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Database: UniProt
Entry: A0A109UYE3_9SACH
LinkDB: A0A109UYE3_9SACH
Original site: A0A109UYE3_9SACH 
ID   A0A109UYE3_9SACH        Unreviewed;      1275 AA.
AC   A0A109UYE3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=HCL218Cp {ECO:0000313|EMBL:AMD19933.1};
GN   ORFNames=AW171_hschr31796 {ECO:0000313|EMBL:AMD19933.1};
OS   Eremothecium sinecaudum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=45286 {ECO:0000313|EMBL:AMD19933.1, ECO:0000313|Proteomes:UP000243052};
RN   [1] {ECO:0000313|EMBL:AMD19933.1, ECO:0000313|Proteomes:UP000243052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58844 {ECO:0000313|EMBL:AMD19933.1,
RC   ECO:0000313|Proteomes:UP000243052};
RA   Dietrich F.S.;
RT   "Genome sequence of the yeast Holleya sinecauda.";
RL   Submitted (JAN-2016) 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; CP014243; AMD19933.1; -; Genomic_DNA.
DR   RefSeq; XP_017986929.1; XM_018131183.1.
DR   AlphaFoldDB; A0A109UYE3; -.
DR   STRING; 45286.A0A109UYE3; -.
DR   GeneID; 28723160; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000243052; Chromosome iii.
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   CDD; cd18795; SF2_C_Ski2; 1.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          333..491
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          603..802
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          536..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1275 AA;  145903 MW;  590BB33AE03ACD4A CRC64;
     MSTSSPNDEH LDQLFHELRI SNINGSENFN DQLATYIPDP LPKKFEDICK KYLSQPNTLP
     WELLDLLQDV PKPDFMEDGS SSVKNQRNNY DFIDFVKIPE PLSRTSYHFK RKGIDGKIFQ
     YNEEVNLSEV ENANAANCLN LNRKINREAN SLKGSTSQLP FTPGGVTMSA LQLSSEGSKF
     ATATKLLHRD AQGLFDIPQG MQRGIIPDAP AGGYSDQIHE VKELDSIDNE DEKNKELITL
     RNERKVDHVL HPDSAQESGS NKDKETDLME IDRLLPMGID FGRIIRDPKA TLEKKRWAHV
     VDLSHRLENF DILVPKPART WPFELDIFQQ EAIYHLEKGD SVFVAAHTSA GKTVVAEYAI
     AMSQRNMTKV IYTSPIKALS NQKFRDFKED FDDVEIGLLT GDVQINPTAS CLIMTTEILR
     SMLYRGADLI RDLEFVIFDE VHYVNDQDRG VVWEEVIIML PSHVKFILLS ATVPNTFEFA
     DWIGRTKQKN IYVISTPKRP VPLEINIWAT EKMIPVVNEN REFSASNFKK HVDLLKGDVK
     PSNTPQNSKQ WKPNNSRTTG RGGNKAASDN KRITSGARGP GARGSNRSDF FRRDFPNKQS
     WSKIVNYLKN RELLPAVIFV FSKKNCEDYA ESLVGMDFAT AKEKSQIYMF IEKSISRLKK
     EDRELPQILK MRSFLERCIA VHHGGMLPIV KELVEMLFAK GYVKVLFATE TFAMGLNLPT
     RTVVFSAIEK HDGNSLRYLN PGEFTQMAGR AGRRGKDKVG TVILMTYKRP IEEIPFKEVT
     LGQPTRLKSQ FRLTYNMILN LLRIEALKVE EMIKYSFGEN TKQNLLPEHA KKAESLQDKL
     MELEDIDCKV CADDIETAID LTIKIRDCNR GIINDMDKNK KLFRLMKPGK LTVYRDTNGN
     AKLGSVLRID MSSGMCSMLC FTKPSTLRNG QVNHLPYLTD SKTFIKKHFQ AFSYASPVVD
     QIPFHNIELL SKYVVNLPLH ELINKDKKTL ASFHEKVHMF FRLAPKLKET NMDKEMTLAI
     QQFILDRKHA EEEFFNLKCI GCEHFAEHFS IKYQKHEVTQ EIKNVVHLMS DQNLSLLPDY
     EQRLAVLREC EFIDPSNNVL LKGRVACEIN SGYELVLTEL ILDNFLGDFE PEEIVALLSA
     FVYEGRTKEE EPLITTPRLA KGKKRIAEIY ERLLKVYETH QVPLTKDEAE FLEKKRFALM
     NVVYEWARGL SFKEIMSISV EAEGTIVRVI TRLDEICREV KLAASIIGYS TLHMKMSQAQ
     ELIKRDIVFA ASLYL
//
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