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Database: UniProt
Entry: A0A182X665_ANOQN
LinkDB: A0A182X665_ANOQN
Original site: A0A182X665_ANOQN 
ID   A0A182X665_ANOQN        Unreviewed;       789 AA.
AC   A0A182X665;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA repair and recombination protein RAD54-like {ECO:0000256|ARBA:ARBA00015341};
DE   AltName: Full=Protein okra {ECO:0000256|ARBA:ARBA00029956};
OS   Anopheles quadriannulatus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA005301-PA, ECO:0000313|Proteomes:UP000076407};
RN   [1] {ECO:0000313|Proteomes:UP000076407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AQUA005301-PA}
RP   IDENTIFICATION.
RC   STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA005301-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   AlphaFoldDB; A0A182X665; -.
DR   STRING; 34691.A0A182X665; -.
DR   EnsemblMetazoa; AQUA005301-RA; AQUA005301-PA; AQUA005301.
DR   VEuPathDB; VectorBase:AQUA005301; -.
DR   Proteomes; UP000076407; 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}.
FT   DOMAIN          156..331
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          489..646
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  89953 MW;  A3587AC2A6414959 CRC64;
     MRKSLVPQRC TPSNAVHSPF KSPLSAQKRQ RECRKRLPDK GGPADQPPTP KLSVSEHELM
     IMKILTQPFK IPIANYVPEH STRCLGMKRS AARRALHDPY ACNALVLFSP PELTEHDKLK
     MDKSKIQVHV VVDPLLGNIL RPHQREGVRF MYDCVTGAKG DFNGCIMADE MGLGKTLQCI
     TLLWTLLRQS PDCKPTINKA IIVCPSSLVK NWYKEFGKWL GCRVNCLSID GGSKEQTTKE
     LEQYMANQSQ RHGTPVLIIS YETFRLYAHI LNNSEVGAVL CDEGHRLKNC ENLTYQALMG
     LKTKRRVLLS GTPIQNDLTE YYSLLHFVNP GMLGSTAEFR KQFENPILRG QDANSTDVER
     EKAAERLQEL AALVNRCMIR RTSALLTKYL PVKFEMVVCV RMTEVQAALY KSFLQSDTIR
     RSVMEKNATK ASLTALSNIT SLKKLCNHPD LVYEKIQERA DGFENAATIL PDNYSPRELR
     PELGAKLMLL DCMLASIKTN TTDKIVLVSN YTQTLDLFEK LCRKRGYGYV RLDGTMTIKK
     RGKVVDQFNQ PDSNDFIFML SSKAGGCGLN LIGANRLVMF DPDWNPANDE QAMARVWRDG
     QKKPCFIYRL LATGTIEEKI FQRQTHKKAL STTVVDNAED GERHFTQDDL KDLFKLDEQT
     RSDTHDIFRC KRCTNGVQMK LPPDDSDCMS DLAHWYHCAN NKGIPDDILS KSWDITRCVS
     FVFHHRSNSA VVEQQLAEQR RQQALAKERE EKEEEEEDEE DKENKGYNTE GEEDEEEPED
     DEKDKDFVL
//
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