ID A0A0A2L1W3_PENIT Unreviewed; 1567 AA.
AC A0A0A2L1W3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Dilute {ECO:0000313|EMBL:KGO73141.1};
GN ORFNames=PITC_003300 {ECO:0000313|EMBL:KGO73141.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73141.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO73141.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73141.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO73141.1}.
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DR EMBL; JQGA01000836; KGO73141.1; -; Genomic_DNA.
DR STRING; 40296.A0A0A2L1W3; -.
DR HOGENOM; CLU_000192_3_1_1; -.
DR OMA; EIMFDDR; -.
DR OrthoDB; 1094820at2759; -.
DR PhylomeDB; A0A0A2L1W3; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
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:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd15480; fMyo2p_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR046943; Fungal_Myo2/2A_CBD.
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; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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;
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 6..59
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 74..778
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1229..1498
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 656..678
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 913..1076
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 168..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1567 AA; 179179 MW; 7CD3EA2BA8C3CED0 CRC64;
MAHIYEVGTR AWQPDPTEGW LASEVKEKLE DGEKVQLIFE LENGETKTVE TTQSELQVDN
NPKLPPLMNP AMLEASEDLT NLSHLNEPAV LQAIKLRYAQ KEIYTYSGIV LIATNPFARV
DSLYVPQMVQ VYAGKQRASQ APHLFAIAEE AFADMLRDGK NQTIVVSGES GAGKTVSAKY
IMRYFATRES SDQPGKYTSS RAEAISETEE QILATNPVME AFGNAKTTRN DNSSRFGKYI
EIMFDDRTNI IGAKIRTYLL ERSRLVFQPL KERNYHIFYQ LVAGASDAEK QELGLVAAED
FEYLNQGGTP VIDGVDDKAE FEATRKSLAV IGVPQEDQTG IFRVLAALLH LGNVKITATR
TDSSVSSTEP ALLRACEMLG IDATEFAKWI VKKQLITRGE KITSNLTQQQ ALVVRDSVAK
FIYSSLFDWL VDKINRRLAT DEVLEQSKCF IGVLDIYGFE HFAKNSFEQF CINYANEKLQ
QEFNQHVFKL EQEEYVREEI DWTFIDFSDN QPCIDLIEAK LGVLALLDEE SRLPMGSDEQ
FVTKLHHHFA ADKQKFYKKP RFGKSAFTVC HYAVDVTYES DGFIEKNRDT VPDEHLEVLR
NSSNPFIKEI LETAAAVREK DSAAMSSKPV AAAPGRRIGV AVNRKPTLGG IFKSSLIELM
NTINSTDVHY IRCIKPNEAK EAWKFEGPMV LSQLRACGVL ETVRISTAGY PTRWTYEEFA
VRYYMLCHSS QWTSEIRDMC HAILRKALGD EKQDKYQLGL TKIFFRAGML AFLENLRTSR
LNECAIMIQK NLRAKYYRRR YLDARDSILT TQAFIRGFLA RQHTHEIRRT KAATTIQRVW
RGQKERKRYT QIRKNFILFE SVAKGFLCRR NIMDSINGNA AKVIQRAFRS WRQVRAWRQY
RRQVITIQNL WRGKEARNAY KRLREDARDL KQISYKLENK VVELTQYLQT LKLENKTLIS
QLENYDAQLK SWRTRHNALE ARTKELQVEA NQAGITAARL EAIEEEMSKL QQSHTEAQAT
IKRLQEEERI SRDALQTAND ELGRLRLLDT EHEKDKTGLR QRISDLEEQL EVAKRSVPLH
GVNGDGLPNG GAFQTPTPGL INLVSSKKPK PKRRSAGAER IDTDRFSGAY NPRPVSMAVT
PASMAARQMA AMSPGSESVE VELENLLSEE EELNEEVTMG LIRNLKIPLP TSTPPPTEKE
VLFPAYLINL VTSEMWNNGF VKESERFLAN VMQSIQQEVM QHDGDDAINP GAFWLSNVHE
MLSFVFLAED WYETQKTENY EYDRLLEIVK HDLESLEFNI YHTWMKVLKK KLYKMIVPAI
IESQSLPGFV TSETNRFLGK LLPSNNNPAY SMDNLLSLLN GVYKAMKAFY LEDAIILQTV
TELLRLVGVT AFNDLLMRRN FLSWKRGLQI NYNITRIEEW CKSHDMPEGT LKLEHLMQAT
KLLQLKKATL NDIEIIQDIC WMLSPNQIQK LLNQYLVADY EQPINGEIMK AVASRVTEKS
DVLLLAPVDT EDSGPYEIAE PRVITALETY TPSWLQTPRL KRLAEIVSAQ AMAQQEKLEW
DHGMLEH
//
