ID H3ARE1_LATCH Unreviewed; 1706 AA.
AC H3ARE1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
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:ENSLACP00000012212.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000012212.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000012212.1}
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFYH01167493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01167494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01167495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01167496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01167497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01167498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01167499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01167500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01167501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01167502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000012212; -.
DR Ensembl; ENSLACT00000012304.1; ENSLACP00000012212.1; ENSLACG00000010748.1.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000156988; -.
DR HOGENOM; CLU_003287_0_0_1; -.
DR InParanoid; H3ARE1; -.
DR OMA; HCKAKKL; -.
DR TreeFam; TF315661; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000010748; Expressed in post-anal tail muscle and 4 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 1340..1355
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1392..1408
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1706 AA; 192069 MW; 3A200A703C2B03CB CRC64;
MEDPSSSKSE NHDIRKPSRL GHGEGKSIRI IVNNDIYKHR NEGPLREGGR GTLNWNNKKG
KQNDAGTEKS EGKLCKTVQQ NCSTRCTDLG VNPQNQGHGK ANRSVNGGVL TEKTRVKQVR
VQQPSGKSPN PDAAGNGTSE ECIAVKQKGD RTAESVVEIR KSQVPESKNS ECGKPEEGSD
LEEEFDYLGG HYWRVCVCVL IKFVSLFVLN TEIPGIMGSS PSLGVLQKQS RHCLGNSGKK
HENSQNGISV TSDEAYKDKG SDVLLKEDSC TMNENSDSRL VIDESSLTAE HQLGLKQAEE
RLQRDYICRL EKRSPEYSNC QYLCKLCLVH IENIQGAHKH IKEKRHKKNI MEKQEENDLR
ALPPPSPSQL SALSAAIIKA TRTHGISEED FRVRQKIVLE METIILQHLP GCTLRMYGSC
LTRFAFKTSD INIDVKFPPN LSQPDVLIQV LDILKNSSSY SDVESDFHAK VPIVSCRDKK
SDLICKVSAG NDMACLTTNL LAALGKQEPR LTPLVLAFRY WAKLCHVDCQ AEGGIPSYSF
PIMVIFFLQQ RKEPILPVFL GTWVEGFDLK RIDDYHLKGV EKDKFIHWEY RPSNSGEGRH
VNGGEGKTKA EQRKSGNKKT ESSETDGQSS SVKQKQDKSW LKFEAPPKAS LGQLWLELLK
FYTLEFALEE HVISIRVKEL LIRENKNWPK RRIAIEADPF ALKRNVARSL NSQMVFEYIL
ERFRVAYKYF ACPQSKDETK SKLDTKKKEK TKTGSKKPIK SGETVTNCCL PQWDRSIEQP
TSENGSRTDN LEAVDYSKTH CTSVGCTSNG IGGLLNRNNG IDTLCNAERC KGDTSNTGTR
CLHCKTAGKA HEATEPLHSS ENLLREAEVG HTCNGDDNLK SCCLKTCSVL EEKKDGCSGG
IPCSQKAKCT GVCTTSTSHS CKAVVETHTV KKEERTSAQE MCYVFDKFIL TSGKPPTIVC
SICKRDGHSK NDCPEDFKKI DLKPLPPMTD RFREILDKVC KKCYNERSPP PSEQQNREHI
LASLERFIRK EYNDKARLCL FGSSKNGFGF RNSDLDICMT LEGHETAEKL NSKEIIEGLA
KVLKKHPGLR DILPITTAKV PIVKFKHRDS DLEGDISLYN TLAQHNTRML ATYAAIDPRV
QYLGYTMKVF AKCCDIGDAS RGSLSSYAYI LMVLYFLQQR EPPVIPVLQE IFDGTDIPQR
MVDGWNAFFF DEINELKKRL PELGKNTESV GELWLGLLRF YTEEFDFKEY VISIRQKKLL
TTFEKQWTSK CIAIEDPFDL NHNLGAGVSR KMTNFIMKAF INGRKLFGTP VYPQPGTERD
YFFDSKVLTD GELAPNDRCC RICGKIGHYM KDCPKRRRIL SFQGKLWTKK KENEKEDEKE
AKEEEREPRE KRCFICGDTG HVRRDCPEYR QARQRNNSVS SVAVPVPQMV RSLGSAQPIS
VSQPASSPHQ GQDQPVCTRQ PSESSESHQT PPYSPQPQPQ QFTQNSSQST PTNSSPSQQS
TCQTRHVQQQ QVPQAPPQVQ LPLFNFPQPS PNQYPSLRNM GLLQTHQLQI SNNSWPIHGP
VVHSAPINNQ STLGLNDPSI IFAQPAARPM GIPNTSHERF WHGHMTPNSV VGNGSMGNSD
QGFQGQFTKL NPTSVTWEHP QAAHFPLLQA LWPYNMPQNY LQQGSAGYQQ NKSFYPQGPL
MQNNQRFPLL SQGHPPMNIN YIQQKK
//