ID   A0A0A8K9B1_HUMAN        Unreviewed;       874 AA.
AC   A0A0A8K9B1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=URLC6 {ECO:0000313|EMBL:BAQ19752.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAQ19752.1};
RN   [1] {ECO:0000313|EMBL:BAQ19752.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Daigo Y., Nakamura Y.;
RT   "Isolation and characterization of novel human genes, which are up-
RT   regulated in lung cancer.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AB101208; BAQ19752.1; -; mRNA.
DR   RefSeq; NP_073741.2; NM_022830.2.
DR   AlphaFoldDB; A0A0A8K9B1; -.
DR   SMR; A0A0A8K9B1; -.
DR   Antibodypedia; 28452; 96 antibodies from 17 providers.
DR   DNASU; 64852; -.
DR   GeneID; 64852; -.
DR   KEGG; hsa:64852; -.
DR   CTD; 64852; -.
DR   VEuPathDB; HostDB:ENSG00000149016; -.
DR   HOGENOM; CLU_018757_1_0_1; -.
DR   OrthoDB; 170176at2759; -.
DR   PhylomeDB; A0A0A8K9B1; -.
DR   ChiTaRS; TUT1; human.
DR   ExpressionAtlas; A0A0A8K9B1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
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   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; IPR036236; Znf_C2H2_sf.
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; PF00076; RRM_1; 1.
DR   Pfam; PF12874; zf-met; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 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.
PE   2: Evidence at transcript level;
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          56..128
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          113..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   874 AA;  93847 MW;  85A4117A040FC90D CRC64;
     MAAVDSDVES LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRAAR KAQGLRSVFV
     SGFPRDVDSA QLSEYFLAFG PVASVVMDKD KGVFAIVEMG DVGAREAVLS QSQHSLGGHR
     LRVRPREQKE FQSPASKSPK GAAPDSHQLA KALAEAADVG AQMIKLVGLR ELSEAERQLR
     SLVVALMQEV FTEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLEEPQ PVPKAPESPS
     LDSALASPLD PQALACTPAS PPDSQPPASP QDSEALDFET PSSSLAPQTP DSALASETLA
     SPQSLPPASP LLEDREEGDL GKASELAETP KEEKAEGAAM LELVGSILRG CVPGVYRVQT
     VPSARRPVVK FCHRPSGLHG DVSLSNRLAL HNSRFLSLCS ELDGRVRPLV YTLRCWAQGR
     GLSGSGPLLS NYALTLLVIY FLQTRDPPVL PTVSQLTQKA GEGEQVEVDG WDCSFPRDAS
     RLEPSINVEP LSSLLAQFFS CVSCWDLRGS LLSLREGQAL PVAGGLPSNL WEGLRLGPLN
     LQDPFDLSHN VAANVTSRVA GRLQNCCRAA ANYCRSLQYQ RRSSRGRDWG LLPLLQPSSP
     SSLLSATPIP LPLAPFTQLT AALVQVFREA LGCHIEQATK RTRSEGGGTG ESSQGGTSKR
     LKVDGQKNCC EEGKEEQQGC AGDGGEDRVE EMVIEVGEMV QDWAMQSPGQ PGDLPLTTGK
     HGAPGEEGQP SHAALAERGP KGHEAAQEWS QGEAGKGASL PSSASWRCAL WHRVWQGRRR
     ARRRLQQQTK EGAGGGAGTR AGWLATEAQV TQELKGLSGG EERPETEPLL SFVASVSPAD
     RMLTVTPLQD PQGLFPDLHH FLQVFLPQAI RHLK
//