ID A0A0D2B420_9EURO Unreviewed; 1072 AA.
AC A0A0D2B420;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Upf1 domain-containing protein {ECO:0000259|PROSITE:PS51997};
GN ORFNames=PV08_08618 {ECO:0000313|EMBL:KIW13430.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW13430.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW13430.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW13430.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
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DR EMBL; KN847497; KIW13430.1; -; Genomic_DNA.
DR RefSeq; XP_016233646.1; XM_016382943.1.
DR AlphaFoldDB; A0A0D2B420; -.
DR STRING; 91928.A0A0D2B420; -.
DR GeneID; 27335701; -.
DR VEuPathDB; FungiDB:PV08_08618; -.
DR HOGENOM; CLU_001666_4_0_1; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd21407; 1B_UPF1-like; 1.
DR CDD; cd18039; DEXXQc_UPF1; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21400; ZBD_UPF1-like; 1.
DR Gene3D; 2.40.30.230; -; 1.
DR Gene3D; 6.10.140.1240; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR040812; UPF1_1B_dom.
DR InterPro; IPR018999; UPF1_CH/ZBD.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF364; REGULATOR OF NONSENSE TRANSCRIPTS 1; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF18141; UPF1_1B_dom; 1.
DR Pfam; PF09416; UPF1_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51997; UPF1_CH_RICH; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01341}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT DOMAIN 79..236
FT /note="Upf1"
FT /evidence="ECO:0000259|PROSITE:PS51997"
FT REGION 23..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..119
FT /note="C3H"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 101..129
FT /note="CC/SHH/C"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 147..177
FT /note="C4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 1047..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 118034 MW; F375A6B7A0B9D873 CRC64;
MEAFSNMGNH LVSNSAAAIN ASDDISTVDP DESVLSLAKG PRRRQHDDDE SESVEEDDLE
SLASAAVDGK KQATKAEEEK ELPPHACAYC GIHNPSSVVR CLTCSKWFCS ARGNTSSSHI
VNHLVRARHK EVQLHPSSSL GDTVLECYNC GTKNVFLLGF IPAKSDTVVV LLCRQPCAAM
PSSKDMNWDT SRWQPLIEDR SFLSWLVAQP TDQEQLRARH LSPQMIAKLE ELWKENSAAT
ITDLEKASNI DDEPAPVLLR YDDAYQYQNV FGPLVKIEAD YDRKLKESQS QDNLIVRWDL
GLNNKHLASF ILPKLELGDV KLAVGDEMRL KYTGDLRPAW EGVGYVYKIP NNQSDEVTLE
LRAKGDHKSV PTECTHNFTA DYVWKATSFD RMQLAMRTFA VDEMSVSGYI FHRLLGHEVA
AAPMKTQMPK KFSVPGLPEL NSSQISAVKS VIQKPLSLIQ GPPGTGKTVT SATIIYHLSK
INGGQVLVCA PSNVAVDQLC ERIHRTGLKV VRVTAKSRED VESPVRFLSL HEQVRMNDSN
VELSKLNQLK SELGELSSQD EKKYKSLTRS AEREILQNAD VVCCTCVGAG DPRLAKFKFR
TVLIDESTQS AEPECMIPLV LGCKQVVLVG DHQQLGPVIM NKKAAKAGLN QSLFERLVTL
GCAPIRLNVQ YRMHPCLSDF PSNMFYEGTL QNGVTAEHRT RREIDFPWPV VQSPMMFWSN
LGNEEISASG TSYLNRTEAA NVEKIVTRFF KAGVKPADIG VITPYEGQRS YIVSSMQANG
TFKKELYKEI EVASVDAFQG REKDYIILSC VRSNDHQGIG FLSDPRRLNV AMTRAKYGLV
ILGNPKVLSK HPLWHYLLLH FKGSNCLVEG PLTNLQISLH QFSRPKQSYR GPQRYQMAYN
HATHMASGMM NGRGGPRDGG SVVGYIPDDV SSIHSSAMGG VGVPAGYPPM FQSFTADTWP
SLQNANGRRS NGVKPRGVPG SVAGESTVAT ESDVTGSVIG QGGVSLDQLS IHDVTKHASY
NQADRLKRYV EGGVPNAGYM GGSSRFGKGM HQDEDAQSVS TAFASQVGGG YD
//
