ID A0A067CZL2_SAPPC Unreviewed; 1228 AA.
AC A0A067CZL2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=PH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SPRG_19490 {ECO:0000313|EMBL:KDO32212.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO32212.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO32212.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO32212.1,
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KK583196; KDO32212.1; -; Genomic_DNA.
DR RefSeq; XP_012197415.1; XM_012342025.1.
DR AlphaFoldDB; A0A067CZL2; -.
DR STRING; 695850.A0A067CZL2; -.
DR EnsemblProtists; KDO32212; KDO32212; SPRG_19490.
DR GeneID; 24140847; -.
DR KEGG; spar:SPRG_19490; -.
DR VEuPathDB; FungiDB:SPRG_19490; -.
DR OrthoDB; 55723at2759; -.
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; cd00124; MYSc; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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; 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 InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR13140:SF856; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 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:UP000030745}.
FT DOMAIN 19..123
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 325..1121
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT BINDING 425..432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1228 AA; 136703 MW; 5DBD8DFEFF40A776 CRC64;
MSGFLGRRAS VSAPIADDNV ALEGWLKKRG HHFFSTVKTR YFVLLKDGAL VYFADDKRKK
QKGAVRVAIQ DVVTPTTTKD KMFAFQLKKT SSDHDAKPFV LTMLAATDAE RTCWIEALRK
VMAASVPPVR LTMMLRSTTL RASSTRSLDT GASDVFGMLL EIGKLQQLVQ TAKTEWGDDP
LQWTSDQYLE LCRSIVFTHE QAAGLSLSLL ENQVLQEALE LRYKYEDAHA ARLRLSSADV
NGLSALSTTP PDEAPVLVEA PVLVEMPVET PAPLLPSGTR KYFETLDPAF VALSPRSKTM
AKYTALYQQE ALAAKRSWNA HRELDDDLLQ VLDAPITTDD LVDALARRFE ADRVYTSVGD
TLLMVNPAPR LLHHTAGNSI YDEATVLWYR DHDVAVCSPH PFALAKRTLS SVLDMKEPES
IVLMGESGSG KTDFAKHVLK YIATIQQAPK PPTVQLFTSS TKSTIKMRSD EAHLMDLLAS
KQVQYETIYL DITPERWPEM LAVSHGVKQL PQVHMDHMFF GSYDELQRLE DEEQFVFYVK
NPRAARLLSV LLDGNVLLEA FGNATTMHNP NSSRFGKSTA FRVHTTTGHL YGGAITPFFL
ETSRVTNASA DTFNFHIFYA LLLGGSASLL AELRLDAASP LAFAYLGNAR SSTIASSVAS
YDEDRQRWHQ VLRCFDLVGV SELDRLAIFR VLAAILHLGN IPFDDVLNAQ GVAEGVRIAD
KSALDTIARL LSLAPAAIEH ALCTKRLNVA KASETYELHV HRPHAIKARD SLARLLYDGL
FHALVALLNR STAPSADAPK ELCDVTLLDV FGFEDMQVNS FEQLCINYLT EKLAVLHVQF
ASEAQCALYF AEGLDALWPT HHGSLLVHEG SGMQVLESAV GVWACLEEAT LLHGNEQDAK
QAKNSRFVRA LYLRNASHDG LRVEPDPLQF TVLHHRSAVT YTAINFVAKN SEALSGELQA
LVPTSENAFV KALLTHHTLP SASKRQTPSV SSQYRAHVMA TLAALRETKP HFVHCFRARL
PSSKDYFALD KPLLEAQVKG HMLAQVATWA SLLFRHHTLL AVFHQRYRML FPGPIESLES
QVEAFVHEAL PHEARGRSFA IGATMIFYSD ALQLVLHRQR DRLRADACLV LQSTVRMWRA
KMRVRAIRQS LRQYLEAITA FYAKYNPAKL SQVPTIVRAF RGREADLLAK LERKYAHTGP
STEHEVQDTS LEAFILSVKF DAATVQKA
//
