ID A0A1G4IM94_9SACH Unreviewed; 1265 AA.
AC A0A1G4IM94;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JAN-2026, entry version 37.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=LAMI_0A02190G {ECO:0000313|EMBL:SCU77743.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU77743.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|EMBL:SCU77743.1, ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11717 {ECO:0000313|EMBL:SCU77743.1};
RA Devillers H.;
RL Submitted (MAR-2016) 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}.
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DR EMBL; LT598462; SCU77743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4IM94; -.
DR STRING; 1230905.A0A1G4IM94; -.
DR OrthoDB; 64767at2759; -.
DR Proteomes; UP000191024; Chromosome A.
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:UniProtKB-EC.
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; 3.40.50.300:FF:000987; DEAD/DEAH box RNA helicase; 1.
DR FunFam; 1.10.3380.30:FF:000001; Ski2 ATP-dependent RNA helicase; 1.
DR FunFam; 1.10.3380.30:FF:000004; Superkiller viralicidic activity 2-like 2; 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-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; IPR048727; Ski2_beta-barrel.
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; 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 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000191024};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 329..487
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 593..792
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 535..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..572
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 144089 MW; 11562E34E95FA5E6 CRC64;
MSISYDLEAL ESIYRSLRDI PNEEPPKFVN LKSKADVNED STSTREEIAR KFLTPSNVLP
WQLLNILQVV PANTFHTDNE HVDDDGFDYR SLLEIPEYID RTCLQFRRVG LEGKIYDYKE
TVNLTDVANA NASNSLSLSR RVNQDTNSVR GTTGQLPFAP GGLTMSAINH TAEPSSISAA
TKLLHRDDEG LFDVPPGLER GITPSMAEHL KSSEINEVRR LDVIDDGGKN AQELADRRVE
DEQVVEEEAS KLLSASESKV AAPEADIDDL LPVGIDFGRT IRRPDDMLAR KEWAHVIDLN
HKIENFDELI PNPARKWPFE LDVFQKEAVY HLEQGDSVFV AAHTSAGKTV VAEYAIAMSK
RNMTKTIYTS PIKALSNQKF RDFQETFDDV DIGLITGDVQ INPEANCLIM TTEILRSMLY
RGADLIRDVE FVIFDEVHYV NDQDRGVVWE EVIIMLPQHV KFILLSATVP NTYEFANWIG
RTKQKDIYVI STPKRPVPLQ INVWAKGELI PVISEKREFL LTNFKKHKEL LAGKSASAAS
NGRDDRNSRP SGRGNMIRGG SKVRGGSRGA GAVGSNKSGF FKRSVPNKKT WPNLVNYLRS
KQLLPAVIFV FSKNRCEEYA DWMEGVNFCS GKEKSQIHMF VERSITRLKK EDRELPQIVK
MRSLVERGIA VHHGGLLPIV KELIEMLFAK GLISVLFATE TFAMGLNLPT RTVVFSEIQK
HDGNGLRNLN PGEFTQMAGR AGRRGLDDTG TVIVMAYTSP LEQGTFKEVA LGVPTKLQSQ
FRLTYNMILN LLRIEALRVE EMIKYSFSEN TKQTLLPEQE KKIKVLQSEL DSIQFADCEN
CEVDIDKALD ATIRYRKCTE QIMKELSDGA TVFRLLNVGR LILFRDLDDN AKLGFVFKNI
QRDNNTVVMT ITAPNCLKDG SPNHLPYLSG FPNFVKRNFQ TFKRIDYIME NVPFSDIEII
SAFTLNVSMT DVMKQDEDAL KKFNAEVSLI LKIAAKLREV TYEKKGSLKM YQLVQDRNKI
RDEFKTFTCL TSDKFAEHFV PKFREFQIQR EIKNLYHLMS DQNLNLLPDY EQRLSVLKDT
GFIDQNHNVL LKGRVACEIN SGYELVLTEL ILDNFLGEFE PEEIVALLSV FVYEGRTREE
EPLITTPRLT RGKKRIQEIY QRMLDEYEKF QVPLTKEEAE FLEKKRFALM NVVYEWARGL
SFKEIMEMSV ESEGTIVRVI TRLDEVCREV KTASIIIGDS SLHMKMSQAQ ELIKRDIVFA
ASLYL
//
