UniProt: A0A1S3G6E9

Database: UniProt
Entry: A0A1S3G6E9_DIPOR

LinkDB:  A0A1S3G6E9_DIPOR 
Original site:  A0A1S3G6E9_DIPOR

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Ontology (8)   
   GO (8)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (15)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (1)   
   SMART (2)   
All databases (28)   

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ID   A0A1S3G6E9_DIPOR        Unreviewed;       862 AA.
AC   A0A1S3G6E9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
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|RefSeq:XP_012884398.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012884398.1};
RN   [1] {ECO:0000313|RefSeq:XP_012884398.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012884398.1};
RG   RefSeq;
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}.
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DR   RefSeq; XP_012884398.1; XM_013028944.1.
DR   AlphaFoldDB; A0A1S3G6E9; -.
DR   STRING; 10020.ENSDORP00000003752; -.
DR   GeneID; 105995245; -.
DR   KEGG; dord:105995245; -.
DR   CTD; 64852; -.
DR   InParanoid; A0A1S3G6E9; -.
DR   OrthoDB; 170176at2759; -.
DR   Proteomes; UP000081671; Unplaced.
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   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; 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   SMART; SM00451; ZnF_U1; 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   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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
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          56..138
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          124..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..685
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   862 AA;  94049 MW;  7E39FA1FAEE2A855 CRC64;
     MAAVGSDVEA LPRGGFRCSL CQVTTANRPS LDAHLGGRKH RHLVELRAAR KAQGLRSVFV
     SGFPRDVDSA QLSEYFQTFG PVASVVMDKD KGVFAIVEMG DVSAREAVLS QPQHSLGKHR
     LRVRPREQKE FQSPAAKSPK GVSPDSHQLA KALAEAPDVE AQMVQLVGLR ELSEAERQLR
     NLVVALMQEV FTEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDMEEPQ LASKAPESPS
     LDSALASPLD PQTLACTPAS PLDSQPPASP QDSEALDLEI PSSSLAPQTP DSALASETVA
     SPQSLPPASP IQEDRGEGDL GNAQEQAEAL KEKPEGAAML ELVGSILRGC VPGVYRVQTV
     PSARRPVVKF CHRPSGLHGD ISLSNRLALH NSRFLSLCCE LDRRVRPLVY TIRCWAQGRG
     LSGSGPLLNN YTLTLLVIYF LQTRDPPVLP AVAQLTQKAG EGEQVEVDGW DCSFPRDASR
     LEPSMNVEPL SSLLAQFFSC VSSWDLRDSL LSLREGQALP VAEVPSNLWE GLRLGPMNLQ
     DPFDLSHNVA ANVTSRVAGR LQNCCRAAAN YCRSLQYQQR SSRGRDWGLL PLLQPSSPSS
     LLSATPIPFP PAPFPQLTDV LVRVLREALG CHIEQGTKRP RSEGGRTESP QGGTSKRLKL
     DGQRKNSEEG KEEQQGYEED HGEDRVEEMV IEAGEVPQDW AMRSPGQSGE LPIMTTNCLD
     TLTEQRPMAP EMAGDGSQGE PGKGASYPTL VSWRCALWHR VWQGRRRARR RLQQQSKTGD
     GNKAISGAEW LAMEAQVTQE LRETNAAEQT PDTEPLLTFV ASASQAEQTL TVTPLQDSQG
     LFPDLHHFLQ VFLPQALRNL LK
//

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