ID Q5B054_EMENI Unreviewed; 2379 AA.
AC Q5B054; C8V2S6;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=SNF2 family helicase, putative (AFU_orthologue AFUA_2G09120) {ECO:0000313|EMBL:CBF70236.1};
GN ORFNames=ANIA_06076 {ECO:0000313|EMBL:CBF70236.1};
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:CBF70236.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; BN001301; CBF70236.1; -; Genomic_DNA.
DR RefSeq; XP_663680.1; XM_658588.1.
DR STRING; 227321.Q5B054; -.
DR EnsemblFungi; CBF70236; CBF70236; ANIA_06076.
DR GeneID; 2871021; -.
DR KEGG; ani:AN6076.2; -.
DR eggNOG; KOG0298; Eukaryota.
DR HOGENOM; CLU_000796_0_0_1; -.
DR InParanoid; Q5B054; -.
DR OMA; SMIPYIT; -.
DR OrthoDB; 103295at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; 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; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45626:SF26; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G09120)-RELATED; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:CBF70236.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1343..1758
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1968..2060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1982..1996
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2034..2060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2379 AA; 267053 MW; CE2CBA72C2EFFA45 CRC64;
MPAKRKPPVI ATLASSRSRR YPHQSGTVPE PAHQSEFRLE PGPDLQIRLK VEVEAEFGLH
GTRHHQPKPF TQDGSTISAR QFRPGELEPL SKYEDVSNED DNDGSNVAKR PRMVVVLRLP
LSLNKPGPRF QSVQRAHDTS VTATDPYPDS GAYRAALKRE HPNSIVATSA VKRPRRSPRF
QQSNAGQLEA ADEVLDGAKA HQGVAGVKNK IPSATNNTLP SPSKMVAAMA RSSIIQFSFS
STGCRIPSLD DNNTDQGPSR LDPNTPELIR SQPYSGRMRP RTQLAQHLPP LYKLSDIFKS
LTERAIDLGL DKVLTHLGNR RLRVATVCSG TESPLLALEM VKENLQKYFN RDLDFKHLFS
AEIVPYKQAY IERNFRPRLL FRDVAELKDR VARTAYGSLE KVPKNADMLI AGFSCVDFSG
LNNYRKELDE TGESGDTFWG IICYAKIYRP RMVILENVKT APWAKIEGHW NDIDYVAVHS
DVDTKAYYLP QTRERGYMFC VDKRLLSHLA QNHHGLGLDA DEIGLNMRRE WVDTLAAFKR
PASSPAGMFL LDAEDRRLEQ IEKDMAQKIV ASAATVRATV NWDRYQVRHQ GYRLKQGLGH
RRPISKSQDD GTCKMPDFAW QVWMRSLPER VRCLELSQGL DREMDSRAFG IVGCITPCGI
PYMTTRGGPL CGLESLALQG LPLDRLLLTQ ESQRELQDLA GNAMSSTVVG AAILSALIAG
HKVLRKGDFS QTSKPTSRTQ KSRITPQGDV ALTSSNMHLD PDTVIDILKL REQATTSARY
CVCEGHNSIR ATCSECSGNP QHAYERWLDL PRTVPLDFVS SLRSILPGRL AVRGITPDSY
KELKSNSYIP AKCWSEFLDA VFRAVGDELR FSDINRSECW TVTYDGKYSV LKLVIEPFGS
ITWLFFAKPR ETDPALCLIR EVLSKPVARM TLPVPSHQAG STSSSILEGG TWEICAPLSS
SCSLKFFGTG SKVDSYEARC GLQLPAYQNS QVWSHIIVHG ADKDIKDLEV DVRGTYELLP
DCGTANSCLH RRPATAGGNP TIYLFLDPTK LGEPTNDSFV FALEHRRIPG YATRMTIAEV
SHTWRSSKAT DKAETVIIYY RKWIPCPLIS LQPYSRETGS SIQCYTLDSN ASVAITNGEC
HNANVTLLAF TIPAGVATSD SHSPWFAREW EAINPIDCPE LLRENAWLLQ RAAGYSDFCE
WNQIVEANIQ GPCRVCVPPK PGILWGRDAK GRVKAYEDPY GAARYEREIK SRPSAFLIFR
RECYQDIKAI SAELRVTINV QTLLHQAYGR LPHVQTGSPA ASFYWRLVPN SYDVRDCLYP
KFELRSNRND PQASQPPQFT LEGRPKLRPE QLRSLSWMIA QEKENVEPFI EEETEEALLG
SLMWRAEGRV TVPKTVRGGI LADDVGYGKT AIILGLLDAS FANLNIDLSV SLNSTGFVPS
RATLIVVPRI MVQQWRAEIA KFLGDKYNVL AFSSAAALRK TSIGDIRNSD IILVSRSVFD
TAAYYQHLRR YAGASEAPDK PGRKFDDWFH LAHGFMKQHV RVLAESGPLA FLQSLRNRRA
PTKYPETHQY APSKRLRGKQ YALANKDRDF EMKDDRPYAE ISSNEESSGT SDGEYGNPIM
LKAKIDHLLR LIPPKQFKKN EGLAGEQSSS HGEIEDDWKG FGIDGETQSW EAVLGLPFHA
FHFNRLVIDE FTYAKMDRLT QLLTLQARSK WFLSGTPPLN DFEDVNTIAP FLGVHLGIDA
EDDINSQHFR LKELRKQRSD AETFQAFRAP RSEAWHRRRH ELAQIFLDRF ARRNVAEIDE
IPATEHIVLV RQSPAEKVIY LELYKQLMTY NRQLRRVNGR GGDQAERIDE IIAYSSTPEE
ALLKRCTSLA LQGRWDDDGQ PEAATCASLI RTREEQLDQT KNALNNKLKL AAWLYCSCKH
EHDKFSQFMN SVIMHNFGDK SVTEEVDPLL TMAVKESKRS DWRFFYSGSD SDQKTGDEGQ
HGDVDEDSET IEEEDEDELV LKQKGLGGQR KTQSRFTAES KLKPRHKQKS KAKPTLTRKD
ENKKNKSEPL LPTKPTEPRE FDSELRDVTG VLRKLVVEWV HRKRALRFLT AVRKIQTNPN
PQAIPACDNC QTQPGVLSKL NILGSCGHAL CSNSDCTQKT LEKEECVVEG CRGSGKNFNI
INAMTLGCDT TSTPTAMSSD GDSNGDIDRS SKHGGTKLEA LINIITKFPV EERALLFVQF
PDLMTVASMA LSSAGIKHII ITPTDQKTSS KIEKFQKEGF GDTKVLILNL GNEMAAGLNL
QCANHVIFLS PFLAETQYDY DSVMIQAVGR SRRYGQTRHV HIYHLLAKMT IDVNVFQERR
GNKVLVERGG RATLLDAEEA AEDETMTCQG PAMVVENAI
//
