ID A0A3E2HIG2_SCYLI Unreviewed; 1279 AA.
AC A0A3E2HIG2;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RNA helicase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=B7463_g3202 {ECO:0000313|EMBL:RFU33177.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU33177.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU33177.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU33177.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RFU33177.1}.
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DR EMBL; NCSJ02000040; RFU33177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HIG2; -.
DR STRING; 5539.A0A3E2HIG2; -.
DR OMA; CGSDITR; -.
DR Proteomes; UP000258309; 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 CDD; cd18795; SF2_C_Ski2; 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; 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 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; 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 Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 321..477
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 604..805
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 228..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU33177.1"
FT NON_TER 1279
FT /evidence="ECO:0000313|EMBL:RFU33177.1"
SQ SEQUENCE 1279 AA; 143794 MW; 77C23EB0C979A879 CRC64;
MVPDLVEALE RVNLASKTLD DADDDWIDHI LEEQRPRKRI KPDRESLKRE LKQKYLTPAT
SFSTDWLNKL QQRWEIPPDY VSLFKLAPTQ TRTITRFTRE GLDGKVTGYK EVTVPANSST
AKNSTSFLRK PANRADFVRG AAGFFPFAPG GLEGVEAAAA LDEQALRAGS ITASGTSKLE
KIINISEGGL LEIAPGLSRG LNFDIKKEDV QGQDAEDVEQ MLDEELADNP GGAEATGENG
SMETPDAEED NEEDDIDLML PVEFPALEPH SALAASSARR GGREWAHMID VKRDIPNFHE
LVPDMAREWP FELDTFQKEA VYHLESGDSV FVAAHTSAGK TVVAEYAIAL AAKHMTKAIY
TSPIKALSNQ KFRDFRQVFD EVGILTGDVQ INPEASCLIM TTEILRSMLY RGADLIRDVE
FVIFDEVHYV NDLERGVVWE EVIIMLPEHV TLILLSATVP NTHEFASWIG RTKKKDIYVI
STSKRPVPLE HYLWADKGIF KIVDAEKRFI EKGWKDANDV LSGRDKVKAF PLQSNSDSRG
RGNQRGRGQP QRGGQRGGGQ QRGGAQQRGR GGPPRASHTP GHMGRTGKPG GRTTAAQDKN
LWVHLVQFLR KESLLPACIF VFSKKRCEEN ADALSNQDFC TAAEKSTIHM VIEKSVARLR
PEDRILPQIV RLRDMLGRGI AVHHGGLLPI VKEIVEMLFA QTLVKVLFAT ETFAMGLNLP
TRTVVFSGYR KHDGHAFRNL LPGEYTQMAG RAGRRGLDTV GSVIIVAPGG GEAPPVSELR
QMILGEPSKL RSQFRLTYNM ILNLLRVEAL KIEEMIKRSF SEHATQQLLP EHEKQVKLSE
ADLAKFKREQ CDICDQDLEL CHDAAKDFMQ LTHDLHLGLL ATPVGRRLFT PRRLVVYNRD
GIRTPGILLR EGATTGQAPT VHVLEIKTRR DQRDSTDLLP YLPKYRGMFT KLPQSKKHIS
TKTLYIPVSD LQSLTKTIVK DVIPGMFEGG EPYQAAMKEL ARICNSWEPD VWDELDLSRI
KELQLRDLIN RRSEQAKASQ TGNCLQCPQF LKHFAMRHDE WIIKENISQL RQLMSDQNLQ
LLPDYEQRIQ VLKNLEFIDE GSRVQLKGKV ACEIHSADEL VLTELILDNV LAAYEPAEIV
ALLSAFVFQE KTDMVPNLTS NLEAGMKTII EISEKVNERQ TYHQVILSAD DSNDFVSRPR
FGLMEVVYEW ARGMSFKNIT DLTDVLEGTI VRVITRLDET CREVKNAARI IGDPDLFTKM
QTCQEMIKRD ITAVASLYM
//
