ID A0A1Y2AAS2_9PLEO Unreviewed; 2215 AA.
AC A0A1Y2AAS2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Sec63 Brl domain-domain-containing protein {ECO:0000313|EMBL:ORY19390.1};
GN ORFNames=BCR34DRAFT_595360 {ECO:0000313|EMBL:ORY19390.1};
OS Clohesyomyces aquaticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORY19390.1, ECO:0000313|Proteomes:UP000193144};
RN [1] {ECO:0000313|EMBL:ORY19390.1, ECO:0000313|Proteomes:UP000193144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115471 {ECO:0000313|EMBL:ORY19390.1,
RC ECO:0000313|Proteomes:UP000193144};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY19390.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCFA01000002; ORY19390.1; -; Genomic_DNA.
DR STRING; 1231657.A0A1Y2AAS2; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000193144; 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; 3.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000193144}.
FT DOMAIN 550..734
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 773..981
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1398..1574
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 30..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..265
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2215 AA; 250560 MW; 1CB93B6C36127374 CRC64;
MAEKKENNLA QFKYAAMSNL VLQADRRFVT RRGDENTGDP ESLAGRINIR DMGGRTARDD
APTDQKKPKG PFGVERGGIN EGADVFEREQ RKRKRGDGTG ALGTANQMSQ ADLLVEDLRY
KPRTPATRAT YELITTIVGK NLGDVPTHVT RSAADAVLEY LKDEDLKDFD KKKEVDDILG
ISMGPKEFNE LVSLGKKITD YEAQDEDEDA GEGANVDDDA EVDDNQGVAV VFDEEEDDEN
AGQTFEVRDE DTSDDEEDEE PADQDSDARG LERDLGDTEE MIIQGDVAAS TANKEETDQL
IPAHEIDAYW LQRQIGQIYE DAHTQQEKTR DALKILSGVS DDDDDEKPLR EIENDLMELF
DYEHHELVSK LVLNRDKVVW VTRWRRAAED QDERAAVERE MKAAGHRKIL DELRAREVGT
GATDSTGTKK IKIDLMDIDI PSASKDAEME DEPKHEGLRG GLQPSGRLIN LDNLVFDQGN
HLMTNPNVKL PQGSTRRQFK GYEEIHVPAP KARRDPNEAR NMPTTELPEW ARIGFGSSKE
LNRIQTKCFP TAFNDDGNML ICAPTGSGKT NVAMLAMLRE IGKHRDPRTG EINLDDFKII
YIAPLKALVQ EQVGNFGKRL EPYGIKVKEL TGDRQLTKQQ IAETQVIVTT PEKYDVITRK
ATDTSYINLV RLICIDEIHL LHDDRGPVLE SIVSRTIRRT EQTGEHVRLV GLSATLPNYR
DVASFLRVDT DKGPFHFDAT FRPCPLKQEF IGVTDKKAIK QLKTMNDVCY TKVLEQVGQN
RNQMLIFVHS RKETAKTAKY IRDKALESET IGQILRTDSA SREILREEAE AVQNTDLKDL
MPYGFGIHHA GMSRADRSSV EDLFADGSIQ VLVCTATLAW GVNLPAHTVI IKGTQVYSPE
KGSWVELSPQ DVLQMLGRAG RPQYDTYGEG IIITTQAEVQ YYLSLLNQQL PIESQFVSKL
ADNLNAEIVL GNVRTRDEGV EWLGYTYLFV RMLRSPGLYS VGADYEDDES LEQKRVDLIH
AAAHVLEKCS LVKYDKKSGR LLPTELGRIA SHYYISHNSM ATYNRHIQPG VTSIELFRVF
ALSEEFKYIP VRQEEKLELA KLLGRVPVPV KEGVEEPQAK INVLLQAYVS RLKLEGLALM
ADMVYVTQSA GRILRAIFEI CLKKGWAEVA KAALDLCKMA EKRMWPTMSP LRQFPSCPKE
IILKAERMDV PWKNYFDLDP PNMAEMMGLP KAGKAVCQLV QKFPRLELEA MFQPMTRSML
RFELTIKPNF EWDDQLHGAS EAFWILVEDC DGEEILFHDQ FILRKDFAES DHIVEFAVPL
TEPLPPNYFV TLLSDRWMNA ETKMPVSFRK LILPEKFPPH TSLLELQPLP ISELKRREYQ
QLYEGINSFN RVQTQVFNSL YTSDETVFIG ASAGIGKTFC AEFAILRHWS GDNEGRIVYL
APYQSLVDNQ YKGWQARLSG LRGGKDIVKL TGETSADLRL LEKGDLILAT PTQWDVMSRQ
WQRRKNVQTV ALLIADDLHM LGGSGGHVYE TVVSRMHAMA AQLESRMRIV GLSVSLSNAR
DIGEWIGATK HTIFNFSPRV RSVPLELHIQ SFTIPHFPSL MLAMAKPTYQ AIAQYSPDKP
IMVFVPSRKQ TRGTALDLFS ACVIENDDDR FLNAPLEDIQ PILAKVNEQV LRESLSHGIG
YFHEALSPFD KKAVQHLFKV GAIQVMIVSR DSCWEVENNA HMVVIMGTQF YEGREHRYVD
YPISEILQMF GKAGRVGEDK SAKGFLFLPA VKRDFYKKFL DEALPIESSL HVFLHDAFVA
EISAKTIEST QEAVDWSTYT YFYRRLLANP SYYGLHDVSH EGLSAHLSEL VESILKELAD
ASLIEHDEEE DTITPLNPCM IAAYYNISFI TMQTLMMSLN AKSNIRSVLE IVTAATEFES
IQIRRHEDHI LRRIYERIPY KVEAPNFESP DFKAFVLLQA HFSRMQLPID LAKDQEAVLK
KVLNILSASV DVLSSEGHLN AMVAMEISQM VVQGMWQKDS PLKQIPHFDT DTVKAAEKFG
ITDIYEFMEA MDPEENKDYK KLIQALGLDN RQLADAANFT NDYYPNVEMS FQVVDPEDIT
ANAPSYINVV VSRELEDDDE PKTEVHAPFY PAEKTENWWL IVGDQKTNSL LAIKKITVGR
ELKTKLEFTV PEPGEHELTL LLVSDSYLGV DQAPTFKVNA AEGMDEDESE EEESE
//
