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Database: UniProt
Entry: A0A0J9XI75_GEOCN
LinkDB: A0A0J9XI75_GEOCN
Original site: A0A0J9XI75_GEOCN 
ID   A0A0J9XI75_GEOCN        Unreviewed;      1227 AA.
AC   A0A0J9XI75;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Similar to Saccharomyces cerevisiae YLR398C SKI2 Ski complex component and putative RNA helicase {ECO:0000313|EMBL:CDO57126.1};
GN   ORFNames=BN980_GECA19s00120g {ECO:0000313|EMBL:CDO57126.1};
OS   Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Geotrichum.
OX   NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO57126.1, ECO:0000313|Proteomes:UP000242525};
RN   [1] {ECO:0000313|EMBL:CDO57126.1, ECO:0000313|Proteomes:UP000242525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO57126.1,
RC   ECO:0000313|Proteomes:UP000242525};
RA   Casaregola S.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010140}.
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DR   EMBL; CCBN010000019; CDO57126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J9XI75; -.
DR   STRING; 1173061.A0A0J9XI75; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000242525; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Gene3D; 1.10.3380.30; -; 2.
DR   Gene3D; 2.30.30.1160; -; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016438; SKI2-like.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   InterPro; IPR048727; Ski2_beta-barrel.
DR   InterPro; IPR040801; Ski2_N.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF8; HELICASE SKI2W; 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; PF21409; Ski2_beta-barrel; 1.
DR   Pfam; PF17911; Ski2_N; 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:CDO57126.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          290..446
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          578..755
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          490..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1227 AA;  138081 MW;  7752213D5337EC48 CRC64;
     MSIADIIDSI RVNISSNDPA VDFETFNTKV DETSDEYIQS TFLTPSTHFS NQWLNNLQEL
     PPVDPLSQAT ELFTLPDTRS NTGVRFKRAG LEGRVVAYEE YSITSDALSK TAKNSLSINR
     KTSSKLDFIQ GRAGFMPFTP GGVELPETPV NKQALHRDDN GLYDVPPGFP RGFIEEETAK
     EVNELIYDED EELTDSEDDQ SQELTNQIQN FAFSQSDENS KYSSKELDNL LPDEMTFGRV
     QASDAEALPK AKEWAHVVDV NKAIPNFSEL VPKPAKVFPF ELDTFQKEAV YHLEQGDSVF
     VAAHTSAGKT VVAEYAIAMA TRNMTKAIYT SPIKALSNQK FRDFKEVFDD VGILTGDVQI
     NSEANCLIMT TEILRSMLYR GADVIRDVEF VIFDEVHYVN NQDRGVVWEE AIIMLPEHVK
     LILLSATVPN TYEFANWVGR TKQRDIYVIS TPKRPVPLEH YLWAADAPYK IVDEHKKFLE
     PGYAQASNAV APKPNVASNG RGGGRGGSDA GRGRGGARGR GGRGANRGGG NTQSYVPSYN
     GRQSNNNTFG KRAFLKLCSH LKAKNLLPAV IFVFSQKLCT QYAVSLSSID YSTAKEKSEI
     HMFIDKAVSR LKKEDRNLPQ IQMIRELLGR GIGIHHGGLL PIVKETIEIL FAKSLVKVLF
     ATETFAMGLN LPTRTVIFGS IRKHDGHSLR TLLPGEYTQM AGRAGRRGLD PTGTVMIMTS
     EPFPTASSLR ELILGNPTKL HSQFRLTYNM ILNLLRIEAL RVEEMIKRSF SENANQVMLP
     EHQKTVKLNE QALSQLKRPP CMICDVDMDK VLPLIVRERE LHSSIMDDIS RTTIGRSMFT
     PGRVVVFKDE RNTRAMGIVT KFDDRKRLNL LTFTKLTAKP DKKGDIPFYT GIEGFGKKHL
     SNYFSINLPF GVSIVPVSSV EVISTVRLNM DIPSLIRGHP EEVKKSVNYL KGVLNHQSEL
     KELFIRGIRS PAILSKIHER DRLMLEIKQA KCIQCPTFVD SFLLDYKVFT IKQQIENLQQ
     LMSSENMDLL PDYEQRIEVL KELNYIDEEQ NVQLKGRVAC EINTGFELII TELVLDNFLA
     SYEPEEIVAL LSVFLFPGNT KVEPTTITPQ LDVGKAKIVE VVTKVLDVFE KHKVLVTQEE
     VEFLEKNRFG LMEVIYEWGR GMNFSEIMEL TDVAEGTIVR VISRMDEVCR QVMAAARIIG
     DSTLYDKMEA AQEKIKRDIV FCASLYL
//
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