(data stored in SCRATCH zone)

SWISSPROT: B6HG04_PENRW

ID   B6HG04_PENRW            Unreviewed;      1567 AA.
AC   B6HG04;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   SubName: Full=Pc20g00570 protein {ECO:0000313|EMBL:CAP85386.1};
DE            EC=3.6.4.1 {ECO:0000313|EMBL:CAP85386.1};
GN   ORFNames=Pc20g00570 {ECO:0000313|EMBL:CAP85386.1}, PCH_Pc20g00570
GN   {ECO:0000313|EMBL:CAP85386.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85386.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85386.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782,
CC       ECO:0000256|SAAS:SAAS00572438}.
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DR   EMBL; AM920435; CAP85386.1; -; Genomic_DNA.
DR   RefSeq; XP_002562619.1; XM_002562573.1.
DR   STRING; 1108849.XP_002562619.1; -.
DR   EnsemblFungi; CAP85386; CAP85386; PCH_Pc20g00570.
DR   GeneID; 8307714; -.
DR   KEGG; pcs:Pc20g00570; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   eggNOG; COG5022; LUCA.
DR   HOGENOM; HOG000171839; -.
DR   KO; K10357; -.
DR   OMA; AESDMLQ; -.
DR   OrthoDB; 311886at2759; -.
DR   BioCyc; PCHR:PC20G00570-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01380; MYSc_Myo5; 1.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR002710; Dilute_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR036103; MYSc_Myo5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 6.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF50084; SSF50084; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HG04.
DR   SWISS-2DPAGE; B6HG04.
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00912434};
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00875240};
KW   Coiled coil {ECO:0000256|SAAS:SAAS01040361, ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Hydrolase {ECO:0000313|EMBL:CAP85386.1};
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:UP000000724}.
FT   DOMAIN        6     59       Myosin N-terminal SH3-like.
FT                                {ECO:0000259|PROSITE:PS51844}.
FT   DOMAIN       74    778       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   DOMAIN     1229   1498       Dilute. {ECO:0000259|PROSITE:PS51126}.
FT   NP_BIND     168    175       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION      656    678       Actin-binding. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00782}.
FT   COILED      913    940       {ECO:0000256|SAM:Coils}.
FT   COILED      948    989       {ECO:0000256|SAM:Coils}.
FT   COILED     1000   1076       {ECO:0000256|SAM:Coils}.
FT   COILED     1156   1176       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1567 AA;  179199 MW;  A790A584746C2CCB CRC64;
     MAHIYEVGTR AWQPDPTEGW LASEVKEKLE DGEKVQLIFE LENGETKTVE TTQSELQVDN
     NPKLPPLMNP AMLEASEDLT NLSHLNEPAV LQAIKLRYAQ KEIYTYSGIV LIATNPFARV
     DSLYVPQMVQ VYAGKQRASQ APHLFAIAEE AFADMLRDGK NQTIVVSGES GAGKTVSAKY
     IMRYFATRES SDQPGKYTTS RAEAISETEE QILATNPVME AFGNAKTTRN DNSSRFGKYI
     EIMFDDRTNI IGAKIRTYLL ERSRLVFQPL KERNYHIFYQ LVAGASDAEK QELGLLATED
     FEYLNQGGTP VIDGVDDKAE FEATRKSLAV IGVPKEDQTG IFRVLAALLH LGNVKITATR
     TDSSVSSTEP SLLRACEMLG IDATEFAKWI VKKQLITRGE KITSNLTQQQ ALVVRDSVSK
     FIYSSLFDWL VDKINRRLAT DEVLEQFKCF IGVLDIYGFE HFAKNSFEQF CINYANEKLQ
     QEFNQHVFKL EQEEYVREEI DWTFIDFSDN QPCIDLIEAK LGVLALLDEE SRLPMGSDEQ
     FVTKLHHHFA ADKQKFYKKP RFGKSAFTVC HYAVDVTYES DGFIEKNRDT VPDEHLEVLR
     NSSNPFIKEI LDTAAAVREK DSASMSSKPV AAAPGRRIGV AVNRKPTLGG IFKSSLIELM
     HTINNTEVHY IRCIKPNEAK EAWKFEGPMV LSQLRACGVL ETVRISTAGY PTRWTYEEFA
     IRYYMLCHSS QWTSEIRDMC HAILRKALGD EKQDKYQLGL TKIFFRAGML AFLENLRTSR
     LNECAIMIQK NLRAKYYRRR YLDARDSILT TQAFIRGFLA RQHAHEIRRT KAATTIQRVW
     RGQKEKKRYT QIRKNFILFE SVAKGFLCRR NIMDSINGNA AKVIQRAFRS WRQLRAWRQY
     RRKVITIQNL WRGKEARNAY KRLREDARDL KQISYKLENK VVELTQYLQT LKLENKTLVS
     QLDNYDTQLK SWRTRHNALE ARTKELQVEA NQAGITAARL EAIEEEMSKL QQGHTEAQAT
     IKRLQEEERI SREALQTANE ELERLKLLDA DHEKDKTALR QRISDLEEQL EVAKRSVPLN
     GMNGDGLPNG GAVQTPTPGL INLVSSKKPK PKRRSAGAER IETDRFSGAY NPRPVSMAVT
     PGSMATRQSA AISPGLESVE VELENLLSEE EDLNEEVAMG LIRNLKIPLP TSTPPPTEKE
     VLFPAYLINL VTSEMWNNGF VKESERFLAN VMQSIQQEVM QHDGDDAINP GAFWLSNVHE
     MLSFVFLAED WYEAQKTENY EYDRLLEIVK HDLESLEFNI YHTWMKVLKK KLYKMIVPAI
     IESQSLPGFV TSETNRFLGK LLPSNNNPAY SMDNLLSLLN GVYKAMKAFY LEDAIILQTV
     TELLRLVGVT AFNDLLMRRN FLSWKRGLQI NYNITRIEEW CKSHDMPEGT LKLEHLMQAT
     KLLQLKKATL NDIEIIQDIC WMLSPNQIQK LLNQYLVADY EQPINGEIMK AVASRVTEKS
     DVLLLAPVDM EDSGPYEIAE PRVITALETY TPSWLQTPRL KRLAEIVSAQ AMAQQEKLDW
     DNGVVEE
//

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