ID Q5B2F2_EMENI Unreviewed; 1579 AA.
AC Q5B2F2; C8VH07;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=ANIA_05278 {ECO:0000313|EMBL:CBF82188.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF82188.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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|RuleBase:RU363044};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU363044};
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|RuleBase:RU363044}.
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DR EMBL; BN001305; CBF82188.1; -; Genomic_DNA.
DR RefSeq; XP_662882.1; XM_657790.1.
DR STRING; 227321.Q5B2F2; -.
DR EnsemblFungi; CBF82188; CBF82188; ANIA_05278.
DR GeneID; 2871570; -.
DR KEGG; ani:AN5278.2; -.
DR eggNOG; KOG0987; Eukaryota.
DR HOGENOM; CLU_001324_0_3_1; -.
DR InParanoid; Q5B2F2; -.
DR OMA; CNGTRMQ; -.
DR OrthoDB; 2548034at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR025476; Helitron_helicase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049163; Pif1-like_2B_dom.
DR PANTHER; PTHR45786:SF82; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR45786; DNA BINDING PROTEIN-LIKE; 1.
DR Pfam; PF14214; Helitron_like_N; 1.
DR Pfam; PF05970; PIF1; 1.
DR Pfam; PF21530; Pif1_2B_dom; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU363044};
KW DNA damage {ECO:0000256|RuleBase:RU363044};
KW DNA recombination {ECO:0000256|RuleBase:RU363044};
KW DNA repair {ECO:0000256|RuleBase:RU363044};
KW Helicase {ECO:0000256|RuleBase:RU363044};
KW Hydrolase {ECO:0000256|RuleBase:RU363044};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560}.
FT DOMAIN 476..660
FT /note="Helitron helicase-like"
FT /evidence="ECO:0000259|Pfam:PF14214"
FT DOMAIN 1401..1447
FT /note="DNA helicase Pif1-like 2B"
FT /evidence="ECO:0000259|Pfam:PF21530"
FT REGION 137..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1579 AA; 178354 MW; C310124CB1CF388C CRC64;
MYSTPTRHLF FFASVTDRYG PPSVNKHLAA VFFPIPHICI VHIALSYYCI CLENVRRLFP
VTTDVISVGV TGRISNFSGR LIPPGVALLH GSLASPVDAR ASFGVGDDYQ QSASILANTP
PPADLTDIHN AGYDEDFQAG VSDDEDEPPA AAPPLPISVG NTSVYRGYRS QLHRMRPLNI
GRMDLECPDC HGLHWKAERD KGTSIAAPKF GKCCGGGNNF IPPVEVPTFL QRLFNGSDHD
NGRHFRQNAR LYNCAFSMTS FNAGEDPRLK GQHGPFQIQG QLVHFLGPLL PDADRPPAFA
QLWIYDRLTD AARDRNRALA TAVRCTRFSD LRPGIVGELT EWFELHNRFS QQFMSATEQL
FANEARGTPA ELLLGPGINL VAVEGTDKRR YNLPREGEQV AALLIDPTVN DLDHGTFREV
ILQLRHPVNG SGLKRIDPSH AGYLPMQYPL FFPYGDDGWH WGCRRLDGLR LSARMYHAYR
VHIRRREFSP WHYGGRLWQQ YLVDAWGTIE QAKLEWIRHN QTTIRAELYS GLTDALAAAD
GDVLVANNTG QRVILPSNVV GTPRYMQQLF QDAMAICQFY GPPSLFITFT ANPAWDEVTR
ELRPGETWED RPDIVSRVFN ILRAEMVDEL CKKKLFGVAP GRFFTIEYQK RGLPHMHLVL
FLEERERFLD AAHIDEMVSA ELPDPREDLE LYKLVKKHMI HAPCGPVYNS RAPCCDKHSD
SNMIYCTKRF PKAEQYETQP IEEGYPLYRR RADPRGAYRI KAKNNDMVRI DNTWVVPYNP
YLLKRFRSHI NVEVCRGVDV IKYITKYIYK GPDRASMRSK VADEVDLYLD ARYVGASEAV
WRLLRFPLHQ EWPPVTALHV HEPARHLVYY NSNAGMRELE DCIDGGKSML MGFFEYNAHA
ANPANAALAL NRYLYAKMPQ FFTWDKADRI WRPRTRNRFA IGLCVGPVSF EDLRTHDGIL
YPTFKAACNA RGLLKDDREW HHAFEESVGS AIGAQLRTLF VVALTSGTLN DPPCLWEEFK
CRICSDLEHY EIRRMDNPPD IEDRHIDYGL FIIARMLAEH GERETLDRYG LPLWTAAWGR
LEPQTDVLVP FIPPVDLARR VDALIPSLNI DQRRHFDTVS AAMADRSGEC FYLQGAGGTA
QGKTVLCIAS SGIASLLLPY GRTSHSTFGI PLALHEESTC AVTLRSTRAR VLAGVDLIIW
DEAPMQHRHA FEAVDRLLQD ILKVKQLFGG ISVLTGGDWQ QCLPVVPKAP RAGIISATLR
RSYIWPRLRA ILRLTQNMRL PSVGINRLFS QLLARMSVDN TMHGTLELPD YVMDSASMSV
EELCERVFPA ADMTHCHTAD FQASDPDFFA GRAILSMRNS ALVEFNDRIT DSMRSQESMR
YSADEALTDN VAEGVEEITH EFLQSVDLPG LPPARLRLKV GMPIMLLRNL RATEGLCNGT
RMQIVELCRY TIRARILTGD FRGSVHLIPR ITLYSKPGDL HYVLSRTQFP VRPCFAITTN
KSQGQSLQQV GVDLRVPAFS HGQLYVAMSR VTDVRRLSVL LPPGVRTTNN VVYPEVLQDI
ASLDDVPDWD DGMVTDEAA
//
