ID A0A1E4T5W3_9ASCO Unreviewed; 2112 AA.
AC A0A1E4T5W3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=RNA helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CANARDRAFT_174242 {ECO:0000313|EMBL:ODV87149.1};
OS [Candida] arabinofermentans NRRL YB-2248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX NCBI_TaxID=983967 {ECO:0000313|EMBL:ODV87149.1, ECO:0000313|Proteomes:UP000094801};
RN [1] {ECO:0000313|Proteomes:UP000094801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-2248 {ECO:0000313|Proteomes:UP000094801};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV453848; ODV87149.1; -; Genomic_DNA.
DR STRING; 983967.A0A1E4T5W3; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000094801; 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; 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; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
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:UP000094801}.
FT DOMAIN 448..632
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 667..861
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1295..1471
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 165..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1761..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1762..1778
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2112 AA; 241710 MW; 3093EEB597A67829 CRC64;
MSESTNQYKY DEMSNKVLRT DKRLLDDGLE RNIITTPQSL IGKISVKDLD SSNLESYNYS
PTTPENNEIF DLILTWCSNQ LDNDVPDDIL RSLADILLEI LKADTLNEMI KKSKIEDTLD
GKLTDESFKE ILSLSNEITD YNVQDNGDHS DEEGLGIVID SEDEISNDED NDNDEDHEAS
GEEDAPKGDD DNDSSLVPDN DDILKLSKEN LDPKVHMIDI KSIDRLWLTR QIASTITELD
SYKHAELSIQ VFNLLKDSAA GKIDARRFEN SLHALFDFDN NMLIQKIMHN QMRVYYGIIL
SESPIDEKDT IFNEMISKDL ESLVNEYKGI RKHQDDDSET SHKLQRISET EKQSMNMEVK
KPKYLDLDSL VFDKGSRFMT TSKFQLPQGS FKRTRKSWEE IHIPPPKQPE LQEDERLVEI
SELPEWAQTV FPSSETKTLN RIQSKVYPTA FLEDSNILMC APTGAGKTNV AMLSILRTIS
KFMDDQGHLD LNNFKIVYIA PLKALVQEQV REFQRRLNQF GITVNELTGD SNLTKHQIAS
TQIIVTTPEK WDVITRKMSD ISYTSLVRLI IIDEIHLLHD ERGPVIESIV ARTQRNNDDS
NDEPVRLVGL SATLPNYKDV AELLRVNESK GLFYFDASYR PCPLAQQFIG ITEKKSLKRF
QAMNEICYEK VVENVSKGHQ VIIFVHSRKE TEKTAKWITE KLIENEKLAE IIKFTPGVEE
ILRSESEQAK SEGLKSVIPM GFGIHHAGMV KQDRSTAEDL FAQGYLKVLV STATLAWGVN
LPAHTVIIKG TNVYSPEKGS WVELSPQDIL QMLGRAGRPR YDTHGEGIII TAQDEVKYYL
AILNQQLPIE SQLISKLADN INAEIVAGTI QNMEDCVQWL SYTYLYVRMS RARLLYHIGP
SYDADTDLTE RRKDLAHSAL TILAKNGLIK YDYSKDLIAT TDLGKIASHY YISYRSMKNY
DKQLKPFMTE IDIFRMFSTS EEFKYVPVRQ EEKVELVKLM QQAPIPINES AEDPLAKINI
LLQAYISKLK LVGFALMSDM IYVVQSAGRL FRAMLEIAIK KKWSRLSKLL IDICKMVEKR
LWLTNSPLRQ FPNAPIEVIQ ITERSMTPWK HYLNLNDEYE VGQAFKSDRY GRLGFELLGK
FPRISVETSI QPITSTLVKI EVEVLPQWVW DTSIHGYSQS FKMIIEDCDS EKILHIDTLV
VMKEYVNQPH IIDCVVPLFD TTQPNYFVSF ISDSWLHCET KDPIMLMNLI VPKKFPAPYS
LMTIHSTPTS DLGIDEFSTV FPFENFNTLQ SHVLNSAYNS QDNLLFCCSK GNGKTTVAEL
TLLNHWREEK GRAVYLVPTQ EQVDRVFIDW KKRLSGVAGG KEINRLTGEL SADLKLLGSS
HLILATPEQF DLISRRWQQR RNIQSIELFI ADDCHTAGSG AQGTIYEVVL SRMRFIAANL
EKNIRIVALG SSIADSKNFG AWLGVPKQNI MNFDSTERVH PLEVKLHHSE ITHHPSFVLA
MIKSTYNAIS EMDEDIGEDK AIVFVPSRKY CVDVSKELIK RLNKDDVSWL RTDLESIEGR
LNKVIDLSLR ESLKFGIGYY YKSMQPSDRS MVEKLFDAGA LSCLLATKET SFWCPAANFV
VVLSTQEYEG KEHRYIDYSL NELQEMVGLA RLEKGTAKAL IFTNVTRLEY YKKFLAESLP
IESHLNFFLH DCFINEISTQ LIKNRQDCVD WLTYSYFYRR LQMNPTYYNL HEVSEVGVSE
YLSELIESTL NDLVEGKMIE AKLDDDDDDD DTSEDDEHES EGKIEITPLN GCMIAAYYNV
SFITMQTFAL SLNSKTKLRK LLEVVSSAYE FESIPIRKHE NEFLAKLYNR LPVKSSSEPN
FELPSFKAFL LLQAHFSRIN LPPDLTSDLN TILLKIVNLL YAAVDILSSE GNLNAMSAMD
LTQMVVQSQW DTDHPLKQIP YFENEIIAKC TEKKVETVYD IMALEDDERE EVMESLNDKQ
LNKVAEFVNK YPNLEISYEL DLSEPIVANQ PKEIVISIDR DEEAEDLSVS CSRYPFPKLE
NWWIVVGNQK TKQLFAIKKL MITKLSQQVK LSFTIPEAGE QRLSVWCMCD SYIDADKQIE
ITDVVVEAEA EE
//
