGYSH EGGESVTVVK NTETLAMVAA FLGLSVQDLE ESLRYKTKTI HRERVTVMLD
     SKGARENADE LATTLYSLLV AYIMEGVNQR ICAAEDAVAN TISIVDFPGF ADHPSTGSVL
     DQLLNNAANE SLYNICLSSF FERTSEMLES EEVSVPATSY FDNSDAVRGL LKHGNGLLAI
     LDDQTSRGRT DVQFLESIRK RFENKNKAIS VSSATSTIPG SNFATTNLAA SFTVRHYAGE
     VDYPVNKLVE ENGDVVSGDL MNLMKGTKSE FVGSLFGQEA LNTVSHPAER TAIVQAQVSS
     KPLRMPSVSR KKHNELRRMA SRRADRSPAP PDEEDPMPAL EEQRSRRTKS IAGLTQGAAA
     QFLSALDNIA KSLTAPNVNN YFVFCLKPND RRIANQFDSK CVRQQIQTYG IAEISQRLRM
     ADFSIFLPFG EFLDLADAET TTIVGSDAEK AQLVLDRKHW LANEARVGNT GVLLSERCWA
     SIALTGFHNA AYFGGEVARL SRPGSADPFS DSKARLLPPG GGTPGSFGEE TKGGGYFGSR
     ELDSRSDAGA SAFNSGDMFR NLETKEELAE KANKKKMQEV DVVPVSGSRK RWLALVYLLT
     WLVPDFAIKW FGGMKRKDVR IAWREKFAIN LLIWLMCGFV VFFIVVFPQL ICPKQNVFSA
     AELSAKDGKG SDGSYIAIRG NVFDLGAFMP SHYPSIIPQS SLKKYAGVDA TSLFPVQVSA
     LCQGTSGSVD PSIQLDYSQT NTSGSASVIS STDTNAKYHD FRYFTNDSRP DWFTEQMIML
     KSNFRKGDIG YTPKYVKTLA GKSKSIAILN SRIYDFTAYN AGGRTTRAPP GQTVPDNVDT
     NFMDQSVVDL FTQRSGQDVT KYWNALTLDA DVKSRMQTCL DNLFFVGVTD TRNSAQCLFA
     QYILLAVSIL LCSVIGFKFF AALQFGGRNM PENLDKFIIC QVPAYTEDED SLRRAIDSAA
     RMRYDDKRKL LVIICDGMII GQGNDRPTPR IVLDILGVTE TVDPEPLSFE SLGEGMKQHN
     MGKVYSGLYE VQGHIVPFMV IVKVGKPSEV SKPGNRGKRD SQMVMMRFLN RVHYNLPMSP
     LELEMHHHIR NIIGVNPTFY EFMLQIDADT VVAPDSATRM VASFLRDTRL IGVCGETSLS
     NAKSSFITMM QVYEYYISHN LTKAFESLFG SVTCLPGCFT MYRIRAAETG KPLFVSKEII
     NDYSEIRVDT LHMKNLLHLG EDRYLTTLLM KYHNKYKTKY IFHAHAWTIA PDSWTVFMSQ
     RRRWINSTVH NLIELIPLQQ LCGFCCFSMR FVVFLDLLST IVAPVTVAYI VYLIVLLATS
     SSVVPLTAFI LLGAIYGLQA IIFILRRKWE MIGWMIVYIL AMPIFSFGLP LYAFWHMDDF
     SWGNTRLVTG EKGKQVLISD EGKFDPNSIP KKKWEEYQAE LWEAQTQRDD TKSEMSGYSY
     GTKSYHPAAS VYGGGYDTQH LIPHSRSASQ LDLHQSMYGG GYNQSRMSLA PSETLGGEML
     PSGRSVADME MADLTGLPMD DAILNEIRDI LSTADLMTVT KKGIKMELER RFNVNLDAKR
     AYIGSATEAI LSGQL
//
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