ID G1LS11_AILME Unreviewed; 1647 AA.
AC G1LS11;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
GN Name=TUT4 {ECO:0000313|Ensembl:ENSAMEP00000009848.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000009848.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000009848.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000009848.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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};
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DR STRING; 9646.ENSAMEP00000009848; -.
DR Ensembl; ENSAMET00000010277.2; ENSAMEP00000009848.2; ENSAMEG00000009340.2.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000156988; -.
DR HOGENOM; CLU_003287_0_0_1; -.
DR InParanoid; G1LS11; -.
DR OrthoDB; 170176at2759; -.
DR TreeFam; TF315661; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 917..932
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1297..1312
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1361..1377
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..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1485
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 129..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1647 AA; 185431 MW; 8DF415FEEE325C5C CRC64;
MEDSKTSTNE NHEPKKNAWA LSEESKAVKV ISNQTLKARN DKSIKEIGTS SPNKNSSKKN
KQNDICIEKT EVKSCKVNAA NIASPKDLGL VLRDQSHCKT KKSPNSPVKA EKVPVSQAKA
EKLPKSPNSP AKTEKTPKSL SSQRKMEKVP SSQMKSEKVP GSPAEPEKAP SLVLKENIRR
TEFQQIGKKI PSSFTSLDKV NMDVEGGKSA SETAPQSQKQ QACTDNTGDS DDSASGIEDI
SDDLSKMKND DSNKENSSEM EYLENATVID ESALTPEQRL GLKQAEERLE RDHIFRLEKR
SPEYTNCRYL CKLCLIHIEN IQGAHKHIKE KRHKKNILEK QEESELRSLP PPTAAHLAAL
SVAVIELAKE HGITDDDLRV RQEIVEEMSE VITTFLPECS LRLYGSSLTK FALKNSDVNI
DIKFPPRMNH PDLLIQVLGI LKKSVLYIDV ESDFHAKVPV VVCKDRKSGL LCRVSAGNDM
ACLTTDLLAA LGKLEPVFTP LVLAFRYWAK LCYIDSQTDG GIPSYCFALM VMFFLQQRKP
PLLPCLLGSW IEGFDPKRMD DFQLKGIVEE KFVKWEYNSS SATEKNSIAE ENKAKADQPK
DDTKKTETDN QSNAMKEKHG KSPLTLGTPN QVSLGQLWLE LLKFYTLDFA LEEYVICVRM
QDILTRENKN WPKRRIAIED PFSVKRNVAR SLNSQLVYEY VVERFRAAYR YFACPQRKGG
NKSTVNSMKK EKGKVSNKKP VKSDNMASSC TLLGESTEKI NAERGQPDKY DEMECTSQRC
ITEDDSLLVN ELDLAELGQE SCLSTGEGSE LEPKSNKKQD DLAPSETYLK KELSQCNCID
YKSPDPDESV GTDCRSNIET ESSHQNVSTD 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 PKRRSSLLFR
LKKKDSEEEK DGNEEEKDSR DLVDARDLHD TREFRDPRDL RCFICGDAGH VRRECPEVKL
ARQRNSSVAA AQLVRSLVNA QQVAGSGQQQ SDQSVRTRQS SECSDSPSYS PQPQPFPQNS
SQSAAITQSP SQPGSQPKLG PPQQGAQPPH QVQMPMYNFP QSPPAQYSPM HNMGLLPMHP
LQIPAPSWPI HGPVIHSAPG SAPSNIGLND PSIIFAQPAA RPVAIPNSSH DGHWPRTVAP
NSLVNNGTVG NSEPGFPGLN PPIPWEHAPR PHFPLVPASW PYGLHQNFMH QGNARFQPNK
PFYTQDRCAT RRCRERCPHP PRGNVSE
//