ID H3AT32_LATCH Unreviewed; 783 AA.
AC H3AT32;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Speckle targeted PIP5K1A-regulated poly(A) polymerase {ECO:0000256|ARBA:ARBA00021679};
DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
DE AltName: Full=RNA-binding motif protein 21 {ECO:0000256|ARBA:ARBA00030790};
DE AltName: Full=U6 snRNA-specific terminal uridylyltransferase 1 {ECO:0000256|ARBA:ARBA00033036};
GN Name=TUT1 {ECO:0000313|Ensembl:ENSLACP00000012803.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000012803.1, 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:ENSLACP00000012803.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000256|ARBA:ARBA00024620};
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: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
CC Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000256|ARBA:ARBA00008593}.
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; AFYH01108637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006000217.1; XM_006000155.2.
DR AlphaFoldDB; H3AT32; -.
DR Ensembl; ENSLACT00000012897.1; ENSLACP00000012803.1; ENSLACG00000011278.1.
DR GeneID; 102348918; -.
DR KEGG; lcm:102348918; -.
DR CTD; 64852; -.
DR GeneTree; ENSGT00940000159914; -.
DR HOGENOM; CLU_018757_1_0_1; -.
DR OrthoDB; 170176at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000011278; Expressed in pelvic fin and 6 other cell types or tissues.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd05402; NT_PAP_TUTase; 1.
DR CDD; cd12279; RRM_TUT1; 1.
DR Gene3D; 1.10.1410.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034388; Star-PAP_RRM.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF127; SPECKLE TARGETED PIP5K1A-REGULATED POLY(A) POLYMERASE; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 55..137
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 125..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 88782 MW; 148D9D49E7C1635B CRC64;
MELSADVEAL LRGGFHCRLC DINVPNQPSL EDHIKGKKHQ KLLSVRTNRK SQEERSVFVS
GFKRGTSDLE ITGHFQRYGS VSSVIMDKNK GVYAIVELDN IETLQKVLSE TQHCMNGQRL
QVKPREKKEF KYTPKKKQSS HRNQVLSQEE LSEALCQANH VDEQMSQLMQ LFELSDSERK
VRELLVTLLQ EVFSEFFPGC KVLPFGSSVN CFDTHACDLD LFLDLENTKT FQAKAKADAE
EVVEGNGEDA QSEDSILSDI DLETASAVEV LELVATVLQK CVPGVHKVQA VTTARLPVVK
FVHKETGLQG DVSINNRLAV RNTKFLQLCA SMDERVRPLT YAVRYWAKQK QLAGNPFGGG
PLLNNYALTL LVIFYLQNRT PPILPTVSKL KAITEDQEQC VIDGYDCSFP SDNSKVEPGE
NSENLCSLLA EFYNFYTEFD FAGTVISLRE GRDLPVTEFV DPELNRKLRL GPINIQDPFE
LDHNVAGNIN DKTGQKFKKE CSDASKYCRS LQYQRKSNKG KVWGLVRLFH THSSAESSPS
TSQRQAGTQD RMVIIIPFKL SALSDDTKKS LHGSSDFREI WFEKVCCALL YVMEEVLQCS
CSSTEENGTC VSSDHVNINE NSEDLVVLSD DNPQPGSKRL FEEEMLKASP SKKPKLENLK
FRDSVMWYIT VWHKVWMGRR KVRRQLRHNT GTQNEADCST EVSCFDLETK VTKAILEQER
EADATKPLIT LTMSAKVLGR NKDTSTCLQF TPVQDDQFLF HDFFHFLESF VPKMIKKHIE
KLD
//
