ID   DPO3A_SYNY3             Reviewed;        1355 AA.
AC   P74750; P73215;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   25-MAY-2022, entry version 154.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
DE   Contains:
DE     RecName: Full=Ssp dnaE intein;
DE   Flags: Fragments;
GN   Name=dnaE-N; OrderedLocusNames=slr0603;
GN   and
GN   Name=dnaE-C; OrderedLocusNames=sll1572;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   CHARACTERIZATION OF SPLIT INTEIN.
RX   PubMed=9689062; DOI=10.1073/pnas.95.16.9226;
RA   Wu H., Hu Z., Liu X.-Q.;
RT   "Protein trans-splicing by a split intein encoded in a split DnaE gene of
RT   Synechocystis sp. PCC6803.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:9226-9231(1998).
RN   [3]
RP   CHARACTERIZATION OF SPLIT INTEIN.
RX   PubMed=10734038; DOI=10.1074/jbc.275.13.9091;
RA   Evans T.C. Jr., Martin D., Kolly R., Panne D., Sun L., Ghosh I., Chen L.,
RA   Benner J., Liu X.-Q., Xu M.-Q.;
RT   "Protein trans-splicing and cyclization by a naturally split intein from
RT   the dnaE gene of Synechocystis species PCC6803.";
RL   J. Biol. Chem. 275:9091-9094(2000).
RN   [4]
RP   CHARACTERIZATION OF SPLIT INTEIN.
RX   PubMed=11170467; DOI=10.1021/bi001786g;
RA   Martin D.D., Xu M.-Q., Evans T.C. Jr.;
RT   "Characterization of a naturally occurring trans-splicing intein from
RT   Synechocystis sp. PCC6803.";
RL   Biochemistry 40:1393-1402(2001).
CC   -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria. This DNA
CC       polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC       is the DNA polymerase (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the PolIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III complex
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: This protein undergoes a protein self splicing that involves a
CC       post-translational excision of the intervening region (intein) followed
CC       by peptide ligation.
CC   -!- MISCELLANEOUS: The intein is a split intein capable of protein trans-
CC       splicing. The N- and C-terminal halves of dnaE are encoded by two
CC       separate genes located 745 kb apart in the genome and on opposite DNA
CC       strands. The dnaE-N product consists of a N-extein sequence followed by
CC       a 123-aa intein sequence (Ssp dnaE1), whereas the dnaE-C product
CC       consists of a 36-aa intein sequence (Ssp dnaE2) followed by a C-extein
CC       sequence. The N- and C-extein sequences together reconstitute a
CC       complete DnaE sequence that is interrupted by the intein sequences
CC       inside the beta- and tau-binding domains.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BA000022; BAA18870.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BA000022; BAA17242.1; ALT_SEQ; Genomic_DNA.
DR   PIR; A59016; A59016.
DR   PIR; S75328; S75328.
DR   PIR; S76958; S76958.
DR   PDB; 1ZD7; X-ray; 1.70 A; A/B=775-933.
DR   PDB; 1ZDE; X-ray; 1.95 A; A=770-936.
DR   PDB; 3NZM; X-ray; 1.55 A; A=772-933.
DR   PDB; 4GIG; X-ray; 1.80 A; A=775-933.
DR   PDB; 5OL1; X-ray; 1.75 A; A=776-889.
DR   PDB; 5OL5; X-ray; 2.33 A; A/B/C/D=776-931.
DR   PDBsum; 1ZD7; -.
DR   PDBsum; 1ZDE; -.
DR   PDBsum; 3NZM; -.
DR   PDBsum; 4GIG; -.
DR   PDBsum; 5OL1; -.
DR   PDBsum; 5OL5; -.
DR   AlphaFoldDB; P74750; -.
DR   SMR; P74750; -.
DR   IntAct; P74750; 2.
DR   STRING; 1148.1653960; -.
DR   MEROPS; N10.003; -.
DR   PaxDb; P74750; -.
DR   PRIDE; P74750; -.
DR   EnsemblBacteria; BAA17242; BAA17242; BAA17242.
DR   EnsemblBacteria; BAA18870; BAA18870; BAA18870.
DR   KEGG; syn:sll1572; -.
DR   KEGG; syn:slr0603; -.
DR   eggNOG; COG0587; Bacteria.
DR   InParanoid; P74750; -.
DR   PhylomeDB; P74750; -.
DR   EvolutionaryTrace; P74750; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   Gene3D; 1.10.10.1600; -; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 1.
DR   Pfam; PF07733; DNA_pol3_alpha; 1.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   Pfam; PF02811; PHP; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   SMART; SM00306; HintN; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF51294; SSF51294; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
DR   TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR   TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Autocatalytic cleavage; Cytoplasm; DNA replication;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Protein splicing;
KW   Reference proteome; Transferase.
