ID A0A2K5J7K1_COLAP Unreviewed; 1490 AA.
AC A0A2K5J7K1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000024878.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000024878.1}
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 RefSeq; XP_011801269.1; XM_011945879.1.
DR RefSeq; XP_011801270.1; XM_011945880.1.
DR STRING; 336983.ENSCANP00000024878; -.
DR Ensembl; ENSCANT00000047876.1; ENSCANP00000024878.1; ENSCANG00000035790.1.
DR GeneID; 105514492; -.
DR CTD; 79670; -.
DR OMA; CSDIDIC; -.
DR OrthoDB; 170176at2759; -.
DR Proteomes; UP000233080; Unplaced.
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:UP000233080};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 960..975
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1342..1356
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1447..1463
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..855
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1490 AA; 170430 MW; AF2D83F2EBC35D5B CRC64;
MGDTAKPYFA KRTKDRGTMD DDDFRRGHPQ QDYLIIDDHA KGHGSKMEKG LQKKKITPGN
YGNTPRKGPC AVSSNPYAFK NPIYSQPAWM NDNHKDQSKR WLSDEHTGNS DNWREFKPGP
RIPVINRQRK DSFQENEDGY RWQDTRGCRT VRRLFHKDLT SLETTSEMEA GSPENKKQRS
RPRKPRKTRN EENEQDGDLE GPVIDESVLS TKELLGLQQA EERLKRDCID RLKRRPRNYP
AAKYTCRLCD VLIESIAFAH KHIKEKRHKK NIKEKQEEEL LTTLPPPTPS QINAVGIAID
KVVQEFGLHN ENLEQRLEIK RIMENVFQHK LPDCSLRLYG SSCSRLGFKN SDVNIDIQFP
AIMSQPDVLL LVQDCLKNSD SFIDVDADFH ARVPVVVCRE KQSGLLCKVS AGNENACLTT
KHLTALGKLE PKLVPLVIAF RYWAKLCSID RPEEGGLPPY VFALMAIFFL QQRKEPLLPV
YLGSWIEGFS LSKLGNFNLK DIETDVVIWE YTDSAAGVTD TAKEEASRET PIKRGQVSLI
LDMKHQPSVP VGQLWVELLR FYALEFNVAD LVISIRVKEL VSRELKDWPK KRIAIEDPYS
VKRNVARTLN SQPVFEYVLH CLRTTYKYFA LPHKVTKSSL PQPLNAVTCV SEVINHDPDV
QTKDDKLKNS VLAQGPGATS SAANTCKVQL LTLKETAESF GSPPTEEMGN EHIRVHPENS
DCIRADVNCD DYKDDKVHHQ ETGRKNEKEK VGRKGKHLLA VDQKRGEHVV CGSTHHNESE
ISLDLEGFQN PTAKECEGLA TLDNKADLDG EIVEGTEELE GSLNHFTHSV QGQISEMIPS
DEEEEEDEEE EEEEEPRLTI NPREDEDGMA NEDELDNAYT GSGDEDALSE EDDELGDPAK
YEDVKECGKH VEGALLVELN KISLKEENVC EENSPVDQSD FFYEFSKLIF TKGKSPTVVC
SLCKREGHLK KDCPEDFKRI QLEPLPPLTP KFLNILDQVC IQCYKDFSPT IIEEQAREHI
RQNLESFIRQ DFPGTKLSLF GSSKNGFGFK QSDLDVCMTI NGLETAEGLD CVRTIEELAR
VLRKHSGLRN ILPITTAKVP IVKFFHLRSG LEVDISLYNT LALHNTRLLS AYSAIDPRVK
YLCYTMKVFT KMCDIGDASR GSLSSYAYTL MVLYFLQQRN PPVIPVLQEI YKGEKKPEIF
VDGWNIYFFD QIDELPAYWP ECGKNTESVG QLWLGLLRFY TEEFDFKEHV ISIRRKSLLT
TFKKQWTSKY IVIEDPFDLN HNLGAGLSRK MTNFIMKAFI NGRRVFGIPV KGFPKDYPSK
MEYFFDPDVL TEGELAPNDR CCRICGKIGH FMKDCPMRRK VRRRRDQEDA LNQRYPENKE
KRSKEDKEIH NKYTEREVST KDDKPIQCTP QKAKPVRAAA DLGREKILRP PVEKWKRQDD
KDLREKRCFI CGREGHIKKE CPQFKGSSGS LSSKYMTQGK ASAKRTQQES
//
