ID A0A0D0DMS0_9AGAM Unreviewed; 1066 AA.
AC A0A0D0DMS0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Upf1 domain-containing protein {ECO:0000259|PROSITE:PS51997};
GN ORFNames=PAXRUDRAFT_30067 {ECO:0000313|EMBL:KIL00093.1};
OS Paxillus rubicundulus Ve08.2h10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=930991 {ECO:0000313|EMBL:KIL00093.1, ECO:0000313|Proteomes:UP000054538};
RN [1] {ECO:0000313|EMBL:KIL00093.1, ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIL00093.1,
RC ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
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; KN824842; KIL00093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0DMS0; -.
DR STRING; 930991.A0A0D0DMS0; -.
DR HOGENOM; CLU_001666_4_0_1; -.
DR InParanoid; A0A0D0DMS0; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000054538; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR006935; Helicase/UvrB_N.
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; PF04851; ResIII; 1.
DR Pfam; PF18141; UPF1_1B_dom; 1.
DR Pfam; PF09416; UPF1_Zn_bind; 1.
DR SMART; SM00382; AAA; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
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:UP000054538};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT DOMAIN 84..239
FT /note="Upf1"
FT /evidence="ECO:0000259|PROSITE:PS51997"
FT REGION 92..124
FT /note="C3H"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 106..134
FT /note="CC/SHH/C"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 152..182
FT /note="C4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 1035..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 118073 MW; 834125E73B43539A CRC64;
MDSFDNFQYD SASSYGGARS VVDDNSSVYT ANTNAPVDLS SLSIADDRSQ TASNEHDGHL
HHTTRATIDE DFDAVLDDLK DEGAVDLPLH ACSYCGIHSP ASVVKCLVCS KWFCNSRGNT
SASHIVNHLV RAKHKEVILH AESPLGETTP ECYNCGSKNV FMLGFIPAKS DTVVVLLCRQ
PCAATTKDMS WNAALWAPLI DDRSFLSWLV KPPSETEQLR SRQISFNQIN RLEDLWRENA
NATLEDLEKP GVDDEPQSIL MRYEDAYQYQ NIFGPLVKIE ADYDKRLKES QTQTDITVRW
DLGLNQKRVA WFCLPKLESG EVRLAVGDEL RLRYQGELHK AWDGVGHVIK IPNNVSDEIG
LELRRTEGVP TDCTHGFSAD FVWKSTSFDR MQLAMKTFAV DEKSVNGYIY HKLLGHEVEP
QVLRTQMPKR FSAPGLPELN HSQMYAVKSV LQKPLSLIQG PPGTGKTVTS ASIVYHLAKM
NPGQVLVCAP SNVAVDQLTE KIHATGLKVV RLTAKSREAL DSSVAFLTLH QQVANSTTHV
ELQKLIQLKN EQGELSSNDE RKYKTLIRQC EKEILSAADV ICCTCVGAGD PRLSKFKFRT
VLIDEATQAA EPGTSSLALE CMIPLVLGCK QVVLVGDHQQ LGPVIMNKKA ARAGLTQSLF
ERLVVLGNRP IRLQVQYRMH PCCSEFPSNM FYEGTLQNGV TAPERLRKNV DFPWPVPDTP
MFFYQNLGQE EISSSGTSFL NRTEASNVEK IVTKFFKSGV VPAQIGIVTP YEGQRSYIVN
YMQFNGSLKK DLYKEIEVAS VDAFQGREKD YIILSCVRSN EHQGIGFLND PRRLNVALTR
AKYGIVILGN PKVLSKHPLW HYLLTHYKEK NCLVEGPLNN LQPSMIQFSK PRRALKMDSF
RRYETNAREY IPNNGTGRSG TPIRFDPGFY RTHDALAYIP SDVQSLRSQA TYSSGLPMFA
ATGGFPPGVP RGPGGAGKRS AYGSYASSIV SQDAGPASIA SIGGSVGGSL AYSQSDRLRR
RGSFSSAAGT DMGSMSGYDY KSQDETTDTE DMKSQYTGTQ SGVTVF
//
