ID X0B3J5_FUSOX Unreviewed; 2207 AA.
AC X0B3J5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Pre-mRNA-splicing factor brr2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOMG_00836 {ECO:0000313|EMBL:EXK47433.1};
OS Fusarium oxysporum f. sp. melonis 26406.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089452 {ECO:0000313|EMBL:EXK47433.1};
RN [1] {ECO:0000313|EMBL:EXK47433.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26406 {ECO:0000313|EMBL:EXK47433.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum melonis.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXK47433.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26406 {ECO:0000313|EMBL:EXK47433.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "Annotation of the Genome Sequence of Fusarium oxysporum f. sp. melonis
RT 26406.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH659329; EXK47433.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOMG_00836; -.
DR HOGENOM; CLU_000335_1_0_1; -.
DR Proteomes; UP000030703; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18019; DEXHc_Brr2_1; 1.
DR CDD; cd18021; DEXHc_Brr2_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR048863; BRR2_plug.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 535..719
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 757..966
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1386..1562
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 31..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2187..2207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..261
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2191..2207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2207 AA; 250086 MW; 316B28296A28FCD4 CRC64;
MSDANRDVSQ YKYSAMSNLV LQADRRFVTR RTDEATGDPE SLAGRLSIRD MGARVARDDA
PKPKKQPGLP EIERGSLREG EDILAREQRR RKAEAPQSTG ILGANDLLVE GITYRPRTAA
TRQTFDLIIT SVAKTLGDVP HEVVRSAADA VLEYLKDDDL KDLDKKREID DILGVTLNPK
EFNELVNLGK KITDYDAQDD DEDVAMGGAD GEDAEIDERQ GVAVAFDEDE EDDEGGLVHE
VRDESSEDEE EEEEEEKEQS AEGKEEDAVA DVGDEMILDS APSGGKQDEK DKHSIPARDI
DTFWLQRQIG TLYPDAHEQS DKTKEALKIL SGEPGEDGEE KSLRDVENDL MELFDYEHHE
LVQKLVENRE KVFWLTKLAR TQTPEERADV EREMVSEGLQ WILNELKGKD TAEGKKGKID
IKMDIDVPAS FTADGPKAER AEGQLVGGLQ PRKLINLDNL VFDQGNHLMT NPKVRLPEGS
TKRTFKGYEE IHIPTPKKRN EPGDVLIPIS DMPEWSRNPF SKNQSLNKIQ SKCYPSAFDD
DGNMLVCAPT GSGKTNVGML AILREIGKHR NPETGDIDLD AFKIVCIAPL KALVQEQVGN
LGGRLEPYGI RVAELTGDRQ LTKQQIAETQ IIVTTPEKWD VITRKSNDLT YTNLVRLIII
DEIHLLHDDR GPVLESIVSR TIRKTEQTGE PVRIIGLSAT LPNYKDVASF LRVDTKKGLF
HFDGSFRPCP LRQEFVGVTD RKAIKQLKTM NDVCYNKVIE HVGTNRNQML IFVHSRKETA
KTARYIRDKA LESDTINQIL RHDAGSREVL NEASSQATDQ DLKDILPYGF GIHHAGMSRA
DRTDVENLFA HGAIQVLVCT ATLAWGVNLP AHTVVIKGTQ VYSPEKGSWV ELSPQDVLQM
LGRAGRPQYD TYGEGIIITT QSEMQYYLSL LNQQLPIESQ FVSKLVDNLN AEIVLGNVRT
RDEGVEWLGY TYLFVRMLRS PGLYQVGAEY EDDVALEQKR VDLIHSAAMV LRKSNLIKYD
EKTGKLQSTE LGRIASHYYI TFGSMETYNN LIQPSITTIE LFRVFALSAE FKYIPVRQDE
KLELAKLLGR VPIPVKESIE EPHAKINVLL QAYISRLKLD GLALMADMVY VTQSAGRILR
AIFEIAMKKG WASVAKTALD LCKMAEKRMW PTMSPLRQFP SCPRDVIQKA EKIDVSWSSY
FDLDPPRMGE LLGLPRAGRT VCGLVNKFPR VEVQAQVQPM TRSMLRVELS ITPNFEWDDS
IHGAAESFWI IVEDCDGEDI LYHDTFLLRK EYAESEQNEH IVDFTVPITD PMPPNYFVSV
ISDRWMHAET RLPVPFHKLI LPEKFPPHTE LLELQPLPVS ALKVSSYIDL YPVWKQFNRI
QTQTFNSLYK TDANVFIGAP TGSGKTVCAE FALLRHWTKG DVGRAVYIAP FQELVDSRLQ
DWQKRLSHLN GGKEIVKLTG ETATDLKLLE KGDLILATPT QWDVLSRQWK RRKNVQTVEL
FIADEVHLLG SSQGYVYETI VSRMHYIRTQ TELPLRIVAL SVSLANARDI GEWIDAKKHD
IYNFSPHVRP VPLELHLQSF TNTHFPSLML AMAKPTYLAI TQMSPDKPAM IFVPSRKQTR
ATARDLLAAA FADDDEDRFL HAEVEQMKPL LERINEEALA EALSHGVGYY HEALSQSDKR
IVKHLYDNGA IQVLVASRDV CWELNSTAHL VIVMGTQYFE GREHRYVDYP LSEVLHMFGK
ALRPSKDGRG RGFLMLPQVK REYYKKFLNE ALPVESHLHN YLHDVFVTEI STKMIESGDD
AINWTTFTYF YRRLLANPSY YSLTSTTHEG LSNYMSDLVE TTLRELSESK IIEFDEDDGS
VAPQNAAMIA AYYNISYITM QTFLLSLSAR TKLKGIMEIV TSATEFESIQ IRRHEDGLLR
RIYDRVPVKM SEPVYDSPHF KSFVLLQSHF SRMQLPIDLA KDQEVLLSRV LSLLSAMVDI
LSSEGHLNAM SAMEMSQMIV QGMWDRDSPL KQIPHFSPEV VKVANEFGIK DIFDFMEAMN
PDENADYNKL VKRLGLSQNQ LAQAANFTND KYPDLELEHE VLDEGEIRAG EPAYLNIKIA
RNLEEEDGDY DSTVHAPFYP SKKMENWWLV VGDEKTKSLL AIKRVTIGRE LNVRLEYTVP
SPGEHDLKLF LMSDSYVGVD QEREFSVTAA EGMDVDDDEE DEDEDEE
//
