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Database: UniProt
Entry: G1LS11_AILME
LinkDB: G1LS11_AILME
Original site: G1LS11_AILME 
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
//
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