ID U7PJL2_SPOS1 Unreviewed; 1166 AA.
AC U7PJL2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=ATP-dependent RNA helicase DOB1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1624_07920 {ECO:0000313|EMBL:ERS95843.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS95843.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; KI440852; ERS95843.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PJL2; -.
DR STRING; 1391915.U7PJL2; -.
DR eggNOG; KOG0948; Eukaryota.
DR HOGENOM; CLU_002902_0_1_1; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000018087; 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; 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};
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:UP000018087}.
FT DOMAIN 194..350
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 461..635
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 130539 MW; 548A7C514F589782 CRC64;
MDIDELFEVF DKPPSGPSQP QGGRATTPGD ASRKRKAVGL SEASAETANK AAKDVPAIPI
GETSNDADIS SAAEDVLMNE DDEEDEDEDE DEEDTNGDGN GVDKQNKRRK KDGEAEPVLT
DTFQTAESRE VAPASGFAPQ KETESLVLQH NIQHQVALPP DLNYEYVPLS EHKRPAEPAR
EYPFELDPFQ SMAISSIERE ESVLVSAHTS AGKTVVAEYA IAQCFKRNQR VIYTSPIKAL
SNQKFRDFMG EFGDVGLMTG DITINPTASC LVMTTEILRS MLYRGSEIMR EVAWVVFDEI
HYMRDKSRGV VWEETIILLP DKVRYVFLSA TIPNAFQFAE WIAKIHRQAC HVVYTDFRPT
PLQNYCFPAG GDGILLVVDE RGVFKEKNFN TAMALVEQNK GADPADPNAK QNGRGKNKKI
NKGGGNESTS DIYKIIRMIM KKNFHPVIVF NFSKRECEML ALKISGMNFN NESEQALVTK
VFENAIDTLS ETDRELSQIT HLLPLLRKGI GVHHSGLLPI LKEIVEILFQ ENLIKVLFAT
ETFSIGLNMP ARTVVFTQVR KFDGVSMRPL TSSEYIQMSG RAGRRGLDDR GIVIMMVDDK
LEPETAKAIV AGKQDRLNSA FHLGYNMILN LQRIETVSPE YMLERCFFQF QNAASVPAFE
KELKALQHER DSTIIPDENT VKEYYKLRQL IEEYRKDMVL VMQHPNFCLP FLQPGRLVHI
KTPGSGEDFG WGAVLSFSQR RAPKRGEDEV PPQESYCVDV ALFISDSKSA QSIAPGFPLG
EVAPGAVPWV DNANSSTASG SEDNGSGDNT SGNDKNSKTS KASRASKASN KKEDKDTNKE
KSNMTDARVE IVPCLLSTIV AMSKLRIFMP DNVTKSAGKD RTGKVIREVQ RRFPDGIPVL
DPIENMKIND ESFKKLIRKI ELLEAKLLAN PLHGSPILPE LWEKYHHKAE LGEKIKEKKK
AIAQAHSIAQ LDELKSRKTV LRRLGFINED DVVQLKARVA CQISSTEGHE LLLSELLFNR
FFNDLSPEVV ASVMTCFLFD EKVEAPDLKE DLAKPLREIK SQAKIIAKVS QESKLDINEE
EYVASLKWQL METVLAWAKG ASFADICKMT NAYEGSLVRL FRRLEELLRQ MAEAGKVMGS
EEITKKFEES LEKIKRGIVA AQSLYL
//
