ID A0A1Y1JJ96_PLAGO Unreviewed; 2890 AA.
AC A0A1Y1JJ96;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-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};
GN ORFNames=PGO_111780 {ECO:0000313|EMBL:GAW81728.1};
OS Plasmodium gonderi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=77519 {ECO:0000313|EMBL:GAW81728.1, ECO:0000313|Proteomes:UP000195521};
RN [1] {ECO:0000313|Proteomes:UP000195521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30045 {ECO:0000313|Proteomes:UP000195521};
RA Arisue N., Honma H., Kawai S., Tougan T., Tanabe K., Horii T.;
RT "Plasmodium gonderi genome.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755}.
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:GAW81728.1}.
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DR EMBL; BDQF01000012; GAW81728.1; -; Genomic_DNA.
DR EnsemblProtists; GAW81728; GAW81728; PGO_111780.
DR OMA; ESYYYAS; -.
DR OrthoDB; 5475218at2759; -.
DR Proteomes; UP000195521; Unassembled WGS sequence.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 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; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR013697; DNA_pol_e_suA_C.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR029703; POL2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10670:SF0; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT 1; 1.
DR PANTHER; PTHR10670; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR SMART; SM01159; DUF1744; 1.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000195521};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1947..2481
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 221..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1523..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2233..2302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2550..2570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2233..2253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2278..2297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2890 AA; 339929 MW; 89CF44146E7A053C CRC64;
MTTQARTKGW EKDSKINADY EYERLIKLEN KFNIKPWLSK GKKEGYLYNI VPTTLNVVVN
SSNKFQKKTG VHMYFVSDNN KTWRLTLFYR PYFYMKTKNI HNYEAVAKYL KKELDKNNVE
IDYVKKEDLS LYDHLNKKRS YLSNIFFKLS FDTIENLMNA RDFLSKIIEK NKKNKKHNNS
SNNDKHIFNE CEYELSQSKL EFSYKHDFSY TKYDEQEDSG WAKKSHDAVS SSPSGHRVDK
EKQNDQKKGN IVTNSADKER DSKKNDAHAT MSNQKLNMNE IVVNTKRQIL SKEEIMDEIV
EIYEYDVKYI TRICIDKNIR CGVWYKVTRD EEELYTESIH FEILNKKVLA PLNVLAWDIE
CYKDELKFPD KEKDEIILIS YMYNAQGYLI VNRNVMSKNI TEFLYKPNEE YSGAGTFKIF
NEQNEYFLLK RFLEHIKILK IHIFVTYNGD FFDIPYLCRR CEINNLSVPK EIGFIMNNNK
QECSCNFILN IDAYKWVERD SYLPNGSRTL KSVCKIKLKY NPTEVDPEQM VPIARKNPQH
