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Database: UniProt
Entry: H3ARE1_LATCH
LinkDB: H3ARE1_LATCH
Original site: H3ARE1_LATCH 
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};
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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
//
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