ID W5JTL9_ANODA Unreviewed; 883 AA.
AC W5JTL9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA repair and recombination protein RAD54-like {ECO:0000256|ARBA:ARBA00015341};
DE AltName: Full=Protein okra {ECO:0000256|ARBA:ARBA00029956};
GN ORFNames=AND_001574 {ECO:0000313|EMBL:ETN66628.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN66628.1};
RN [1] {ECO:0000313|EMBL:ETN66628.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN66628.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN66628.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC001574-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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; ADMH02000413; ETN66628.1; -; Genomic_DNA.
DR AlphaFoldDB; W5JTL9; -.
DR STRING; 43151.W5JTL9; -.
DR EnsemblMetazoa; ADAC001574-RA; ADAC001574-PA; ADAC001574.
DR VEuPathDB; VectorBase:ADAC001574; -.
DR VEuPathDB; VectorBase:ADAR2_011758; -.
DR eggNOG; KOG0390; Eukaryota.
DR HOGENOM; CLU_000315_10_1_1; -.
DR OMA; KCQTHEL; -.
DR OrthoDB; 5480555at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673}.
FT DOMAIN 281..447
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 601..749
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 98855 MW; 1D7003C2B32D442D CRC64;
MRRSCAPSMK RPQATEDSAC AVKRPLVSSS GAASNSKQTG ISSSSSKENV GALKDTAIFK
VVWGKISTRK HKTWEGDGTL EVSGRSALLR DETGKVISTA SGLKLEEVTE GIQIIVGSKE
VEVLERITES TEPVSNCSKN VASANKIPRI LKPPSTSFKA PEQRKTAPDQ LQPDISSHDS
LTEKDSFTKV DTTPSVPVNR QFKPIATYTA PDEGSKNDQA EVVEPLFMKK PSFEHRFHHN
PNNELTVADV QVPACLARHL RPHQRDGVAF LYECVTGMRM MEPPGGYYGA ILADEMGLGK
TLQCISLMYT LLKTGPYGKP LARRILIVTP SSLVENWDRE ITKWLRNERL FTFIVGPHNK
LRLYAQSLHI PVLIISYEML AKQIDELETV KFDLIFCDEG HRLKNSNVKV FGVLSKLECR
RRVLITGTPI QNDLAEFYSL INFVNPGLLG SYQDFKARYE TPIIISQRPG VLPQSIELGI
ERLNELNVIT GRFVLRRTQE VINRYLPEKH ELVIFCHPSE LQTQLLRTAL TFYEEERSGS
NAITPLQLIT ILKKICNHPS LVKVTGRGDP ESLLHRLADQ LPDWQAMGPS DSAKLAIVDT
LLEDLIVKQE KVVIVSYYNK TLDMIAGLCE HYNYKHSRLD GSTVASDRSK IVATFNNAAS
DIFILLLSAK AGGAGLNLIG ASRLVLYDND WNPANDLQAM SRVWRDGQTR TVFIYRLLTA
FSIEERIFQR QISKTSLSGT VVDQKRNMNN LQFSDEELKD LFSFVDPQHA NDCLTHSLLE
CPCAGIGTIP EPEVTDDEPS DELDRLLRDP PIALPSETES RYRVRHGVPG GRSKTKYALK
MQELMRWEHH RSPVSESVME QLGLSGCSEE VVFLFRNIVS DGK
//
