ID B3M3A2_DROAN Unreviewed; 1921 AA.
AC B3M3A2;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=TATA-binding protein-associated factor 172 {ECO:0008006|Google:ProtNLM};
GN Name=Dana\GF18554 {ECO:0000313|EMBL:EDV43563.1};
GN Synonyms=dana_GLEANR_19811 {ECO:0000313|EMBL:EDV43563.1};
GN ORFNames=GF18554 {ECO:0000313|EMBL:EDV43563.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV43563.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV43563.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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DR EMBL; CH902617; EDV43563.1; -; Genomic_DNA.
DR RefSeq; XP_001955002.1; XM_001954966.2.
DR STRING; 7217.B3M3A2; -.
DR EnsemblMetazoa; FBtr0123254; FBpp0121746; FBgn0095572.
DR GeneID; 6501327; -.
DR KEGG; dan:6501327; -.
DR eggNOG; KOG0392; Eukaryota.
DR HOGENOM; CLU_000315_1_1_1; -.
DR InParanoid; B3M3A2; -.
DR OMA; WYSDIAC; -.
DR OrthoDB; 180798at2759; -.
DR PhylomeDB; B3M3A2; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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 InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044972; Mot1.
DR InterPro; IPR044078; Mot1_ATP-bd.
DR InterPro; IPR022707; Mot1_central_dom.
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; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR Pfam; PF12054; DUF3535; 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; SSF48371; ARM repeat; 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 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1361..1531
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1693..1853
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 84..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1921 AA; 211983 MW; 88B0F1D7A60F8218 CRC64;
MTSRLDRLFI LLESGSTAAT RQAAAKQIGE VQKLYPHELH SLLNRLVGYL HSTSWETRIA
AAQTVEAILK QVPQWQPELQ ALPKKEPATT AAAALEEDSC QSSGSSSTTA SERLLSFDEF
DLQQILHKGA RLIGSEGNEF DVQEEQPASG GGAEEQSLAS RLSRQRAVLN DKLGLTTAAK
LGVNLTDMIT DEDVALSRGG TSYNVNAEKL PVEHILNIKS SNGAGAGQTQ LSCREMNRAK
RKARQNTASS AAGSVVTPTC SRRNSNSNHS TGSNHSNNGT STTLTSLDEP EKKKLKASER
QEIFYSLNCA VPDATGTWVD AVSWPLENFC ARLFIDLFHA KWEVRHGAAT ALRELINQHA
QGAGKSVQQS REQMDESHSR WLEDAALRLL CVLCLDRFGD FVSDQVVAPV RETCAQVLGT
LVKEIDATKV QRIVDILLQL IQHKNEWEVR HGGLLGLKYV FVVREELLPI YLPLSISNIL
VGLLDAVDDV GAVAASTLIP VSSWLPKLLN PSQVSSIVKM LWDLLLDQDE LTSACNSFMG
LLAAILCLPK AASWVEMEPM ATLVPRLFPF LSHSTSSVRR STLKTLLTLT SADKVKVEPK
EEEPIKAAVE QPKMKLNFGV SEWKWQLLQQ ALRHIYQRIL VEPQADIQSL ARQVWSNLIE
HADLGALLHA ACPYVSSWIC LSMQPPRLAF DPGVLIRAGG DSSSTSRKKT ARIGDDLGGA
TLAHTNATLK LYLGGSEATP VEVREANFMR ARIASSRALG ALSHYLVQPA PGVVYSPQTE
SPTDCYTKVL LVHLNAHSAV QRIVCGLIIA FWALEDEPVR PGPPNLQEKL HQCVSEYIYY
DEVAVSLTRL LQEAQDFIAT LKQNKIPIND FNNAKILTLD QIEAVATKLT ENLRNYPLKP
KSLDLLEERR RSLQASYQQT TSEQGAYHVS AQAALAGAIC ALHCLPEKLN PVVKPLMESI
KREQCVQLQQ LSAEFLVHLM DQVCDRNPSP NSKILNNLCT LLRSDGEHTP KLVMPLQTLQ
QTPPSPCVTN SCVYYGILTL ALQQAVTTTT TTRGGGAGAV TPTTPAVPRG PGRPPANEIL
AAASAVAAHI DLKAQQAKEA EAKQCRTQRL GAASAIEKLC STFGEHIVEK VSVFQQLMFG
KVTQFVKETD EQQLANTLPE LGVCTELISS LQLIETAAPH LHVALHPQMF ALLPPLGVIV
RHPLKSVRHM AARCIAVLAE IDACQTMQFV VQQLLPQLGK VEQLIERQGA MEAIERVVSR
LQIKVVPYIV LLVVPLLGAM SDPDESVRLL STHCFANLVQ LMPLDGKAEQ LKSEPLQAQK
TRDREFLDYL FHPKSIPDYR VPVRISVELR SYQQAGINWL WFLNKYNLHG ILCDDMGLGK
TLQTICILAG DHLQRTKSKQ ADLPSLVICP PTLTGHWVYE VDKFLAEGSV LRPLHYYGFP
VGREKLRSEI GTNCNLVVAS YDTVRKDIDF FNGIHFNYVV LDEGHIIKNG KTKSSKAIKR
LKANHRLILS GTPIQNNVLE LWSLFDFLMP GFLGTEKQFV QRFSRPILAS RDAKSSAKEQ
EAGVLAMEAL HRQVLPFLLR RVKEDVLKDL PPKITQDLLC ELSPLQLRLY EDFSNKHLKD
CLDKLSDSPA SAMVAENLGA KTHIFQALRY LQNVCNHPKL VLRQSEDLAQ VSAQLAQSNS
SLDDIEHSAK LPALKQLLLD CGIGVQTESV SQHRALIFCQ LKAMLDIVEH DLLRRHLPSV
TYLRLDGSVP ASQRQDIVNN FNSDPSIDVL LLTTLVGGLG LNLTGADTVI FVEHDWNPMK
DLQAMDRAHR IGQKKVVNVY RLITRNSLEE KIMGLQKFKI LTANTVVSAE NASLQTMGTS
QIFDLFNGGN GNGQGTSTAG STAAGGPMSM NTIIENLPDL WSEHQYEEEY DLGNFVQALK
K
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