ID A0A094FQN6_9PEZI Unreviewed; 2689 AA.
AC A0A094FQN6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA polymerase zeta catalytic subunit {ECO:0000256|ARBA:ARBA00021589};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=V500_07812 {ECO:0000313|EMBL:KFY86180.1};
OS Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY86180.1, ECO:0000313|Proteomes:UP000029284};
RN [1] {ECO:0000313|EMBL:KFY86180.1, ECO:0000313|Proteomes:UP000029284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY86180.1}.
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DR EMBL; JPKC01002385; KFY86180.1; -; Genomic_DNA.
DR STRING; 1420913.A0A094FQN6; -.
DR HOGENOM; CLU_000203_0_0_1; -.
DR Proteomes; UP000029284; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016035; C:zeta 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:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
DR CDD; cd05778; DNA_polB_zeta_exo; 1.
DR CDD; cd05534; POLBc_zeta; 1.
DR CDD; cd21675; SMP_TEX2; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 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; 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; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000029284};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00023055};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 1762..1788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2039..2230
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 480..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1855..1874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2310..2341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2367..2435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2441..2460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2518..2689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2367..2413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2415..2435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2441..2457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2521..2541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2548..2586
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2590..2609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2689 AA; 300891 MW; B9019D72183B19CD CRC64;
MDLFRVRLNC IDHYQAFPTR FDPQLRRDVA PSEINNEPKV PVIRVFGTTE TGQKVCAHIH
GTFPYLYIDY NGQVTSHEIG AYIHRLHLSI DHALAVSYRR SVYDRRTRFI ARITLVKGVP
FYGYHVGYQY YLKIYALDPA VMTRLADLLR QGAIMKRVFQ PYEAHLQFIM QWMTDYNLYG
CGYIDNQRVY FRGPVPKYEE LDRLSHLWHD RSIPAEFVIS EAKLPRLSHC SLEVDIMVQD
ILNRQEIAQR PLHHDFIERS NPLPLDQKLV HSMSELWRDE TKRRKAKMKV AEPGSNAFPP
