ID F1KX53_ASCSU Unreviewed; 746 AA.
AC F1KX53;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA repair and recombination protein RAD54-like {ECO:0000256|ARBA:ARBA00015341};
DE AltName: Full=Protein okra {ECO:0000256|ARBA:ARBA00029956};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY42457.1};
RN [1] {ECO:0000313|EMBL:ADY42457.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- FUNCTION: Involved in mitotic DNA repair and meiotic recombination.
CC Functions in the recombinational DNA repair pathway. Essential for
CC interhomolog gene conversion (GC), but may have a less important role
CC in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51
CC enhances the ATPase activity of okr/Rad54.
CC {ECO:0000256|ARBA:ARBA00024776}.
CC -!- SUBUNIT: Interacts (via N-terminus) with spn-A/Rad51.
CC {ECO:0000256|ARBA:ARBA00011467}.
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DR EMBL; JI167366; ADY42457.1; -; mRNA.
DR AlphaFoldDB; F1KX53; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18004; DEXHc_RAD54; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022776};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 245..412
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 546..703
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 746 AA; 83539 MW; 018DF2DDC43D01BE CRC64;
MRRSAVLSLN DAADSGGSAN KRRALSEIPL VSYDMEPAYC CPSIPAHCVV NGDDVSVHLQ
GDMRCRRYAV VYGRVSTRKH KRWEGDGVLV CRDRFAMLQT EDGKDIARVS AFSKRHLDAL
EPGHRLVIGG FELEVQEEFH GESECENLSA SSRHGSASAA DMKPISADDT FQSASGRIPS
CSSGRKLGRK FVQPLLRTHI PSSSYDFVVN KNEVDVSGED AVVLDGPLAR HLRPHQKEGL
TFLFRRLKDP GGGVILADEM GLGKSVQAIS LLWILLKQLK QKGATSMKFI LIAPTSLIGN
WRCEFNKWLP HSEQLLFPVT KTSEVRKFMA YSGYSPVLLI SYDVVVRCAE LLEKISFALM
ICDEAHRLKN FNGNLRQSVS RLRTERRLLL TGTPIQNDMS EFFSLLDLAK PAAFGSLAQF
RSMMANEDGM HDIQLLLSEI LLRRTADVNF NNLPPRHEYV LWCRLSKVQQ LIYNRIIGLA
SSDHLAIIDM LRKLCNHPSI LYQSLTSKHG AFNSCESTLN ATVLRAFPSS FEPNCSTIVD
SGKLSVFVKM MVSLRETNEK VVVVSNFTKT LDMLSEVCKG IFCTVTRLDG SVVPHRRMQL
VDEFNTSSLP NHVFLLSTKA GGVGLNLIGA SRLVLFDSDW NPAFDVQAMA RIWRDGQKMP
CHIYRLVTAG TIDEKILQRQ VMKSGLGTVV ELDSLNERRF PLGRLLVLLI NWRCPFLLDF
AAFQHIRNIV PFEMEAPGGA YWSYLH
//
