ID A0A067CKI7_SAPPC Unreviewed; 1794 AA.
AC A0A067CKI7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Myosin {ECO:0008006|Google:ProtNLM};
GN ORFNames=SPRG_05632 {ECO:0000313|EMBL:KDO29680.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO29680.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO29680.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO29680.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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; KK583205; KDO29680.1; -; Genomic_DNA.
DR RefSeq; XP_012199738.1; XM_012344348.1.
DR STRING; 695850.A0A067CKI7; -.
DR EnsemblProtists; KDO29680; KDO29680; SPRG_05632.
DR GeneID; 24128021; -.
DR KEGG; spar:SPRG_05632; -.
DR VEuPathDB; FungiDB:SPRG_05632; -.
DR OMA; GKCQSIL; -.
DR OrthoDB; 68658at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd14892; MYSc_Myo31; 1.
DR CDD; cd00821; PH; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 4.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 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 Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR025939; Aida_C.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF845; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14186; Aida_C2; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00015; IQ; 18.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS51911; C2_AIDA; 1.
DR PROSITE; PS50096; IQ; 12.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW 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:UP000030745}.
FT DOMAIN 62..762
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REPEAT 1289..1309
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1409..1508
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REPEAT 1539..1577
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1578..1610
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1645..1794
FT /note="C2 Aida-type"
FT /evidence="ECO:0000259|PROSITE:PS51911"
FT REGION 638..660
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1319..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1794 AA; 203519 MW; 5CA80CD37491B091 CRC64;
MAAKKHRREG EKVWCPDPRN VWQLGSIVED DGESLFVLTP DDNEEHKFAV TQTHPFDVSH
AQLLPNVSDM DNLHEAPLLD LLRRRYEQDL IYTFTGDILI SINPYKNIPL LYNFPEIDSL
SKQENPAPHV FVTADGAYRA LQKDGKCQSI LVSGESGAGK TEASKYIMRY LANISQSGKG
AAAANGGGSS VEQCVLQSNP LLEAFGNAKT IRNDNSSRFG KFIKINYNRN GTISGASTSH
FLLEKSRIVG CAENERNYHI FYQICSGLSA DERAALYITK AEDYEFLNQG NCITVPEVND
KKCFKELVDA MAIMGIDAET KRTIFALVAA VMHMGNLRFT ENAKMEAQCA DMNQVNQLAS
LMKVAPKDLQ FALCMRTMSA GTRGSVAEIA LSAVDAVKSR NGLAKAIYSA LFDWLVDRIN
AATAQITGAS TERVMEGSPG RFIGILDIFG FEILQANSFE QLCINYTNEM LQQQFNEHVF
VYEQEVYVEE GIDWSKLSFQ DNIPCLELIE KKPLGILILL DEQAMLGRRG SDEKFIQKLH
QTHEKHPNYI KPRFGNEQFI LKHYAGQVTY NVAGFLDKNN DSLHNDLIEL MNSSQLELLK
VLFATPAPAK DEGPKLKRAS MTKMTGTMTV GRKFREQMAE LMAQLHTTQP SFVRCVKPNN
IRFPTGWNAE LILNQLIYLG VMETVRIRRS GFPVRRTFDE FVDKYKLLEK VYSVRAKKVA
STNKEKCEMI LSQALQRENW QLGHKKVFMR DSQLRVLDAV VRKVRIDAAI TLQKYARRQL
ARKRYTKQRR GIIALQALVR MHQARRRFVV LRRRITCLNS HVRKWLARRR FVRIRKAIVR
VQACVRGRRA RKRVAYMRAA PKAATTIGKH MRRYLARKHY LHAKASATRI QSVVRMHLAR
TRFLRLRKAM ILVSKNIKRF VTRRHYKRMQ VAAIALHAVG RGFLARLKYG KKARLRAQLR
ARAQTTIARM VRGYLGRLHY RHARHLIVIV QARVRANRVR TAYLQGRQAT INSQAMIRRS
LARRKFLKEK RMATRLCAFG RMIIARRQYL LAKRRIVLVQ SLVRRYLQGK HYRNIRKQFV
KIQACWRRKQ CVAQYQKTRR AIIVIQSFGR MIPARRQLLV SQAAATRLTS VVRMFLARQA
YLRNKKRIVA IQSVARQWMA RKRYVVTRQR IIRVQAQIRS LLARKVMDKQ RRGMMRVILV
IKKYLARIRL QKKIKLMFAA AQAFDLTTIL RLSQDKDIPN STLVRVRDKS NYLRSLVHIA
AINCDLNLAR FVLSEIPNME DQVISKDTLG NTPLHYAARL AHLDMVKLLA KIANRIQAPP
PVPTPTSSPV GASPANSKDQ SPDAMLRKNS SFGTPRSPGL RSPSIGGIMG GAVPPTPQQK
NNRRKLVSSA SQMPAMSTAP IELPPDMTKV IKAGPLRMAS GAKMASKRHV VLDPVAIAAY
KTANDRIPVK ILELGDATLR RASTIEHCFE IISPRLKSHT NLTGVLSFVA DTEAEVHEWM
LALREINGMR IATTVPPNHN MICIDMLQRK EFVNSQNNHH EAPLHLAVQN SEDEGFEAVK
TAVWLIENDA DINAKDTLGN TPLHYAVIQE RDDLIESLLK KGALTTIRNN AGDTPVDLAN
DESMRELFAP GAVVAVPADR SLLPRPSGPL KVRDGTYVSV LLSAVAIAGG VMQTPHFRIY
SMDPRRAVVD TPQTTPDALI QDGPSLWFGN TWHLQVPLEH MTEGCVAVFE LLRYDYHTDG
PEVFCWTFFR LDLSKITSAP LTFEMYSPPV DPYSQILARM PGDSFFQAEL NISL
//
