ID Q6BI73_DEBHA Unreviewed; 2145 AA.
AC Q6BI73;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 126.
DE SubName: Full=DEHA2G12892p {ECO:0000313|EMBL:CAG90584.2};
GN OrderedLocusNames=DEHA2G12892g {ECO:0000313|EMBL:CAG90584.2};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG90584.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG90584.2, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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DR EMBL; CR382139; CAG90584.2; -; Genomic_DNA.
DR RefSeq; XP_462098.2; XM_462098.1.
DR STRING; 284592.Q6BI73; -.
DR GeneID; 2905011; -.
DR KEGG; dha:DEHA2G12892g; -.
DR VEuPathDB; FungiDB:DEHA2G12892g; -.
DR eggNOG; KOG0951; Eukaryota.
DR HOGENOM; CLU_000335_1_0_1; -.
DR InParanoid; Q6BI73; -.
DR OMA; KEQFRDW; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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; 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:UP000000599}.
FT DOMAIN 481..666
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 677..912
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1329..1506
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2119..2145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2121..2145
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2145 AA; 246439 MW; C28B0EE1228F8D5C CRC64;
MQEPNPEFNK QYKYEEMSNK VLRNDRTRRR DDKDDSNPVS LAGQISVKDM GTRVSQEKTS
DRPVIKEKDI PKQSNPNNYS YTGTLENISY HPTNEETAHI FDLIMVEIHN FLPDSSHDVI
ISAADSVLEI LKQEDTPPAE KRKEITELLD TKINDIEFNG LINLAKRITD YDIQMISEDM
DNEDNDQGIA VMFDNSDEEE DDGIEHNVAE EVEDDKQPEV SEEAENGLND EAVIKTNDKP
SKKETIVVPL HEIDQFYLQR KISSTLVDSD PSIIQQVTNK FVQFLSSYEL STRELENELM
ELMNYEHFDL IKFSIENRWR LVFKIKFLEN ESEESKQKIL EDMAKLKLDS LILEFENQSE
DATPGKKRKL SQDDDDESNK KTKTSIIKPK REPKIVDLDS MSFDQGSHLM TNTKIKLPQG
SYQQNKKLYD VISIPPPSPP PSLEECNEKL VSISELPEWT RCVFPSSETS SLNRIQSKIF
PSAFNSDENL LICAPTGAGK TNVAMLTILR AIHNYRDPET GQLDLRNFKI VYIAPLKALV
QEQMREFQRR LTANFGIIVN ELTGDSSLSK QQISETQVLV TTPEKWDVIT RKSSDLSYTN
LTRLIIIDEI HLLHDERGPV LESIISRTLR QVEYTNDPVR LVGLSATLPN YEDVANLLRV
DFKKGLFYFD SSYRPCPLEQ QFIGIKEKKA IKKLSAMNEA CYDKLLDCAN NKHQMIIFVH
SRKDTYKTAK WLHEKLVQDD KLDVVLKSDS GSREILKSEA EEMDNRSLKE IVPAGFGIHH
AGLNKRERSV VEDLFAQGHL QVLVSTATLA WGVNLPAHTV VIKGTETYSP ERGTWVQLSP
QDILQMLGRA GRPRYDKSGE GVIITSQDEI QYYLAILNQQ LPIESQLMTK LADNLNAEIV
LGTIKSREDA VNWLGYTYLY IRMLRSPALY HVGADYKDDE NLYWKRVDLI HSALTILHEN
KLLVYNHENG DIKSTELGKI SSHYYINYET INMYNNQLKP WSTEIDILKI FSMSGEFKFI
PVRQEEKIEV AKLLEKCPFP IRENPNDPLA KVNVLLQAYI SRLTLDGFAL MADMIYITQS
GGRLLRAIHE ITLRKNWSAL SKITLDLCKM VEKRMWLTNS PFRQFGALVP REIVKASENS
HLPWVSYFNL NASELAEAIN FKGNSQKAYD LLRQFPKLTL NTYAQPITAS LLRVQLEVIP
DWKWNPSIHG NFESFWLLVE DCGGEKILFS DYLRIYRNNA EKEHLVEFTI PILDPVEPVY
FITLINEKWL HSAWRVPLVI TDMKIPKKFP PFTDLLDLQS IPTASLKIPE FIETFEFSYF
NKFQSQVFQA LFNSNENVFI GASKGCGKTV CAELAILKHW KQNKGRIVYI NPTQEIIDKQ
LKIWRKIYSK ITEPSKVINK LSGDLTTDIG LLSSSHLVLA TPEQFEFVSR RWRQRKSVQA
IELLINDDAH MVGNGSRGIA YEILVARMRL ISTQVENGLR IIALSNSLSN GRDFGEWIGC
TKQNVFNFDP SNRFNKIKEI RLQASNFNDN DSFMQSLIRP SYQFLKDNTK EGKSIVFVPT
RKQCIETAFK YIQHSSNDNW SLLRTDLEIL EPYLKRITDK SLTECLSRGI GLYYNNMSQT
DKLIIEKLFN NNVLSILIAS KDTCYYCPSA NNIVVLSTQE FEGKEHRFID YSINNILEMV
GCCKDDVNEA KSLIFTNSAK LNYYNKFLNE ALPIESFLNV CLPDAFITEV STRTFKTRQD
CIDWLTFTYF YRRLLANPSF YDVKDTSHLG ISEFLSVLVE STLKELEEAK IIEIEESEDS
EESGEEEEEI VPLNGAMISA YYNVSFNTVK EFNRLGNKTK LKGILEIITS ASEFDVLPIR
QNEEAILSKV HNKVPVKASD VDYESPYFKA FLLLQAHFSR IPLPLDLAND QKVVLESALK
ILYACIDTLS SEGYLNAIHA MDLSQMIVQA VWNRDNPLKQ VPYFDEAILN RCKKGKVETV
YDIMSLEDEE RNDILRLGDD KLNKVAEFVN QYPNIDISYE LDLSETVKSN EPKEIIIKLE
RDEDMDDLNV VAPFYPFPKK ESWWIVIGDA SSRQLYAIKK ATIDKESQRI KMEFTIPNAG
HHNLSIWCMC DSYVDADKET SLEIEVEEGE EGEEAEADDE NEEEE
//
