ID E2AP89_CAMFO Unreviewed; 682 AA.
AC E2AP89;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=EAG_05176 {ECO:0000313|EMBL:EFN64762.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN64762.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL441481; EFN64762.1; -; Genomic_DNA.
DR AlphaFoldDB; E2AP89; -.
DR STRING; 104421.E2AP89; -.
DR EnsemblMetazoa; XM_011263282.3; XP_011261584.1; LOC105254533.
DR InParanoid; E2AP89; -.
DR OMA; YTEHERM; -.
DR Proteomes; UP000000311; 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; 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:UP000000311}.
FT DOMAIN 106..281
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 441..594
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 682 AA; 77723 MW; 019E4D0F401DFF2B CRC64;
MQKIVSEHEE RVRKLLSKPF KIPVPGYQLS GRVLGLRLPG PRRPLHDPND PNALIVYSPP
ELSEHERLKI DSCKQLVHVV VDPILCNVLR PHQREGVKFM YECVTGKRIE NAYGCIMADE
MGLGKTLQCI TLLWTLLKQG PEAKPLIDKA IIVAPSSLVK NWYNEINKWL NNIVNTLAID
GGKKAEIDTK LLRFMKTYGG RCVTPILIIS YETFRLHAHV LHQDEVGLVL CDEGHRLKNS
ENQTYQSLMG LKAKRRVLLS GTPIQNDLLE YFSLVHFVNQ GLLGTAQEFR RKYETPILRG
QDAAATDDQR KLAQERLSDL VSVVNKCLIR RTSALLSKYL PLKHEFVVCI KMGELQTRLY
KNFIQSESIK RSMEEDDNPK KGGHLSALAA ITLLKKLCNH PDLIYDKIME KSEGFEKAAQ
LLPSHYSTKQ LLPELSGKLM VLDCLLASIK TTTNDKIVLV SNYTQTLDLF EKLCNKRSYN
YVRLDGSMTI KKRSKVVENF NSDTSSDFIF MLSSKAGGCG LNLIGANRLV MFDPDWNPAN
DDQAMARVWR DGQKKTCFVY RFLSTGTIEE KIFQRQAHKK ALSSTVVDQE DDVARHFTIN
DLRDLFKLEQ NTVSDTHDKF KCTRCVNGIE VKGPPEQSDC NSDLSEWRHS HNPRNLPDIS
LRQCWASGIS FVFHHRSHEH IK
//