RENT1_NEUCR
ID RENT1_NEUCR Reviewed; 1093 AA.
AC Q9HEH1; Q7RVU9;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Regulator of nonsense transcripts 1 homolog;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P30771};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q92900};
GN ORFNames=2E4.130, NCU04242;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: RNA-dependent helicase required for nonsense-mediated decay
CC (NMD) of aberrant mRNAs containing premature stop codons and modulates
CC the expression level of normal mRNAs (By similarity). Also capable of
CC unwinding double-stranded DNA and translocating on single-stranded DNA
CC (By similarity). {ECO:0000250|UniProtKB:P30771}.
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:0000250|UniProtKB:P30771};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P30771};
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=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30771}.
CC Note=Associates with polysomes. {ECO:0000250|UniProtKB:P30771}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; AL451022; CAC18314.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA31997.1; -; Genomic_DNA.
DR RefSeq; XP_961233.1; XM_956140.2.
DR AlphaFoldDB; Q9HEH1; -.
DR SMR; Q9HEH1; -.
DR STRING; 5141.EFNCRP00000003901; -.
DR PRIDE; Q9HEH1; -.
DR EnsemblFungi; EAA31997; EAA31997; NCU04242.
DR GeneID; 3877396; -.
DR KEGG; ncr:NCU04242; -.
DR VEuPathDB; FungiDB:NCU04242; -.
DR HOGENOM; CLU_001666_4_0_1; -.
DR InParanoid; Q9HEH1; -.
DR OMA; HHDSIGY; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR CDD; cd21407; 1B_UPF1-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21400; ZBD_UPF1-like; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR040812; UPF1_1B_dom.
DR InterPro; IPR018999; UPF1_CH/ZBD.
DR PANTHER; PTHR10887; PTHR10887; 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; SSF52540; 1.
DR PROSITE; PS51997; UPF1_CH_RICH; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Metal-binding;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..1093
FT /note="Regulator of nonsense transcripts 1 homolog"
FT /id="PRO_0000080714"
FT DOMAIN 95..252
FT /note="Upf1 CH-rich"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 42..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..135
FT /note="C3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 117..145
FT /note="CC/SHH/C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 163..193
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 480..484
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 650
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 687
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 818
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
SQ SEQUENCE 1093 AA; 120088 MW; 8B0E4F0407ACE142 CRC64;
MANMEVSFTH LGNHLVSDSA AAIKAGGSDE LSNIDPDENL LYGVYGGRGP RGNGRRRHDD
DDNETEVLDD DDDESLASVP VDGMKSLKLD APVEEKELPP HACAYCGIHS PSSVVKCLTC
NKWFCSAKGS AFSSHIVNHL VRARHKEVQL HPESSLGDTV LECYNCGTKN VFILGFIPAK
SDTVVVLLCR QPCGASTSTK DMSWDISRWQ PLIEDRAFLN WLVTPPTDAE QLRARHLTPP
MIAKLEEMWK EAPNATVADL EKTAGVDDDP HPVLLKYDDP YHYQNIFGPL VKMESDYDKK
LKEAQSEDGL QVRWHLGLNS KHVASFILPK IESGDVKLAV GDEMRLKYKG ELRPPWEGVG
YVIKIPNNQS DEVEVELRKS ANDKSVPTEC THNFSADYVW KATSYDRMQL AMKTFAVDEM
SVSGYIFHKL LGHEVQVAPT KITMPKKFHV PGLPELNASQ IAAIKQVLSN PLSLIQGPPG
TGKTVTSATI IYHLAKMSNS QVLVCAPSNV AVDQLCERIH RTGLKVVRLT AKSREDVESS
VSFLALHEQV RMNTTNKELD GLVKLKTETG ELSSQDEKRF KQLTRQAERE ILQNADVVCC
TCVGAGDPRL SKMKFRNVLI DESTQSAEPE CMIPLVLGCK QVVLVGDHKQ LGPVIMNKKA
AKAGLNQSLF ERLVKLQFTP IRLKVQYRMH PCLSEFPSNM FYEGSLQNGV TAAERLRKDV
DFPWPVPETP MMFWSNLGNE EISASGTSYL NRTEAANVEK IVTRFFKAGV KPADIGVITP
YEGQRSYIVN TMQNTGTFKK ESYREVEVAS VDAFQGREKD FIVLSCVRSN ENQGIGFLSD
PRRLNVALTR AKYGLVIIGN PKVLCKHELW HHLLVHFKDK KCLVEGPLTN LQPSLLQFGR
PRQAYRPQRS HTQHVASGPS NGRFAAPLTA GSVRDYETGS MVSYIPDDVS SIHSSALGGA
ALSSGYPAMF SNFHPEAWAG LPCAGPNGRP GAKGRGRATE SIAGESVANS EFTDATSSVI
GGKGIGQGGA SLGAGLSEAI GSARPTSYSQ SDRLKQYVES NGRMGVGNGY RRYDDDEKSV
STAFASQIGT GFD
