ID A0A0B7MUA0_9FUNG Unreviewed; 1618 AA.
AC A0A0B7MUA0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=PARPA_00114.1 scaffold 339 {ECO:0000313|EMBL:CEP06860.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP06860.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP06860.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP06860.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; LN718796; CEP06860.1; -; Genomic_DNA.
DR STRING; 35722.A0A0B7MUA0; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000054107; 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 CDD; cd15480; fMyo2p_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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; 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; 5.
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; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
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|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT DOMAIN 86..784
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1248..1555
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 660..682
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 992..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1618 AA; 185269 MW; 92EF92C73669DBC9 CRC64;
MDSLSSGVAQ AVQVYTKGTK AWFEDEDEAW VSASVLTKEE SGTGVKIVFQ DDNDEKREHV
FESTFALLEK QKGANLPPLR NPPKLENTED LTNLSYLNEP SVLNTIRARY FQRNIYTYSG
IVLIAANPFA HVALYEPDII QQYSGKRRGE LEPHLFAIAE DAYRCMVREK SNQTVVVSGE
SGAGKTVSAT HIMRYFATAD DQESGKTKNA SEGMTEVEEQ IMATNPIMEA FGNAKTTRNN
NSSRFGKYIE IQFDNRCNIV GAKIRTYLLE RSRLVYQPET ERNYHIFYQL CTGAPPNESK
DLELGDWSKF HYLNQSGVGS IPGVDDAAEF ELTQKSLSLV GISVENQWSI FKLLAALLHI
GNIEIGGKQD ATLSDDQAAL ITATKLLGIK TSEFKKWLLK KQIITRNDKI VKNLNPAQAT
VVRDSVAKYI YASLFDWLVK IVNDSLSCQE EGLVRTFIGV LDIYGFEHFK KNSFEQFCIN
YANEKLQQQF NQHVFKLEQE EYVKEKIDWK FIDFSDNQPC IELIESKLGI LSLLDEESRM
PSGTDQGFIN KLYANFGPDS KYKDYFKKPR FSNSAFTVVH YAHDVEYDGE GFIDKNKDTV
PDELLALLQN AESIFLKDML STATAAASDA SQEAKPSPVK KVGMAIAKKP TLGSIFKLSL
ISLMDTISQT NVHYIRCIKP NEAKVAWGFE PNMVLSQLRA CGVLETIRIS CAGYPSRWTF
EDFADRFYAL VNSQYWDPNG SPDINKLCRV ILETYITDAD KYQIGQTKIF FRAGQLAYLE
KCRRDRWNEC TILLQKNMRR FIVRIGYLRK LDLISRLQRV ARQKVGAKRL QLARQDKAAL
KIQTEWRRYI QRRRYLRQKD FVVHLQAACR SLLARKIFAH IKEHFAAIKI QSLMRGWRVR
KEFIAKRQLA VQVQTCVRRR LARKQLLQLK QDARSANHFK EVSYKLESKV VELTQSVTQH
KDEKDQLRLK ADALELQVKE WSEKYEKLGE KAKSLQQSAD TSELERQLES LQGERNGIQA
DYKTSLERIK KQDVEIARLN QELERHKDEI AKLKQSQNQQ QQQQQQQRSR SPVSPAPGTT
SFAADEEVAE LKSQIVALKA QLSQSLKNHP KRQASINAYR TLSPQRGGGG DRRGASPDYN
RNRSPSADPR GRSPSALAVR RNSSVDRRRP EPTTSQPTKV IYAEPEQMVP KEIGQRGSLD
AEKIGNPEEA LTTLLQQDSE TLEEEIIQGL LQSLKIVPPE LQKLPAREEV VFPVHIISKV
VTQMWRLGCL SESERLLFRA MDTIQKDCLS FAGEDTIVPC SYWLSNTHEL LSLIYSVEQE
LEREMHYNSV HGRRAVGWHD FEKLVSTVKF ELQCLQDNIY HHWLSELKKK LNKMAIPAVI
ENQSLPGFIT SDSNRFFGKL LTNQPAYSMD DLLNFLNRIH RTMKSYYVEP YVVEQVLTEL
LKLIGITTFN DLVMRRNFNS WKRAMQIQYN ITRLEEWCKA HDVSEATNQL EHLMQATKLL
QLKKATLEDI KIIYDVCWFL APTQVQKLIQ NYIVADYEDP ISVEILRAVA SRVSSSDTGD
VLLLDNVSIE DSDYDQPEPH NVVANSYIPS YLNLQNVQKL IALVNLNEKH KPQRMDSI
//
