ID A0A183CCG1_GLOPA Unreviewed; 1400 AA.
AC A0A183CCG1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_001056200};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_001056200}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
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|ARBA:ARBA00024632};
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DR WBParaSite; GPLIN_001056200; GPLIN_001056200; GPLIN_001056200.
DR Proteomes; UP000050741; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR004868; DNA-dir_DNA_pol_B_mt/vir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013955; Rep_factor-A_C.
DR PANTHER; PTHR33568; DNA POLYMERASE; 1.
DR PANTHER; PTHR33568:SF3; DNA-DIRECTED DNA POLYMERASE; 1.
DR Pfam; PF03175; DNA_pol_B_2; 1.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 54..164
FT /note="Replication factor A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08646"
FT DOMAIN 891..1146
FT /note="DNA-directed DNA polymerase family B
FT mitochondria/virus"
FT /evidence="ECO:0000259|Pfam:PF03175"
FT REGION 1261..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 177..204
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1262..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1391
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1400 AA; 161392 MW; A8179A0F1EC97EC1 CRC64;
MSGLLRFKLD NSGGAGGQKR RQGEESFPSS VKELRDVVEF NAAGLFFVMA KIVNLQYRIY
NACPLKHKGL FCRRKLDDEM RCAVCDHRAK KPLQNLFVRI ELQDRKDPEC TQYATLFSYG
AEKFLNLKAV EVAEMSETNP ERLEALLEAK LDKKVIVKLN LKEAKGDYEG SELDWIIATI
SNAEDEAKKN EEEEEEEVKI VDEDSRRQQI HQIGGNGRAR GDDGEPVAAT EQPLFQQTAH
YVHRLDRFSL SRHITEFVLN ASNEEPDEAL RAAFDSLISQ AIQNSEQQSG RRVLKIGITL
QGRGLYDPIL LPPRSPEQNS ADALMGELDK LGQSDGDAGE DDGGDWVDKK TLLLSEPVQI
IITCISPPAG AGPRFHPYQH WGYNEQFRIQ IRNEGDNYCM FYALLAARAY HDRELFEEWH
NAPPQQQQQE QQFARLSLMQ DFCQDTDVFK RLLANFATLR SAVERLMRAA DIPEDLNAYG
MDHLQSVQDY WDQRFPSLYR IVLFEDRPEE LPKPIWKVGP DHPCQKEVGV KIRCPSCNRF
FFSRRCFDGH KGQTCALLKR CTCCQRVYQL NPRLPHKCFS KYCRRCKVYH DSKSGCFIQK
LRVPPEKPRY RIVCWDTETR LQPTVEGQQV HKVNYLSARV TCADCADLLA QGHQQRDDCE
ICKNEEGLVE RMKDWSEAGG DEPVEAFVEW ILTAENYTVR LPHLPDREEY CTGSMKHDKY
TENRLTPFFL PDELREYCRN DTEILLKSVL QFRHILMHDI TNGFEVLPIS CTIASACMCI
FRAKFMKSNQ LAIVPEAGYE RNDRASVLAI KYLDWKAKSE GVQISHAGNG REMRIKKYKL
DGWIEQQNKC IEECEINALL ADPRNAEMKA FFDDLGVERG PIEPRLAFCG VYDIVSLYPW
VNYDTDYPIG IPKIVHPTAE EIVVDWGSPN DLRYRGIYRV RVIPPRGLRI PVLPVKLDEH
EQRSYTGNYT HIELERALQN GYKIDRFWRA WHYEHWSDQI FKEYVRLFLK LKIEASGFPE
GVVSDEQKRI FAAEYLRIYH VQIDLESVKK NPGLRFIAKL MLNSLWGKFG MRNELGSNKV
ITRPQEFYKL VLDHKIELSA IIPLSDDAIR VTYKHKKHFA QEHSSSNIVL SLWTTSRARL
KLLDFMMQIQ NTEGAELLYT DTDSVIVKHR RNVVPIQTGE YLGQMSEEYT GYEIRAFICG
GAKQYAFQMI DKRSGETKYV QKIRGITFDV RNSQALQFEH FKQKVLNFGG HDQRPAVFSY
DKIQPTRSSQ IITREQRKQN MSADNTKPST DVHDKTADKS DKETLPPKAA NETDSAEKKK
KEPPSPTDQL EEVSSSAEIS KMSAIGRKRR HSSEECCSSS LEGEEAEEYM SDDEVEYEEG
TDDESPEEGD EEKEKEQQPQ
//