FT   CHAIN           1..774
FT                   /note="DNA polymerase III subunit alpha, 1st part"
FT                   /id="PRO_0000007364"
FT   CHAIN           775..897
FT                   /note="Ssp dnaE intein, 1st part"
FT                   /id="PRO_0000007365"
FT   CHAIN           898..933
FT                   /note="Ssp dnaE intein, 2nd part"
FT                   /id="PRO_0000007366"
FT   CHAIN           934..1355
FT                   /note="DNA polymerase III subunit alpha, 2nd part"
FT                   /id="PRO_0000007367"
FT   NON_CONS        897..898
FT                   /evidence="ECO:0000305"
FT   STRAND          781..784
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   TURN            785..787
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          788..791
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   HELIX           792..797
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          803..807
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          811..817
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          820..834
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          839..842
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          847..850
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          855..857
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   HELIX           858..864
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          868..871
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          877..879
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   TURN            883..885
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          887..889
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   HELIX           890..893
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          896..899
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          901..916
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          923..925
FT                   /evidence="ECO:0007829|PDB:3NZM"
FT   STRAND          928..932
FT                   /evidence="ECO:0007829|PDB:1ZD7"
SQ   SEQUENCE   1355 AA;  153001 MW;  7C4F61EE4C36EE0F CRC64;
     MSFVGLHIHS DYSLLDGASQ LPALIDRAIE LGMPAIALTD HGVMYGAVEL LKVCRGKPIK
     PIIGNEMYVI NGDIEINKRH RRFHQVVLAK NNQGYRNLVK LTTISNLKGI QGSGIFARPC
     INKELLEQYK EGLIVTSACL GGEVPQAILK GDLDHARQVA KWYKNLFGDD YYLEIQDHGS
     VEDRLVNINL VKIAQELDIK IVATNDSHFI SCNDVEAHDA LLCIQTGKLI TEEKRLRYSG
     TEYLKSAEEM HLLFRDHLPD DIIETAIANT LEVADKVEAY SILGEPRIPH YPIPPNHTPE
     TYVEDIAWDG LLERLKCRER ADITPVYKER LEYELRMLEK MGFCTYFLVV WDYIKYARDH
     GIPVGPGRGS AAGSLVAYCM KITNIDPVHH GLIFERFLNP ERKSMPDVDT DFCIDRRDEM
     IEYVTQKYGE DKVAQIITFN RMTSKAVLKD VARVLDIPYA ESDKMAKMIP VSRGKPAKLK
     VMISDQTPEP QFKARYDNEP WVKKWIDMAI RIEGTNKTFG VHAAGVVISS EPLDQIVPLQ
     KNNDGAVITQ YYMEDVEAMG LLKMDFLGLK NLTTLQRAVE LVAETKGIEL DLDDLPLQER
     KALQIRARTG SKKLPDDVKK THKLLEAGDL EGIFQLESQG MKQIVRDLKP SGIEDISSIL
     ALYRPGPLDA GLIPIFINRK HGREEISYQH KLLEPILNET YGVLVYQEQI MKMAQDLADY
     SLGEADLLRR AMGKKKAEEM QKHRAKFVDG STKHGVPSRI AENLFDQMVK FAEYCLSFGT
     EILTVEYGPL PIGKIVSEEI NCSVYSVDPE GRVYTQAIAQ WHDRGEQEVL EYELEDGSVI
     RATSDHRFLT TDYQLLAIEE IFARQLDLLT LENIKQTEEA LDNHRLPFPL LDAGTIKMVK
     VIGRRSLGVQ RIFDIGLPQD HNFLLANGAI AANCFNKSHS TAYAYVTYQT AYLKANYPVE
     YMAALLTASS DSQEKVEKYR ENCQKMGITV EPPDINRSQR HFTPLGEAIL FGLSAVRNLG
     EGAIEQIITA RDNSEEKRFK SLADFCTQVD LRVVNRRAIE TLIMAGAFDG VQSNRNQLLH
     DLELVIAWAQ KRAKEKETGQ LNIFDSLTAG ESIKAKEAAN NGFEQEPSAP PVAEFSLQEK
     LQLEKEHLGF YVSEHPLKSV QRSARLLSPI NLVDLDQYKV RQKVSAVAIL VAVKKIITKK
     NGQPMAFLTL EDMSGQSEAV VFPSNYERLQ DVLIEGSQQM IWGKVDRRDD QYQLIVEDLE
     PVEEVKMVML DLTPQEIANT STQARLKQIL QSHAPQKEQM KIPVVACINE GPTKHFIRFG
     ENYWVNDYGT AVASLQELGF RARLEPLLPQ SQSVG