ID M7X7R8_RHOT1 Unreviewed; 2190 AA.
AC M7X7R8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Pre-mRNA-splicing helicase BRR2 {ECO:0000313|EMBL:EMS26140.1};
GN ORFNames=RHTO_00568 {ECO:0000313|EMBL:EMS26140.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS26140.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS26140.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS26140.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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DR EMBL; KB722642; EMS26140.1; -; Genomic_DNA.
DR RefSeq; XP_016277259.1; XM_016414252.1.
DR GeneID; 27364581; -.
DR eggNOG; KOG0951; Eukaryota.
DR HOGENOM; CLU_000335_1_0_1; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase 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; 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; 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; 2.
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, ECO:0000313|EMBL:EMS26140.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 532..716
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 727..944
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1379..1555
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 20..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..254
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2190 AA; 245933 MW; 8275F0E41B0E9727 CRC64;
MPPNPSAYAG YQYHAMSTLV TTADRPRHRE NEPTGEAESL VGRINPKEMG ARAFREDLNV
EERRKKADKE RERRERKEVE GGARKSGRST VAGGMRYGDV LEATQDLEGL DYRPRTSETR
AVYELILSLV HTLLGDTPPA MVRSAADMIL GYLKDDSLKD LDKKREVESL LSMSVPNEKF
AELTALGKKI TDYGDEEDTG KGAAEDEDAD AGKIDDDVGV AVVFEEEEED EDQEDGEGFE
VRDEDTDEDE DERVEGPTGT GGGVGDDEMA TGADMDGDGD TVLVGGEGAP SARGKRGATK
DGSVPAREID GFWLQRLFAS SYPDPIEAAQ KTEQAMSLLS SEGNTRDVEN SLMDLTDYDK
FELVSTLVAN REKIVWCTKL ARSNDDEKMD VEVAMREKGV GWILKELRGE TSKSRANGDA
MDVDVATKPV TVGPAKGTLK PGEAAPPPRK VLDLESMAFA QGGRLMSNKK CKLPEGSFKR
SKKGYEEIHV PAPKPAPLKD GELVPVSSMP QWAQEAFKGN PTLNRVQSRL FPVAFGTDEP
LLLCAPTGAG KTNVAMLTIL NELAKHRNEA TGEFDFSAFK IVYVAPMKAL VQEMVGNFTK
RLSPYGVVVN ELTGDRQLTK QQIAETQIIV TTPEKWDVIT RKSTDTSYTN LVSLIIIDEI
HLLHDERGPV LESIVARTIR RMEQTHNYVR LVGLSATLPN FKDVARFLKV DPDKGLFYFD
SSYRPCPLKQ EFIGVTEKKA IKRYQVTNEI CYEKVLEHAG KDQVIIFVHS RKETAKTARF
LRDAAVENET ITQFLRADPA TREILTTEAE SVTDPNLKDL LPFGFAIHHA GMNRVDRTLV
EDLFGDGRIQ VLVSTATLAW GVNLPAHVVI IKGTQIYNPE KGRWVELSSQ DVLQMLGRAG
RPQYDTFGEG IIITNHSELQ YYLSMMNQQL PIESQFVSKL ADNLNAEIVL GTVRNRDEAV
QWLGYTYLYV RMLGTPSLYS VDPNYAEDDP LLEQKRSDIV HTAAVLLEKS GLVRYDRKTG
VFHSNELGRI ASGYYVTHNS MGVYNQHLKS ASGFIELFRI FSLSEEFKNV PVRPEEKLEL
AKLLERVPIP VKESVDDPSA KINVLLQAYI SQLKLDGFAL VADMVYVTQS AGRILRAMFE
ICLKRGWAAL THKALALCQM VEKRMWGTMT PLRQFKGVPL DVVRRAERKE FPWYRYFDLE
PAELGELIGE PKAGRLVHRL VHQFPKLELQ AHVQPITRSL LRVELTITPD FQWEEKVHGG
AESFWVLVED VDGEVILFHD QFLLRQRYAE QDHYVTFTVP MLDPLPPNYF ISVVSDRWLH
AETRLPLSFK HLILPEKFPP PTTLLDLQPL PVSALHNREF QALYSDIEAF NKIQTQVFQA
LYTANDNVFV GAPTGSGKTI CADFALLRLW SQAEPRRAVC IEPFQEIVDA RVAEWRTKFG
KLQGGKEVVA LTGETSADLR LLDKGDLIVC TPTQWDVLSR RWKQRKNVQT VGLVIADELQ
LIGGEIGPTY EVILSRTRYV AAQTENPTRI VAFGVSLANA RDLGEWLGCT AQTIFNFSPG
ARPLPMEVHL QSFNVPHFPS LMIQMAKPTY LAITEYANDR PVICFVPSRR QCRATADDIL
TYCLADQEES RFLNVEPSEL APHLEHVQDA GLRATLEHGV GFYHEALSKQ DKRVVEMLYN
SGAIQVVVAS KDVAWSMPLT AYMVVIMGVQ SFEGKEHRYV DYPFTDVLQM MGRACRPEHD
SSSRCVLMCQ QVRKDFFKKF LNEGLPIESH LHLSLHDHFN AEIVTKTIEN KQDAVDWLTW
TWMYRRLVAN PNYYNMQGTT HRHLSDHLSE LVESTLADLQ NSKAITVEDE MDVSALNLGM
IAAYYNINYV TMDIFSMSLT EKTKLKGLLE IVSSAAEFEN VPIRHHEDQL LRKVYDRVPV
KLANVDYESP HFKVNVLLQA HFSRLTLPAD LAADQAQILP KVITLLSACV DVAASSGYLN
AVGAMELAQC VTQATWDSDS PLKQIPHFSS EVIQRCQAAN VNSVYDLLEL EDTDRDKILQ
FTPRQMRDVA AFANRYPSVE VTYAIEDQDE LSAGEPIVVN VHLEREADED EEIDTTVIAP
FFPARKTEQQ YLVLAERSTK QLHAVKKVTV NRRLSTKLEM TLSKGSHDLV LLLICDSYLG
CDQEFELNDI KVAEAAESDD DSDGDEMDED
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