ID G3AE77_SPAPN Unreviewed; 1151 AA.
AC G3AE77;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN ORFNames=SPAPADRAFT_48591 {ECO:0000313|EMBL:EGW35611.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW35611.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair by
CC homologous recombination and in genome maintenance. Capable of
CC unwinding D-loops. Plays a role in limiting crossover recombinants
CC during mitotic DNA double-strand break (DSB) repair. Component of a
CC FANCM-MHF complex which promotes gene conversion at blocked replication
CC forks, probably by reversal of the stalled fork.
CC {ECO:0000256|RuleBase:RU367027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU367027};
CC -!- SUBUNIT: Interacts with the MHF histone-fold complex to form the FANCM-
CC MHF complex. {ECO:0000256|RuleBase:RU367027}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367027}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC FANCM sub-subfamily. {ECO:0000256|ARBA:ARBA00009889,
CC ECO:0000256|RuleBase:RU367027}.
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DR EMBL; GL996499; EGW35611.1; -; Genomic_DNA.
DR RefSeq; XP_007373023.1; XM_007372961.1.
DR AlphaFoldDB; G3AE77; -.
DR STRING; 619300.G3AE77; -.
DR GeneID; 18871242; -.
DR KEGG; spaa:SPAPADRAFT_48591; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_1_1_1; -.
DR InParanoid; G3AE77; -.
DR OMA; TIAHINT; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd18033; DEXDc_FANCM; 1.
DR CDD; cd12091; FANCM_ID; 1.
DR CDD; cd18801; SF2_C_FANCM_Hef; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR039686; FANCM/Mph1-like_ID.
DR InterPro; IPR044749; FANCM_DEXDc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR14025; FANCONI ANEMIA GROUP M FANCM FAMILY MEMBER; 1.
DR PANTHER; PTHR14025:SF20; FANCONI ANEMIA GROUP M PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000709}.
FT DOMAIN 93..260
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 424..628
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 481..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 130038 MW; B7D7A622B810F49F CRC64;
MPVIPIHDEE DDDDWAFDDE EEDPELQQIL QNGVSSKRQR TLDGNIVPTI TSVQQLPKPI
PVNIPSHHPI DYENLKTYIY PTNFQIRDYQ YNIVQRAFYD NLLVALPTGL GKTFIASTVM
LNFLRWFPQS KIIFMAPTRP LVAQQIKACC SITGIPSSKV AILLDKTRKN REEIWDTRQV
FFTTPQVVEN DLARGILNPK SVVLLVIDEA HRARGNYSYN NVVKFLSRFN NSFRILALTA
TPAGDVEGVQ DIIDNLKISK VEVRTEHAID ITKYMKRKQI VKRTVNASSE IQELIGLLAT
AISPVLKSAN ERGVFDITDP TRINHFQCME ASRKVTMNRT MPSGLKWSNF YMLQLLGVVG
QCYRRLNIYG VRSFYTYFNE KYNEFKGKKS KSQINSDFYF SDEIKQVLKR SDEVLKGKGY
SHPKIETLMD ELTDFFADGV SSDSRVIIFT EYRESALEIV QCIERTETNL KPHIFIGQSK
EKERFDETKS KTKGKSKKRA HDGDDDVRDS TRTSSEDAQI KGMNQKLQKE IIKKFKAGAY
NILVATSIGE EGLDIGEVDL IICYDSTSSP IKNIQRMGRT GRKRDGKVVL LFSSNEELKF
DKAMAGYEYI QQHIQKGDLI TLCSRNRIIP DIYTPKVVEQ FIEIPDENIE LKSEDDEDEI
IRIATQYMLG GSQKKKKSTK KPLASKKKFF MPDNVETGFQ SVTNMIKKSG DEVEKKRERD
ILDSFLDSSD DDDLPIIANP SLVRSSTSSR KLKVVDSDSN DDIPISSTSR QHSNPQASDS
PNKRQVIDLK SDEDIPIASK AVSKSDSSKK KQVSSDSDNE LSIHKDLNTP ASSLVSEFPV
SSKSESGSIP IDLDDDFSFS SDDESEVSES TREPTPLVPS SPKPKPKSLG VKRAVVVPND
HTASPPPVTS IPVEKAKMLT KISESNFNIP SSFNPHSEIG RPKKTLGLKR TRVNILDQLK
NRQSQLAATH EDINRDHSGT RSAPIVLDDI DLPNYTPDSQ VCVKHELEQD QTNDYSIDVE
SEPDKSTISV HDSGHDTVVI NQSRVNKHYD IEQKSHNSSI YEFSSDSEGL LTEDQRMQLY
TNYYVPVDPS QTVQFYDPFD GLKGKKKNHG KIPHSLNTEK LIDYLNRGIL EKPGEDGTDD
SSFDLSSIVY D
//
