ID A0A0D2CVK4_9EURO Unreviewed; 1075 AA.
AC A0A0D2CVK4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Upf1 domain-containing protein {ECO:0000259|PROSITE:PS51997};
GN ORFNames=PV05_06510 {ECO:0000313|EMBL:KIW54127.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW54127.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW54127.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW54127.1,
RC ECO:0000313|Proteomes:UP000054342};
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 xenobiotica CBS118157.";
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; KN847320; KIW54127.1; -; Genomic_DNA.
DR RefSeq; XP_013314711.1; XM_013459257.1.
DR AlphaFoldDB; A0A0D2CVK4; -.
DR STRING; 348802.A0A0D2CVK4; -.
DR GeneID; 25328418; -.
DR HOGENOM; CLU_001666_4_0_1; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000054342; 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:UP000054342};
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 22..58
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 967..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1075
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 1075 AA; 118557 MW; B205F9CEF781D163 CRC64;
MEAFSNMGNH LVSNSAAAIN ASDDISTVDP DESILSLAKG PRRRQHDDDE SESIEEDDLE
SLASAAVDGK KQVTKAEEER ELPAHACAYC GIHNPSSVVR CLSCSKWFCS ARGNTSSSHI
VNHLVRARHK EVQLHPSSSL GDTVLECYNC GTKNVFLLGF IPAKSDTVVV LLCRQPCAAM
PSSKDMNWDT SRWQPLIEDR SFLSWLVAQP TDQEQLRARH LSPQMIAKLE ELWKENSAAT
ITDLEKASNI DDEPAPVLLR YDDAYQYQNV FGPLVKIEAD YDRKLKESQS QDNLIVRWDL
GLNNKHLANF ILPKLELGDV KLAVGDEMRI KYTGDLRPAW EGVGYVIKIP NNQSDEVTIE
LRSKGDHKTV PTECTHNFTV DYVWKATSFD RMQLAMKTFA IDEMSVSGYI FHRLLGHEVA
AAPMKTQMPK KFSVPGLPEL NSSQINAVKS VLQKPLSLIQ GPPGTGKTVT SATIIYHLSK
INGGQVLVCA PSNVAVDQLC ERIHLTGLKV VRVTAKSRED VESPVGFLSL HQQVRMNDSN
VELGKLNQLK SELGELSSQD EKKYKSLTRA AEREILQNAD VVCCTCVGAG DPRLAKSKFR
TVLIDESTQS AEPECMIPLV LGCKQIVLVG DHQQLGPVIM NKKAAKAGLN QSLFERLVIL
GCAPIRLNIQ YRMHPCLSEF PSNMFYEGSL QNGVTAEYRI RKEVDFPWPV VNSPMMFWSN
LGNEEISASG TSYLNRTEAA NVEKIVTRFF KAGVKPGGIG VITPYEGQRS YIVSSMQVNG
TFKKELYKEI EVASVDAFQG REKDYIILSC VRSNDHQGIG FLSDPRRLNV AMTRAKYGLV
ILGNPKVLSK HPLWHYLLLH FKERNCLVEG PLTNLQISLH QFSRPKQSYR GPQRYQMAYN
HASHMASGMM NGRGGPRNDY RDGGSVVGYI PDDVSSIHSS AMGGVGVSAG YPPMFQGFTP
DTWPALQNAS GRRQNGHKPR GVPGSVAGES TVATESDVTG STIGQGGVSL EQLSIHDINK
HTSYNQADRL KRYVEGGIPN TGYTGNSRLG KGIHQDEDAQ SVSTAFASQV GGGYD
//