LAVYSVSDAV ATFYLYDKFI HNFLFALCSI IPMNPDNVLR QGSGTLCEQL LMAEAYKKNI
LFPNKSKPVY NQYFTDFENK KKYFIYDDSF VGGTVQSLKC GIYRDDLKEY FNLDVDAYKH
MLNNIDSIID FWIHKDLNKN NSVNDNKYIN KNQIINLKKI KSDIINKLNF FIQNPKINTC
PNIYHLDVAA MYPNIILSHR LQPNAIITPD HCFNCSFYKQ RHLCQKQMVW KRKLEISPID
YGHVLSLKQD LKTRLFYPQK SYFKTNNNED SDKSTNDNLL DVPISKKKSW NELTEKQQHE
ELMKVIKDCS QKVFKKTKVA KEVDAASLVC QRENPFYVDT VRTFRDRRYV YKKALKECEH
EKKELLKAKK IDYIKIQELD DKILLNDSLQ LAHKCILNSF YGYVKRKSSR WYSDQMGAIV
TYTGSQIING AFNLINKIGI PMELDTDGIW CMLPKQFPEI YEVLILEKNE LNRLKEYENK
SEEELKNDSN VRKVEFEFPT NILNFQVHKK WTNDQYLVYN ENTDDYECIS KNEIFFELDG
PWHGMFLPAS EKSDDLLKKR YVVFNDKYKI SELKGFEIKR RGELRIIQKF QSEIFNHFLK
GKTKEESYYY ASLTANKWKN LIDTKAVDID NDDELFDLIL SKKVLNKSVK EQPNAKSFGI
TTAKRLSELL SNSSYVEDNN VSTQFIVASK PIGSDITFRA IPIQIFKTNV ETQIHYLGKW
LGVKLPPNVP VNVRDIIDWD YYKQKLEVQI LKLVIIPAIK QNINNPITSI SVPEWLKKQI
NISEGKQKKI TAFFVKKNLK KECVSNENDS SITPTKEILN TDLHPKAETA TEEEDITWKK
DDPSKRSLEK KSPFQVKEDE TCTAPSSLSN ATNPKKRSIE QVLLENLISK RKKLGQLNKS
NLDHSNSGSM VYKKVNSLDA YLEKNNNIII INHEKININN LKYTELLEMF ETDFKKWIQI
NNAIWKNNRS QIKKIRNEGK FKRKKYSLQD ERNEKEKKNN GATSGANVGA HFGAYIGDDD
EKTNSQKMSN LEPKYLHVIQ NDMDIVYLYK KVKKKKTTSH FKKGKNIGTN ASFTSGGMNS
YSPMNNNSKS DKHTLLKPYL KYFKHETDSD SSNDENDIFN DTNNVLDEND DDGIYYAIVS
LKNMNKFYKI KIQVYRHIYI NNYDPLDIKS NSKITINLVS SSGLSGSSNN ENFIFHSNAF
ANCFLPRNVK IFNLYEFIMS EKYFNRYVVN TLNANYHESI VSVYETKIPL YFDFLSRYGN
SVEIDSTNYN SIFDENKCFK SHCFSKVEKN KIKNVSQDYL DDIHIIHIHI FHTLIDTVCN
RIFISVYDQF EENSDDLSIG NKIMFSGIPS DKNFDPYETF IKFLQLQEHY AHFKDNITFD
TNANGIFTNN TTSGNFFTKN KDIHNDQSKL FYTDQIEETN KKQILDHLFD KNFFIKNVQR
DLLFLYHYRK FDTYYESNSN VYKVLEYLDL YLNKYRNNML SGKKKYIFYV SSTIDKKKLG
WWSTGKYFPC YFKKFENSGK YQNISRVSYK QDAFNLSLQL FFENYHKVEE DLNFSRISNI
PLFNLLNVNK KNQKHKFIYD ILYASFLKKY KGILWLSYFG NYDLGIPCLN INNFCDYDLV
KKNSDIINQG IYRGYIVHLF FNESLIFNSV RLFTKYANAN SSKEYYNPTI SGKNSHMKKN
YHKRVQNGDM VKNRHPMKHT KNSVRKNVEE DLDADDMSTT DDNNSKIGTY GNRKGREGSV
SENLDRGTKK NDFYDDNEMQ ENNGLSDFSE KKNLIKNKYD INSIVEQNSH VSQFSNFAFK
LLGQSLEYLI SKISSLSMLI TNKTFESISD IFTSFYFWVS SNSSLLYDVA LYNKVLECSE
IYQNNLINIM KKKFNANIIF ADLRNLVISF NEFSVISGRN ILKNLIKYFS HSDSIYANVP
FYIKQEYIAA CQFDKYNFIR YKEYSNPNEE NTDENLKIIE YLPPICESFL RYVLDVITLN
PLQDIVALYE KWNHHNNKQS EAENKLTLSS EPAKMDEQNN NEASKPNQTN MKDEKNYFNI
ILKTDKLTDK INLAQRAQLK YIYDNSFDDL GEVCESFALI NENVDVLSYK IEEKLKDLWF
MPGIIYKKIK KSIKYKKYLV ENYWPYDDDD DEIDENNMSM VPFLFPKTLG NLAKRESNWK
LEIVKFCIFL MENDKLLNLE NENCNEAFHE KRHELFEIIG DCEYNRKNSH WKSPCQELIL
KDIFCENCSS VYHMNVVTSL VEAEINGKAS FIWLCKNCNS KYDNEFIELK ILSLLQETFD
AYNAQDLVCK NCNSIKSFYR RAICKCGQTF MPRLDIANWT RTLEIMENLA TMLNMPILLD
ALKSMKTYLV
//
