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Database: UniProt
Entry: A0A329SGS9_9STRA
LinkDB: A0A329SGS9_9STRA
Original site: A0A329SGS9_9STRA 
ID   A0A329SGS9_9STRA        Unreviewed;      1336 AA.
AC   A0A329SGS9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Myosin-13 {ECO:0000313|EMBL:RAW34888.1};
GN   ORFNames=PC110_g8792 {ECO:0000313|EMBL:RAW34888.1}, PC113_g3486
GN   {ECO:0000313|EMBL:KAG2865729.1}, PC115_g8387
GN   {ECO:0000313|EMBL:KAG2925146.1}, PC117_g3260
GN   {ECO:0000313|EMBL:KAG2951879.1}, PC118_g8596
GN   {ECO:0000313|EMBL:KAG2984932.1}, PC129_g7001
GN   {ECO:0000313|EMBL:KAG3222288.1};
OS   Phytophthora cactorum.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW34888.1, ECO:0000313|Proteomes:UP000251314};
RN   [1] {ECO:0000313|EMBL:RAW34888.1, ECO:0000313|Proteomes:UP000251314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10300 {ECO:0000313|EMBL:RAW34888.1,
RC   ECO:0000313|Proteomes:UP000251314};
RA   Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT   "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAG2865729.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=15-7 {ECO:0000313|EMBL:KAG2865729.1}, 4032
RC   {ECO:0000313|EMBL:KAG2925146.1}, 4040 {ECO:0000313|EMBL:KAG2951879.1},
RC   P415 {ECO:0000313|EMBL:KAG2984932.1}, and P421
RC   {ECO:0000313|EMBL:KAG3222288.1};
RA   Armitage A.D., Nellist C.F., Bates H., Vickerstaff R.J., Harrison R.J.;
RT   "Effector identification in a new, highly contiguous assembly of the
RT   strawberry crown rot pathogen Phytophthora cactorum.";
RL   Submitted (OCT-2018) 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}.
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:RAW34888.1}.
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DR   EMBL; RCMG01000053; KAG2865729.1; -; Genomic_DNA.
DR   EMBL; RCMI01000216; KAG2925146.1; -; Genomic_DNA.
DR   EMBL; RCMK01000046; KAG2951879.1; -; Genomic_DNA.
DR   EMBL; RCML01000222; KAG2984932.1; -; Genomic_DNA.
DR   EMBL; RCMV01000187; KAG3222288.1; -; Genomic_DNA.
DR   EMBL; MJFZ01000186; RAW34888.1; -; Genomic_DNA.
DR   STRING; 29920.A0A329SGS9; -.
DR   Proteomes; UP000251314; Unassembled WGS sequence.
DR   Proteomes; UP000697107; Unassembled WGS sequence.
DR   Proteomes; UP000735874; Unassembled WGS sequence.
DR   Proteomes; UP000736787; Unassembled WGS sequence.
DR   Proteomes; UP000760860; Unassembled WGS sequence.
DR   Proteomes; UP000774804; 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; cd14901; MYSc_Myo40; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 2.30.42.10; -; 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; 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; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF845; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00612; IQ; 3.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50096; IQ; 4.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50106; PDZ; 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:UP000251314}.
FT   DOMAIN          94..825
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1244..1324
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          39..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..717
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1205..1228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         198..205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1336 AA;  151184 MW;  15A0638E752BD6A4 CRC64;
     MEVGAPVWVF DRELWHEAVV AAPVDASSGL VECAIEPEPN DENLVTPEGD DVVPDAQDFQ
     TPRKRRNSRR NSMRRAVSIK TEFVLPRNQG EHYHTVQDLT KLVHLHEPAI LQVLRRRFFH
     GEIYTSTGQI LVAMNPFRRL SLYSDDIKDQ YYDLGGNAQA DKSTLAPHVY SVADQAFRTM
     LVPRSGDNKT DQTILVSGES GAGKTETTKL IMNYLAYVST KRTRRPIRAS NCDQTTIHDR
     VLESNPILEA FGNARTTRNN NSSRFGKFIK LGFTSSGEML GASISTYLLE RVRLVSQGKG
     ERNYHVFYEM CGGSSASERQ ELALLDLHEY AYLNQSECYE RLDGVNDAES YQVTRRAMSS
     IGMSPEEQLN VMKIVSAVLH LGNLCFTTAT RNGGKDDASV VDMDECGDNI KAICSLLGVE
     EDVLRSTLCS KKIKAGAEFI TTRLPVAQAL STRDSVVKTL YSNLFNWLVD RINRSIEYKE
     EAGGNQFIGV VDIFGFEIFE QNRLEQLCIN YANEKLQQLF GRFVFRMEQD QYVAEEIPWK
     FVDYPNNDVC VALVEKRHTG IFSLLDEQCL IPRGNDEKLA NKYYELLAGK HESFSVTKLQ
     RAKGQFVIHH YAGNVCYMTD GFCDKNKDHM HTEAVDLLRT SKFSFVRACF ENSVNAGGNS
     SPRNGRTESR GSDGTRRRSG GIMSSTVVAQ FKSQLSSLLE VLNATEPHFI RCIKPNDQAS
     ASQFERRRLL EQLRCSGVLE AVKISRSGYP VRFPHEVFIK TYSCILSQIP SAQGQVEKEV
     ALQMVEKLAG KLQVDTDAKH PPFQVGKTKV FCVLEAHQAL ETARSKALYK SVITLQRYCL
     GYTMRARYQR KRRSSIRIQA IWRSWSCWHR YQRFIRRERA ALKLQCTTRG FLARKQLKRI
     HAVTVIQSFV RGWLVRREYS ANTLSFEHDV SYVGSLDERS TTASSISLSE SISKDRKNTT
     ISFQSSVSTS DYSDTDGSIS IRSSSRISRK KMIEEYEPPT QIQNEYEIVW ECGLLGLYFE
     SDPISGMPIV RRVHESLSNC ADIFEVSRGD VLLAVGKVKV KKGDIRRILT LLQEVQKPVR
     LHFLRNPTES FRLRSGSLEL LGEEDYEVLW KEGVPLGLGF RPDPSSGYPC VLQSQGNQLL
     PGMFNVRAGD HLVFINEFST QGVRFQKVID ILESGPRPAV LRFRHTDLVE DPQHQLDQTM
     SLDSSVLSNP QDDSHSMGMS RLTRPSRVSM NPKNDHSLYY ITWKEEDGPL GIVVKQESTS
     YYPRVINVKS EGAVTRESQK NRVEIGDVLL SINNNNISKM GFGAAMKLLQ KGPKPLLLMF
     QRPRTSLSMT TRSCNL
//
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