ID A0A498MUX3_LABRO Unreviewed; 1296 AA.
AC A0A498MUX3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=ROHU_021284 {ECO:0000313|EMBL:RXN25789.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN25789.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN25789.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN25789.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN25789.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN25789.1}.
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DR EMBL; QBIY01012279; RXN25789.1; -; Genomic_DNA.
DR STRING; 84645.A0A498MUX3; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 2.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR NCBIfam; TIGR00592; pol2; 2.
DR PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 2.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 2.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF90234; Zinc finger domain of DNA polymerase-alpha; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 43..104
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 334..631
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 696..851
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 865..1105
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1145..1177
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT DOMAIN 1178..1288
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1296 AA; 146850 MW; B6691E4B07A9C1EF CRC64;
MAPVSNSDKD IDGGDCDTSD TCGIATSRSR REKKEKVGRK SALEQLKRAK KGEKVKYEVE
EFTSVYEEVD EEQYSKMVRE RQDDDWIIDD DGTGYVEDGR EIFDEDLDDD ALEKNPKSKQ
GGKGGDSKKN VKKVSVSKPN SIKSMFMNSN VKKPAEKHVD LSQDDLLGDI LQDLHSEVNV
CDLLYQINSC LFLTQKPVLL TPPPIITLKK KKTLGSPMNP FSVKPQVPKE SPEVQMSKPR
PVVTRVPPAE PSPRSSAHVQ PSKPAPTQIK KPKIEEPEGV VYLFGKVWIE SAEAHVSCCV
AVKNIERTMY LLPREHKVNL ATGEQTDSPV GMMDVYQEFN SLSEKFKIMK FKSKPVTKNY
AFEIPDIPSQ CEYLEVKYSA ELPSLPSELK GSTFSHVFGT NTSSLEHFLL NRKIRGPCWL
DVKTPQLSNQ PISWSKVEAV AQKTDFISVV KDLPPPPLVV MSISLKTVQN PKTHQNEIVS
LAALIHHKFH LDKAPPRPPF QTHFCVVSKP NDCIFPYDFK DAVRKKNGIV EIAGTERALL
GFFLAKMHKI DPDVLVGHDI FGFDLEVLLQ RINVCKVPHW SKIGRLRRAN MPKLGGRSGF
AEKSATCGRL VCDVEISAKE LIRCKSYHLT ELAAQILKTE RVVVPPENIR NFYGDSPHLL
YFLELTWMDA KLILQIMCEL NVLPLALQIT NIAGNVMSRT LMGGRSERNE FLLLHAFHEK
NFIVPDKQFF KKPQQDQGED EDIESGKGKS TKTRKKAAYA GGLVLDPKVG FYDKFILLLD
FNSLYPSIIQ EFNICFTTVE RGATNAQKKS EEDDDEIPEL PDPSLEMGIL PKEIRKLVER
RRQVKQLMKQ ADLNPDLCLQ ILMHTKEMVQ RMNLEVIYGD TDSIMINTNS TNLEEVFKLG
NKVKSEVNKL YKLLEIDIDG VFKSLLLLKK KKYAALMVEP QGDGKYTTKQ ELKGLDIVRR
DWCDLAKECG NYVIGQILSD QNRDTIVENI QKHLIEVGEK VANGSIPLNM FEIHKSLTKD
PQDYPDKKSL PHVHVALWIN SQGGKKVKAG DTVSYVICQD GSNLAASQRA YALEQLQKQP
GLNLDTQYYL SQQVHPVVGR ICEPIEGIDA VLIATWLGLD PSHFRAQQQH QREDEADNFL
GAPAQLTDEE RYRDCERFTF TCPDCGTENI YDNVFEGAGW LLCEDQACRN RTRRLPIAFS
RSGPICPACL RSTLRPEYSE KALYNQLSFY RYIFDWEYAV NKVLTVEDRT FLRNICKEDK
EVYKTLKDVV DKVLSTSGYS EVNLAKLFQA FTALKY
//
