ID A0A0A2IUG9_PENEN Unreviewed; 1079 AA.
AC A0A0A2IUG9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Upf1 domain-containing protein {ECO:0000259|PROSITE:PS51997};
GN ORFNames=PEX2_060770 {ECO:0000313|EMBL:KGO53470.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO53470.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO53470.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO53470.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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}.
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:KGO53470.1}.
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DR EMBL; JQFZ01000250; KGO53470.1; -; Genomic_DNA.
DR RefSeq; XP_016596072.1; XM_016743350.1.
DR AlphaFoldDB; A0A0A2IUG9; -.
DR STRING; 27334.A0A0A2IUG9; -.
DR GeneID; 27678769; -.
DR HOGENOM; CLU_001666_4_0_1; -.
DR OrthoDB; 170190at2759; -.
DR PhylomeDB; A0A0A2IUG9; -.
DR Proteomes; UP000030143; 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; 2.
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:UP000030143};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT DOMAIN 63..220
FT /note="Upf1"
FT /evidence="ECO:0000259|PROSITE:PS51997"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..103
FT /note="C3H"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 85..113
FT /note="CC/SHH/C"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 131..161
FT /note="C4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 951..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 118706 MW; 504C4AF708918795 CRC64;
MSYQPEDPSA GAEINEIALG RARPRRHDDE DEGSDTFEDD DMESIVGAPT NGHQKSQGNG
EEEIELPAHA CAYCGIHNPS SVVKCLSCNK WFCSARGNTS SSHIVNHLVR ARHKEVQLHP
GSSLGDTILE CYNCGTKNVF LLGFIPAKSD TVVVLLCRQP CASMPSSKDM NWDTSRWQPL
IEDRSFLPWL VGAPTDQEQL RARHLSPQLI AKLEEMWKDN SQATLEDLEK ATAVDDEPAP
VLLRYDDAFQ YQNIFGPLVK IEADYDRKLK ESQSQDGLIV RWDLGLNNKH LASFVLPKLE
LGDVKLAVGD EMRIKYNGEL RPKWEGVGYV IKIPNNQSDE VTIELRAKGD HKSVPTECTH
NFMADYVWKS TSFDRMQCAM KTFAVDEQSV SGYIFHRLLG HEVAAAPMKT QIPKKFSVPG
LPDLNGSQIN AVKSVLQRPL SLIQGPPGTG KTVTSATIIY HLAKINGGQV LVCAPSNVAV
DQLCERIHRT GLKTVRVTAK SREDVESAVG FLSLHEQVRM NDSNIELVKL NQLKAELGEL
SSQDEKRLKQ LTRSAEREIL TNADVICCTC VGAGDPRLSK GKFRTVLIDE STQSAEPECM
IPLVLGCKQV VLVGDHQQLG PVIMNKKAAK AGLNQSLFER LVILGCSPIR LNVQYRMHPC
LSEFPSNMFY EGSLQNGITI ADRVRRDVDF PWPIIDDPMM FWSNLGNEEI SASGTSYLNR
TEATNVEKIV TRFFKAGVQP RDIGIITPYE GQRSYIVSSM QATGTFKKEH YKEIEVASVD
AFQGREKDYI ILSCVRSNDH QGIGFLSDPR RLNVALTRAR FGLVILGNPK VLSKHPLWNC
LLQHFKERHC LVEGPLSNLQ ESLIQFSRPK QAYRGPQRFQ MSFSQTNNAP NNAVNGRNGG
HRNEYHDSGS VVGYIPDDVS SVHGSALGGV GLPSGYPPMF QNFGESWPAI SGGRRANGGR
PKGAPSVAGE SVAATESDVT CSVTDGRSVD QGGVSLTGLS INDMSKQPSL SQSDRLKRYV
ESGGREPYRA GVPDNGSIFG GSSASIRVTR GAPGQNPHDD DDARSVSTAF ASQVGGNYD
//