EVLISMSAGL RSSEKGRWAH EEEYRELVHN RIQEERAKSD GSNVSFDTFI KPKPAEDYIN
TTFQSVEDLY PENLGPILGL KNEENSVLPK EEFVPGNIEV DENCIFNVSD ENESPYDSDD
EIIRDIEQPQ KKRGNTVLPP ILATNSFKFE HTVDPNTVPL SNASRVHVAG DLCSSIALGG
RDHRTKTGTY EPKREATPNS TPEVASSEVT AEGLQDINVA TSLGESKPPS LKRSISLMPS
DEGYNKRRKF DFVIAPITPT SFAIESRPIV SHQALPGYES MAENGNCNAR KKGSMLSEID
QHNLPLLPTV NGLSHTLNPG QKLARPNTGS GKLDPQPRPN PEPTDPQETD TMFRLSQCGS
SQDQGKTASN ESKNLFGAAP PSIQTQLEPE ARNIPSPSGQ QLKLVSSIIW DLRGTNWVAR
SKYVVAFAKS PPLKETVIPS LHPPVIYQGP YYGNELDVPE RPTEWAGKEF KLESLTVPFL
PDFDETGTSA ASLGEKIAVV YNKLSEKHVY DRRQQRCRLR VWEIGEPPPA FNDVAEWECK
EILAKTMSIT LKSEGQTGLQ PENSVHSQIE GPTQTNKHGF QYTQPQKTST LQNNAQYMSV
MSLEVHINTR GNLAPNPQED EIQCAFWSLQ LGEDHPDDPG AGAASHVGIV VSSEDGQAAK
NIAKQTPIQV FEESSELDLL VRIVEIVRTY DPDILTGYEV HNCSWGYLVE RAKLKYEYNL
CEELSRMRTH SHGHSERDSD KWGFRQTSAI LVTGRHMINI WRAMRNELNL LQYTMENVVF
HLLHRRIPHY AWRDLTLWYT SGKFADLAKV IDYYLCRVQL DLAILDQNEL ITRTSEQARL
LGVDFFSVLS RGSQFKVESL MFRIAKPENF VLVSPSRKQV GAQNALECLP LVMEPQSAFY
TSPLLVLDFQ SLYPSVMIAY NYCYSTFLGR IVNWRGGAGK MGFSEYKRQD RLLELLKDFI
NISPNGMMYT KPEIRKSLLA KMLGEILETR VMVKSGMKFD VNDKTTQKLL NNRQLALKLI
ANVTYGYTSA SFSGRMPCAE IADSIVQTAR ETLEKAIALV HSVKRWGAEV VYGDTDSIFI
YLKGRTKDQA FDIGNEIAER VTNMNPRPVK LKFEKVYLPC VLLAKKRYVG FQYEKKDQQE
PKFDAKGIET VRRDGTPAEQ KIEERALKIL FRSSDLSAVK GYFQAQCEKI MTGSVSIQDF
CFAKEVRLGS YSDKGPPPPG ALISIKRMLE DHRVEPQHGE RVPYVVITGA PGARLIDRCV
APETLLQSDH NELDSEYYIS KNLIPPLERI FSLVGANVRS WYDEMPKIQR VRRLDVDPQL
SGEPADLPFS KKTLESYMKS SSCLVCQEKL ESNTAICPTC LGNRPSSMLA LQTRLAAMER
KYQALENVCR SCSNIPWTDE VRCDSKDCPV FYSRVKEKAR LTTERKVAGR LMERLQGDTG
GHEDLEWISG GTVQTMMGGV TYFLFVYVLG GLTFLPLLVV VLIIHAYLTF PVRKAPIEVP
GAPGSSGLLR DGDRADAIRS ASKSLDEKFQ SRSSQESDVA AGYFAVCREY VPGGINGKPP
ERTTPTGSTV VTSPSPSVYQ SMYRSIFDRK KDTNPLDIKG VGKPTSRGGN VFYVVLRHQH
ILLFDTEEQL EVRYVLSLAH HDVSIYGGGE EIPDGELFIK RNAICLTRRA DVGEMTPDGT
PSKPFYLFTD SLSEKEDFYF ALLKNVQRRP EDSSNVPKPL QFDVKHIIEL VQRLHSSEEN
MQIRWFNAIL GRIFLGIYKT PDVEAFIRAK ITKKISRVKK PAFLSKIVLR NVDMGEGAPY
ITNPRLKDLT VDGDCTIEGD MLYTGNFRVE IAATARIELG SRFKAREVDL VLAVTIRRVE
GHMLLRIKPP PSNRLWMTFE TAPRIDMSIE PIVSSRQITY TLILRQIENR IKEVIAESIV
MPFWDDLAFF NTDGKKWRGG IWTDSELSRP SQTLETIIAE DGDVDELEQV ENGTSSSLPP
IGKSMSTPAL ESSLHVESFA RKTAKSVFNL GPSKKSASST SVETKSSATS NKPKSIRKHS
FASAVVSTDN TNIDALKVES SSDHSSAAST MAALSAKSPP PSATASPVGS PSKPSSILKP
KSGSISSFSS READNVECAE LDSTISDKLR RADTESLKLN QHKSEETFAE SRGKFSDSSH
AEAIGSSHLG LIGQDANGSL NMMEDSEAGA SVGRGSTPKR NTLSAVANAA ENARKWGINA
LQRSRDQTKI SMASEVGSET PDLTQPMGRG KPLPPPGTPL PLPNRRTKTA PIPVPKRRPL
PPPYLTRQPS EVKARSSRSS STSRQAPPLP KRHSRNDYAA SEEGVLVVAA PDSEPVSPTE
DSANAYISRW EGGDNDDEAN DEANDEAGTS AKEDPLLPIN VLESTGSLH
//
