ID A0A2K6BTP0_MACNE Unreviewed; 1505 AA.
AC A0A2K6BTP0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
GN Name=TUT7 {ECO:0000313|Ensembl:ENSMNEP00000014779.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000014779.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000014779.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide;
CC Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173116; EC=2.7.7.52;
CC Evidence={ECO:0000256|ARBA:ARBA00024498};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSMNET00000038984.1; ENSMNEP00000014779.1; ENSMNEG00000031427.1.
DR GeneTree; ENSGT00940000156859; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000031427; Expressed in bone marrow and 12 other cell types or tissues.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProt.
DR GO; GO:0061157; P:mRNA destabilization; IEA:UniProt.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR CDD; cd05402; NT_PAP_TUTase; 2.
DR Gene3D; 1.10.1410.10; -; 2.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF34; TERMINAL URIDYLYLTRANSFERASE 7; 1.
DR Pfam; PF03828; PAP_assoc; 2.
DR Pfam; PF19088; TUTase; 2.
DR Pfam; PF16631; TUTF7_u4; 1.
DR Pfam; PF00098; zf-CCHC; 3.
DR SMART; SM00343; ZnF_C2HC; 3.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 2.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 3.
DR PROSITE; PS50158; ZF_CCHC; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 975..990
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1357..1371
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1462..1478
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..870
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1505 AA; 172272 MW; 5FAAD43FB6AFF247 CRC64;
MPSFRCKVRK LKSKTMGDTA KPYFAKRTKD RGTMDDDDFR RGHPQQDYLI IDDHAKSHGS
KMEKGLQKKK ITPGNYGNTP RKGPCAVSSN PYAFKNPIYS QPAWMNDNHK DQSKRWLSDE
HTGNSDNWRE FKPGPRIPVI NRQRKDSFQE NEDGYRWQDT RGCRTVRRLF HKDLTSLETT
SEMEAGSPEN KKQRSRPRKP RKTRNEENEQ DGDLEGPVID ESVLSAKELL GLQQAEERLK
RDCVDRLKRR PRNYPAAKYT CRLCDVLIES IAFAHKHIKE KRHKKNIKEK QEEELLTTLP
PPTPSQINAV GIAIDKVVQE FGLHNENLEQ RLEIKRIMEN VFQHKLPDCS LRLYGSSCSR
LGFKNSDVNI DIQFPAIMSQ PDVLLLVQDC LKNSDSFIDV DADFHARVPV VVCREKQSGL
LCKVSAGNEN ACLTTKHLTA LGKLEPKLVP LVIAFRYWAK LCSIDRPEEG GLPPYVFALM
AIFFLQQRKE PLLPVYLGSW IEGFSLSKLG NFNLKDIETD VVIWEYTDSA AGDTDTAKEE
APREKPIKRG QVSLILDMKH QPSVPVGQLW VELLRFYALE FNVADLVISI RVKELVSREL
KDWPKKRIAI EDPYSVKRNV ARTLNSQPVF EYILHCLRTT YKYFALPHKI TKSSLPKPLN
AVTCVSEVIN HDPDVQTKDD KLKNSVLAQG PGATGSAANT CKVQPLTLKE TAGSFGSPPT
EEMGNEHIRV PPENSDCIRA DVNDDDYKDD KVHHQETGRK NEKEKVGRKG KHLLAIDQKR
GEHVVCGSTR NNESEISLDL EGFQNPTAKE CEGLATLDNK ADLDGEIIEG TEELEGSLNH
YTHSVQGQIS EMIPSDEEEE EDEEEEEEEE PRLTLNQRED EDGMANEDEL DNTYTGSGDE
DALSEEDDEL GDPAKYEEVK ECGKHVEGAL LVELNKISLK EENVCEENSP VDQSDFFYEF
SKLIFTKGKS PTVVCSLCKR EGHLKKDCPE DFKRIQLEPL PPLTPKFLNI LDQVCIQCYK
DFSPTIIEEQ AREHIRQNLE SFIRQDFPGT KLSLFGSSKN GFGFKQSDLD VCMTINGLET
AEGLDCVRTI EELARVLRKH SGLRNILPIT TAKVPIVKFF HLRSGLEVDI SLYNTLALHN
TRLLSAYSAI DPRVKYLCYT MKVFTKMCDI GDASRGSLSS YAYTLMVLYF LQQRNPPVIP
VLQEIYKGEK KPEIFVDGWN IYFFDQIDEL PAYWPECGKN TESVGQLWLG LLRFYTEEFD
FKEHVISIRR KSLLTTFKKQ WTSKYIVIED PFDLNHNLGA GLSRKMTNFI MKAFINGRRV
FGIPVKGFPK DYPSKMEYFF DPDVLTEGEL APNDRCCRIC GKIGHFMKDC PMRRKVRRRR
DQEDALNQRY PENKEKRSKE DKEIHNKYTE REVSTKEDKP IQCTPQKAKP VRAAADLGRE
KILRPPVEKW KRQDDKDLRE KRCFICGREG HIKKECPQFK GSSGSLSSKY MTQGKASAKR
TQQES
//
