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Database: UniProt
Entry: C4JT03_UNCRE
LinkDB: C4JT03_UNCRE
Original site: C4JT03_UNCRE 
ID   C4JT03_UNCRE            Unreviewed;      1071 AA.
AC   C4JT03;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=ATP-dependent RNA helicase DOB1 {ECO:0000313|EMBL:EEP80750.1};
GN   ORFNames=UREG_05592 {ECO:0000313|EMBL:EEP80750.1};
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP80750.1, ECO:0000313|Proteomes:UP000002058};
RN   [1] {ECO:0000313|Proteomes:UP000002058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010140}.
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DR   EMBL; CH476617; EEP80750.1; -; Genomic_DNA.
DR   RefSeq; XP_002584903.1; XM_002584857.1.
DR   AlphaFoldDB; C4JT03; -.
DR   STRING; 336963.C4JT03; -.
DR   GeneID; 8441098; -.
DR   KEGG; ure:UREG_05592; -.
DR   VEuPathDB; FungiDB:UREG_05592; -.
DR   eggNOG; KOG0948; Eukaryota.
DR   HOGENOM; CLU_002902_0_1_1; -.
DR   InParanoid; C4JT03; -.
DR   OMA; IMLKNYN; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000002058; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR   CDD; cd18024; DEXHc_Mtr4-like; 1.
DR   CDD; cd13154; KOW_Mtr4; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 2.40.30.300; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR048392; MTR4-like_stalk.
DR   InterPro; IPR025696; MTR4_beta-barrel.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016438; SKI2-like.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21408; MTR4-like_stalk; 1.
DR   Pfam; PF13234; MTR4_beta-barrel; 1.
DR   PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EEP80750.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002058}.
FT   DOMAIN          158..314
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          397..598
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1071 AA;  121062 MW;  F6275F2937EE8F9B CRC64;
     MDELFDVFEA APASGATPSQ PAKPRPKKDK SKKRQANGDV KEDAVITDVN GADQISAQSE
     TEPVLEVQTE QPEPKRPRIE PEPIVADTFE TEQSREIAAS AGLQTTQEGT AVVLSHQVRH
     QVALPPNYPY VPISAHKPPE KPARTWPFTL DPFQQVSIAS IERDESVLVS AHTSAGKTVV
     AEYAIAHCLK NNQRVIYTSP IKALSNQKYR EFAAEFGDVG LMTGDVTINP TATCLVMTTE
     ILRSMLYRGS EIMREVAWVV FDEIHYMRDK TRGVVWEETI ILLPDKVRYV FLSATIPNAM
     QFAEWITKTH GQPCHVVYTD FRPTPLQHYL FPAGGEGIRL VVDEKGGFRE ENFQKAMGEI
     ADKKGDDPAD TNARGKGKGK NKKTNKGGEK GPSDVFKIVR MIMMKSYNPV IVFSFSKREC
     EAHALTLKNL TFNDDSEKDM VSKVFNSAIE MLSDEDKKLP QIVNLLPLLR RGIGVHHSGL
     LPILKETIEI LFQENLIKVL FATETFSIGL NMPAKTVVFT NVRKFDGTSQ RWLTPSEFVQ
     MSGRAGRRGL DDRGIVIMMV NEEMDPTVVK EIVRGEQDKL NSAFYLGYNM ILNLLRVEGV
     SPEFMLERCF AQFQSASSVG TLEKELEELE SQRKNIIIPD EGTIREYYDS RQLLATYNEE
     MRLTICKPDY CQRFLDSGRL VNVQHEKHDF GWGLVVNFQQ RKAPRSMQEE YPPHESIIVD
     VLLNVAENAH FSYKSDQMLP PGVRPAKKGE NSTMAVVPMV LSCIKAFSTM RITLPKELKS
     DDSKKYTAKV LAEVQRRFPD GIPVLDPINE MGIKEEGFKR TLRKVEVVEA RLLANPLHNS
     PRLPELYDQY ATKVELGNKI KDTKRQISVA MSIIQLDELK CRKRVLRRFQ FINESEVVQL
     KARVACEISS GDELMLSELL FNGFFNTLTP EQCAAVLSVF VFEEKSKETP PITNEELAKP
     LRDIQAQARI IAKVGQESKL AINEQEYVES FRWELMEVIY QWAKGGSFAE ICKMTDVYEG
     SLIRTFRRLE ECMRQMAQAA KVMGSSDLES KFEASLSMVK RDIVAAQSLY L
//
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