ID A0A2Y9IWZ3_ENHLU Unreviewed; 1659 AA.
AC A0A2Y9IWZ3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
GN Name=LOC111142844 {ECO:0000313|RefSeq:XP_022351884.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022351884.1};
RN [1] {ECO:0000313|RefSeq:XP_022351884.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022351884.1};
RG RefSeq;
RL Submitted (NOV-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_022351884.1; XM_022496176.1.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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 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; IPR002934; Polymerase_NTP_transf_dom.
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:SF49; TERMINAL URIDYLYLTRANSFERASE 4; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 2.
DR Pfam; PF19088; TUTase; 1.
DR Pfam; PF00098; zf-CCHC; 2.
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; 2.
DR PROSITE; PS50158; ZF_CCHC; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nucleotidyltransferase {ECO:0000313|RefSeq:XP_022351884.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 927..942
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1307..1322
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1366..1382
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1409..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1659 AA; 186679 MW; AA8A83E5E5493A04 CRC64;
MEDFKTSKNE NHEPKKNAWA LSEESKAVKV ISNQTLKARN DKSIKEIGTS SPNKNSSKKN
KQNDICIEKT EVKSCKVNAA NIASPKDLGL VLRDQSHCKT KKSPNSPVKV EKVPVSQAKA
EKSPKSPNSP VKTEKTPSSQ VTATEKALSS QRKMEKVPSS QMKLEKVPGS PAEPEKAPSL
LLKENMRRTE LQQIGKKIPS SLTSLDKVNI DVDGGKSALE NSPGSQKQQA CTDNTGDSDD
SASGIEDISD DLSKMKNDDS NKENSSEMDY LENATVIDES ALTPEQRLGL KQAEERLERD
HIFRLEKRSP EYTNCRYLCK LCLIHIENIQ GAHKHIKEKR HKKNILEKQE ESELRSLPPP
TPGHLAALSV AVIELAKEHG ITDDDLRVRQ EIVEEMSKII TTFLPECSLR LYGSSLTKFA
LKNSDVNIDI KFPPKMNHPD LLIQVLGILK KSVLYIDVES DFHAKVPVVV CKDRKSGLLC
RVSAGNDMAC LTTDLLAALG KLEPVFTPLV LAFRYWAKLC YIDSQTDGGI PSYCFALMVM
FFLQQRKPPL LPCLLGTWIE GFDPKRMDDF QLKGIVEEKF VKWEYNSSSA TEKNSIAEEN
KAKADQPKDD TKKTDTDNQS NAMKEKHGKS PLTLGTPNQV SLGQLWLELL KFYTLDFALE
EYVICVRIQD ILTRENKNWP KRRIAIEDPF SVKRNVARSL NSQLVYEYVV ERFRAAYRYF
ACPQRKGGNK STVDSMKKEK VKISNKKPVK SDNMASSCCI LLGESTEKIN AERGQPDKYD
EMECTSQRCI TEDNSLLVNE LDLAELGQES SRLSTSEGSE LEPKSNKKQD DLAPSETCLK
KELSQCNCID YKSPDPDDSV GTDCRSNTET ESSHLIVSTD TSATSCNCKA TEDASDLNDD
DNHPTQELYY VFDKFILTSG KPPTIVCSIC KKDGHSKNDC PEDFRKIDLK PLPPMTNRFR
EILDLVCKRC FDELSPPFSE QHNREQILIG LEKFIQKEYD EKARLCLFGS SKNGFGFRDS
DLDICMTLEG HENAEKLNCK EIIENLAKIL KRHPGLRNIL PITTAKVPIV KFEHRRSGLE
GDISLYNTLA QHNTRMLATY AAIDPRVQYL GYTMKVFAKR CDIGDASRGS LSSYAYILMV
LYFLQQRKPP VIPVLQEIFD GKQIPQRMVD GWNAFFFDKT EELKKRLPSL GKNTETLGEL
WLGLLRFYTE EFDFKEYVIS IRQKKLLTTF EKQWTSKCIA IEDPFDLNHN LGAGVSRKMT
NFIMKAFING RKLFGTPFYP LIGREAEYFF DSRVLTDGEL APNDRCCRVC GKIGHYMKDC
PKRRRLKKKD SEEEKDGNEE EKDSRDLVDP RDLHDTREFR DPRDLRCFIC GDAGHVRREC
PEVKLARQRN SSVAAAQLVR NLVNAQQVAG SAQQQGDQSI RTRQSSECSD SPSYSPQPQP
FPQNSSQSAA ITQSPSQPGS QPKLGPPQQG AQPPHQVQMP MYNFPQSPPA QYSPMHNMGL
LPMHPLQIPA PSWPIHGPVI HSAPGSAPSN IGLNDPSIIF AQPAARPVAI PNSSHDGHWP
RTVAPNSLVN NGTVGNSEPG FPGLNPPIPW EHAPRPHFPL VPASWPYGLH QNFMHQGNAR
FQPNKPFYTQ AGLPMHSNQP ILLSQGYPYL NVSYIQQKK
//
