ID W6QIA8_PENRF Unreviewed; 2398 AA.
AC W6QIA8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Prefoldin {ECO:0000313|EMBL:CDM29307.1};
GN ORFNames=PROQFM164_S01g003119 {ECO:0000313|EMBL:CDM29307.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM29307.1};
RN [1] {ECO:0000313|EMBL:CDM29307.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM29307.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; HG792015; CDM29307.1; -; Genomic_DNA.
DR STRING; 1365484.W6QIA8; -.
DR OMA; QRAMDIE; -.
DR OrthoDB; 1094820at2759; -.
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:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}.
FT DOMAIN 110..160
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 164..858
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..759
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1457..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2257..2279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2367..2398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 936..970
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1009..1261
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1308..1431
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1608..1642
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1717..1785
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1948..2039
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2082..2179
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 50..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 257..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2398 AA; 276029 MW; 476268CF553196B6 CRC64;
MLPSQLNGSP KRASLFARPS SSQGTHSPHT RPKSAIITPS NALESARGHL RNTSVSQLSP
SLSLSGNRER SNSAKNSPSS GTFAPSFIKS EELRRGADQI RGLEGDNDFS GNKYVWIRDP
QKAFVRGLVL EEFEGGRLLV QTDDGDQQEL DADQVDKVNP AKFDKADDMA ELTHLNEASV
VHNLHTRYQS DLIYTYSGLF LVTINPYCPL PIYTNEYIKM YKGRGREETR PHIFAMADEA
FRNLVEEGQN QSILVTGESG AGKTENTKKV IQYLAAVATS DTPYGRSGAK QLTGLSQQIL
RANPILEAFG NAQTVRNHNS SRFGKFIRIE FSRAGQISGA LIDWYLLEKS RVVKPNPNER
NYHVFYQLLQ GADRETREKL LLADLQIEDF AYTRDGNDSI VGVSDQEEWN SLIEAFHVMN
FDDEDQLCIL RTIAAVLHLG NVSVAKASMR ADQATLAPEG YSSMEKACYL LGIEAEAFVK
GLLHPRVKAG REWVEKVQTP DQVRMALDAL SKGIYERGFG NLVARINGQL GRSMASDDNY
FIGVLDIAGF EIFDNNSFEQ LCINYTNEKL QQFFNHHMFV LEQEEYAREQ IEWQFIDFGK
DLQPTIDLIE LTNPIGIFSC LDEDCVMPKA TDKSFTEKLH SLWDRKTPKY HASRLNQGFI
LTHYAAEVEY NTSDWLEKNK DPLNDNITRL LAASKAPHVA NLFSDCADSE EDGGNHPRSR
VKKGLFRTVA QRHKEQLSSL MAQLHLTHPH FVRCILPNHK KRPKMLHAPL VLDQLRCNGV
LEGIRIARTG FPNRLPFTEF RQRYEVLCQD MPKGYLEGQT IARTMLAKLG MDRGWYRVGR
TKVFFRAGVL ADLEEKRDQL IRTIMSKFQS LARGFVQRRI SNKRLYRAEA TRIIQQNFHA
YLDLKGSPWW RMFSRMKPLL GDTRNAKEVK KRDDKIQQLE IKMKQDLAER NKLDEERRRT
EIEIQKIQHT LESERALALD KEEIFKRLQY REVELADKLS GAIADQEGLE EQLDELVFAK
RKIDDELQLR ITQLEQAGLI IQQLESEKNS LHSRVKELDI KLSETEAQFS GKDLQIQELG
QEIKILQSHL SLKDRKLQDL EAKLLKTDQD LDIKLANTSK ELDKSKKQIR DVTEENRSIR
DQIAELSSTS TSYEELLRRK ESEIAVLRND VQIHEEEKRS IESEKISLAA RHDNMQSKLR
EVQAERDAMR SEQRQLQREA ADLKNLLENK RSEDAEAGQS RKLLEEQIND LKHHLFQAQA
DLSRERQSRD DVQMLSEHNL ALLTQKYETL NDSKITIEKE MYIQQDSLRR ATEARVTAET
TKKELQSELI KLRERFTDAE TARMNAEAEI ERKIMSQAEE RMTSSRKDLE EKARQLEEVE
TERSQLSARI QELMHSISES ENFRLRHDQH KERLERELVT LRGRLTASEN DNKSLLTKIQ
QKNLDIARSN SKASDNNRLR LTTLQKEKSR LDEETKRLSR QLEDSQVMIR SLEKQKEKLS
LSLEDLNHEV NREHKTSRNA EKAASAANLQ LAEANRKLET ERQLRNQAQA NTRQTQGTLD
RANKEIEDLH RQLILLHKVF EPEATEPAQS WEAVQPHLSK KVDLAQVLET VQNRLGVTEE
KYARAESQLA EMRRRHGDEM KELDAKYSSS KRALLEEIDQ NEVTNNRTPA HLRKNSENAA
KKYSNPTTPN RRYNVFEAPN DSARSDRTVD TQAYQRRMDT AAELEELQNK LQMTEMQNKH
LQSQLGRSTP TADIWQDESP SIRRMQLLER ENGRLHDQLD DSSKKVSSLE RSIRSGELSL
RDVQAKSHEE LYDLINSQEQ SRRSLLKVHN ETMTEFGDAK AQFEKLKRAR ATLEVELRDA
LSEAQELQVG REQDAVSRNQ LLQEFSDLQI RLDAESSRSA DLESSLMLYK SRSDEYFNKL
EQAEIAVMKA SRAEQFAKSQ GQEAEETCAQ IMSERKEMDA LVEDLQRQAQ SLEARMEDQA
AELQGALQAK QRLQNELEDY RNQRAIDLED KETSMEQTRQ KYQREFSTLN NELEMERERV
LNGRGETSRL REELENLRSK WDNEVLNSST WAKEKSRMDV VLQDVTNSRD EAVNAHNEAQ
SKVVSLLSQV RTLRTSIEDV QAERDMLLKD KKMLEGRLAE AGDRLEDLAK GESPSMRNAA
SMDRELLELK SRIAQQEDVS AAAVGKMRRA DALATEMQKE VTAEREANAQ LFKEKAAVEK
QLKEAQLRCL DLETKSYSSG SQDVRFLHKR IKELETHLEE QESKHSSEQR SLRNVDRTVK
DLQSQIDRRD KVNTQLTDEV NRARDKIERL LRNIEEIQHN DSDAQLLARR AERDLREERE
KALRLERELE GWKALRVERG SVIGRGVTFS DTGSRRGSGV YGSNDIPQRQ PSNTKGFL
//
