ID A0AAD3Y9D8_9TREE Unreviewed; 1263 AA.
AC A0AAD3Y9D8;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=Antiviral helicase {ECO:0008006|Google:ProtNLM};
GN Name=SKI2 {ECO:0000313|EMBL:GMK53589.1};
GN ORFNames=CspeluHIS016_0101750 {ECO:0000313|EMBL:GMK53589.1};
OS Cutaneotrichosporon spelunceum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=1672016 {ECO:0000313|EMBL:GMK53589.1, ECO:0000313|Proteomes:UP001222932};
RN [1] {ECO:0000313|EMBL:GMK53589.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HIS016 {ECO:0000313|EMBL:GMK53589.1};
RX PubMed=37821828; DOI=10.1186/s12864-023-09718-2;
RA Kobayashi Y., Kayamori A., Aoki K., Shiwa Y., Matsutani M., Fujita N.,
RA Sugita T., Iwasaki W., Tanaka N., Takashima M.;
RT "Chromosome-level genome assemblies of Cutaneotrichosporon spp.
RT (Trichosporonales, Basidiomycota) reveal imbalanced evolution between
RT nucleotide sequences and chromosome synteny.";
RL BMC Genomics 24:0-0(2023).
RN [2] {ECO:0000313|EMBL:GMK53589.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HIS016 {ECO:0000313|EMBL:GMK53589.1};
RA Kobayashi Y., Kayamori A., Aoki K., Shiwa Y., Fujita N., Sugita T.,
RA Iwasaki W., Tanaka N., Takashima M.;
RL Submitted (JUN-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GMK53589.1}.
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DR EMBL; BTCM01000001; GMK53589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD3Y9D8; -.
DR Proteomes; UP001222932; Unassembled WGS sequence.
DR GO; GO:0055087; C:Ski complex; IEA:TreeGrafter.
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:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IEA:TreeGrafter.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR FunFam; 3.40.50.300:FF:000354; ATP-dependent RNA helicase SKI2; 1.
DR FunFam; 1.10.3380.30:FF:000001; Ski2 ATP-dependent RNA helicase; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 1.20.1500.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR025696; Beta-barrel_MTR4.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR050699; RNA-DNA_Helicase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR InterPro; IPR040801; Ski2_N.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL-RELATED; 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 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP001222932};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 313..471
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 595..783
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 145..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..589
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 140077 MW; AE7EA5336AD6A5C3 CRC64;
MGDNKTPNGG ALPNLERFLE LLAAAANPTS SKLASEDLAQ SLGIQGLPTP TDAVKQLESD
VLSPPTSLSE DLWRWQVPLP TQVPLPPLTL TTLPATHTVA PTFRGIDGTF THWRDALAPK
QPLHPNVSSS MQRQPGALKN FVRGKSTNAP FLPGGLDPVA ASEEPVEDLP EEEGWKTRAP
GLKRGIQLDG ADEFLAEMLG QQSMTPKARR RKRGGDESPT LEVSRLGDDD IPAPDSDEGL
GAPSSRKNVD DLLPVGRLPA PPPPRKNLIK AAEKKEWAHV VDVNQELVNF RELVPEMARE
YPFELDNFQK EAVYRLEMGD SVFVAAHTSA GKTVVAEYAI ALAAKHMTRA IYTSPIKALS
NQKFRDFKTT FDPSTVGILT GDVQINSEGS CLIMTTEILR SMLYKGADLI RDVEFVIFDE
VHYVNDAERG VVWEEVIIML PEHVNIILLS ATVPNTKEFA DWVGRTKRKN IYVISTPMRP
VPLEHFLWAG KELHKIVDSK GQFLGNGYKS AGEALRRKQD KEREAAGLPP LTRTGGRGGA
PIKARDLPTG KSAPFTRTGG GRTHANRGGG QGAAAPAQRG GGGGGGGGRR PGRGQLDQNI
WTHLIAHLRK NKLLPVVNFV FSKKRCEEYA QTLSSTDLCD AKEKSEVHIV WDRALQRLKG
SDRTLPQILR MQVVEILFAR GLVKVLFATE TFAMGVNMPA KSVVFSGIRK HDGTGFRNLL
PGEYTQMAGR AGRRGLDTTG TVIILSGGDE LPGMKELQEM MLGVPNRLTS QFRLTYNMIL
NLLRVEALKV EEMIKRSFSE NAAQKLAPEQ QKQVEQTEKI LAKLPNVECD VCSADISAFY
DLSSEVVRVN AQIVRQAAWA PGKQFSPGRI VLLRDGHYPG NLAVILRKAP SFMQDGVKRD
TRAFWVLALV TKGQKSKRED IKDSDVMPRW PPTLPKSINN PQREVVAVDS TSVAFVTSRM
LKIDVTSILD NRSKEASLKT MNELVDIQAD LASGNSFEEF DWSRLSMLEF QELLRQRIAL
SDRISKLSCQ LCKDFEDHYE IIHERKQVEN SLKALQLALS DQNLELLPEY NSRIEVLKEL
QFIDENATVL LKGRVACEIN SAHELILTEL ILDNVLADYS PEEAVALLSV FVFVEKTDSQ
PQIPAKIAQG LDIIYTIADK VENTQLRQHV AFDDFREKFK PGLVEVVYEW ARGMPFSEIT
NLTDVPEGSI VRIITRLDET CREVRDAARV IGDADLFQKM EEAQALIKRD SEYDFVFAAS
LYL
//
