ID L5KQF2_PTEAL Unreviewed; 871 AA.
AC L5KQF2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 ORFNames=PAL_GLEAN10011483 {ECO:0000313|EMBL:ELK13450.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13450.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB030625; ELK13450.1; -; Genomic_DNA.
DR RefSeq; XP_006911274.1; XM_006911212.2.
DR AlphaFoldDB; L5KQF2; -.
DR STRING; 9402.L5KQF2; -.
DR GeneID; 102892587; -.
DR KEGG; pale:102892587; -.
DR CTD; 64852; -.
DR eggNOG; KOG2277; Eukaryota.
DR InParanoid; L5KQF2; -.
DR OrthoDB; 170176at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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: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 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 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 ECO:0000313|EMBL:ELK13450.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELK13450.1};
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 226..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 93705 MW; 14E90783160A1478 CRC64;
MAAVDSDVES LPRGGFRCRL CHITTANRPS LDAHLGGRKH RHLVELRAAR KAQGLRSVFV
SGFPQNVDST ELSEYFQAFG PVASVVMDKD KGVFAIVEMG DVGAQEAVLS QPQHSLGGRR
LRVRPREQKE FQSPVSKSPK GVAPDSHQLA AALAEVPDVG AQMVKLVGLR ELSEAERQLR
SLVVALMQEV FTEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLEEPQ PAPKAPESPS
LDSALASPLD PQALARTSAS PPDSQPPASP RDLEALDFET PSSSLAPQTP DSALASDTLA
SPQSLPPASP LQEDQGDGDL GKALELAEAL KGEKTEQGAM LELVGSILRG CVPGVYRVQT
VPSARRPVVK FCHRPSGLHG DVSLSNRLAL HNSRFLSLCS ELDGRVRPLV YTVRCWAQGR
GLSGSGPLLN NYALTLLVIY FLQTREPPVL PTVSQLTQKA GEGEQVEVDG WDCSFPRDAS
RLEPSTNKES LSSLLAQFFS CVSCWDLRGS LLSLREGQAL PVAGGLPSNL WEGLRLGPMN
LQDPFDLSHN VAANVTSRVA GRLQNCCRAA ANYCRSLQYQ HRSSRGRDWG LLPLLQPSSP
SSLLSATPIP LPPAPFTQLT AALVQVLREA LGCHIEQGTK RLRSEGGGMG NSPQGGSSKR
LKLDAQKASS EEGKEEQQAC AGDHSEDGVE EMVIEVGETM QDWAMQSPGQ PGEPPLTTGK
PLATGEEQSG PAALTEQGPK GPEAAREGPQ GETGKGASLS VSWRCALWHR VWQGRRRARR
RLQQQTKEGG GGSAARGVEW LATEARVTQE LRGLSSAEQR PETEPLLTFV ASASQADQSL
TVTPLQDSQS LFPDLYHFLQ VFLPQALRNL K
//
