ID A0A2T9YU02_9FUNG Unreviewed; 1637 AA.
AC A0A2T9YU02;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BB561_001576 {ECO:0000313|EMBL:PVU95808.1};
OS Smittium simulii.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133385 {ECO:0000313|EMBL:PVU95808.1, ECO:0000313|Proteomes:UP000245383};
RN [1] {ECO:0000313|EMBL:PVU95808.1, ECO:0000313|Proteomes:UP000245383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWE-8-4 {ECO:0000313|EMBL:PVU95808.1,
RC ECO:0000313|Proteomes:UP000245383};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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:PVU95808.1}.
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DR EMBL; MBFR01000046; PVU95808.1; -; Genomic_DNA.
DR STRING; 133385.A0A2T9YU02; -.
DR Proteomes; UP000245383; 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; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
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; 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:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR PANTHER; PTHR13140; MYOSIN; 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; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 3.
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 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|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000245383}.
FT DOMAIN 83..791
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1318..1571
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 671..693
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 906..933
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 963..1050
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 176..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1637 AA; 187693 MW; 5218EFBDC3408797 CRC64;
MSSDQLDILK YYSKGVKIFF QDNEHGWIQA TIDNKTIDEA KSSIVLTCLN ATGGKLEFSS
TFQQILDSKN AILPPLCNPP MLDGIDDLSN LSHLHEPAVL HNLRVRYEMG NIYTYSGIVL
VAMNPFARVQ LYSQDILEAY AGQVRGELEP HLFAIAEDAY QGMVRDNRNQ TIIVSGESGA
GKTVSAKYIM RYFASAHEDS RDSVRGESGV ISYIEEMILA TNPVLESFGN AKTTRNDNSS
RFGKYLEIEF NKANNITGAF IRTYLLERSR LVYQPLKERN YHIFYQLVAA LPDQQRQSLG
LKSSWKNYTY TNQGGGNTGI ISGVDDAKEF QATCESLQLI GVKSDQQWDI FKILAALLHV
GEIQFKEVGR SGSSVEEGDS GIDQVVQLLQ IDTAELKKCL TKKQITMRSE KIISNLSRAQ
SIVARDSMAK FIYSHIFDWL VVVINAALKA NCENDSRFIG VLDIYGFEHF EKNSFEQFCI
NYANEKLQQH FNRHVFKLEQ EEYQREQLQN WTFIDFNDNQ NCIELIEGRF GIMGILDEES
RLQQGTDETT LTKLYNQFAP DKPGAKKKVH DMDSKKETPS DYFARPRIMK PEFSVFHYAN
CVTYSIEGFV EKNRDTVSDE MQNLLRSSKF TFFTKIIEDP EPEEVVEQPK SRRIDSNPKK
PTLGTVFKKS LIDLMKTIEN TDSHYIRCIK PNEAKTAWGF DGVMVLSQLR ACGVLETIRI
SCAGYPSRLT KQDFVVRYSI LYTNIRNETD IDDAAKILMR NILKDESLYQ IGLTKVFFRA
GILAQLERNR TERLDKSALM LQKNYRRMKQ RRIYLKLRNA TITLQYSVKS FLAKKELQKK
IKEKAVSRIQ HLCRHYIACS LVNTKKSAVL KIQALAKSYL CYKNYRNLLI NSKAVKIQSL
FRGYISYKLE GKVVELTRQL QSQEEKSQML LEKSSALEID VGKWRLKYDD MVSNNAQMKE
EFETQYAAQI ENLKDKLDTA QSELEATREQ IETTRKELEE SQSNLNLSRE ELTNSKLEFE
KAEKALIETN EKLKEELEQT KQRLVDFESA MIAERAEDGG TTRRMMRRST ILVPTALKRG
EPRKWEAAAS YSTGYENAEY SKLASPPEMS INRRPSLTLP VVAGSRQYPN GLTPTSTFES
NELIYNHRRN SFGGSKRSTS IDQIFEKGFK TEDNKGNNPA NENKQRTKGV LEQLKNDLKR
STISGADMQN YAKLLARMGE SEIGFDEDFI LRSEDEVRAM LESDDGLFSE ILNELISNLE
VPIPNLDIEY TPPELLFPAH LIGLCVIKMF QFNLSKRIDK LLVSCISLIQ KKTMTFESDF
SAAFWLSNVF ELLSIVKTSM TERKATGYEY VESERAMTEG MQFLESLLSD IYFGWAKNLQ
RRFIKLIIPG VVESEELPGF TANDSSFFNR IIGSVNKESV VKIEHILNFF NNVWKIMEFY
YVDVAIMNQV MSELLCTIGV TAFNNIIMRR NFCSWKRGMQ IQYNLTRIEE WCKSHDVSDH
TGNLDRLLQL VKLLQLQKST EQDIEIMFEV CDLLNPAQIK KILTIYTVSD YESPILGPLM
PEINRRAALT EKTDKILLDT NDMNDQVLYL TARKVSVIET LIPSDLRLFR LRALVESQTD
EDNASSGNIQ KTYTVES
//
