ID A0A091Q2T5_LEPDC Unreviewed; 2932 AA.
AC A0A091Q2T5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA polymerase zeta catalytic subunit {ECO:0000256|ARBA:ARBA00021589};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE Flags: Fragment;
GN ORFNames=N330_03126 {ECO:0000313|EMBL:KFQ03984.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ03984.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ03984.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ03984.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755}.
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DR EMBL; KK669721; KFQ03984.1; -; Genomic_DNA.
DR PhylomeDB; A0A091Q2T5; -.
DR Proteomes; UP000053001; Unassembled WGS sequence.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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; cd22287; REV3L_RBD; 1.
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; 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; IPR032757; DUF4683.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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; PF15735; DUF4683; 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.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 529..919
FT /note="DUF4683"
FT /evidence="ECO:0000259|Pfam:PF15735"
FT DOMAIN 2068..2286
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 2352..2802
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 2844..2911
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 215..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1534..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1759..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1846..1942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..856
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..974
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1853..1898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ03984.1"
FT NON_TER 2932
FT /evidence="ECO:0000313|EMBL:KFQ03984.1"
SQ SEQUENCE 2932 AA; 330234 MW; AAF86B286303CE97 CRC64;
SSLMLEGVEP QSTCELEVDA VAADILNQLD IEAQIGKNPG LQAIWEDEKQ RRRQKCESSQ
IKTPESQDRG FVPATESEKF FQKRLKEILK QNDFSVTLSG SVDYSNGSEE FSAELTLHSE
VLSPEAFQCT PANMVEVHKD KKMNKESSRM HTDKEEEALI NEEAILNIVE NSQSFQPLSQ
RLSQTTVFMD SSADEAMIDL LAGLENDGYQ MGHHKTLSHH RSLGSCRNSQ NSDDEENEPQ
CEKEEMELSL LMSQRWDSSI EEPGPKRRSA GKNTHRSSTE EDSSSEEEME WSGNNMLLTN
LSIPQLDGTA DENGDNPLNN ESSRTHSSVV ATSKMSVKTS IFHKDAATLE PPSSAKITFQ
CKHTSALSNH VLNNEDLVED LSQPNTETRP ELSVHSLTKE STYSAKYPTP FSNSTHAENS
HKDSNKKDTL PVPSCESNIF EYEDDISSVS RQIPSRKYTS IRKAEKDVSF MHVGRHIGDS
MLNKNLFNFS DLSHSGHSKG KMSSEVNEKS SSASINSFFP ATVTENCELM SCSGGSRTMV
HSLENNTDEG GLNKLKIRYE EFQEHKAEKP SLSQQAAHYM FFPSVVLSNC LSRPQKLAPV
TYKLQQGNKQ SRLKLNKKKH GFISHQEPAS VHDVASVKET CYTQGNACSN IPDKDSALPS
DLVQVPLEAF ENKMPTSTAN YTDCQFADGS LETEQSFGLC GNKYTLRTKR KVNYETEDSE
SSFVAHNSKI NLPQPIESVE SLDGSQKSRK RRKLSKKLPP VIIKYIIINR FRGRKNMLVK
LGKVDSSEER VVLTEEKMNL YKKLAPLKDF WPKVPDSPAT KYPIYPLTPK KSHKRKAKHK
STKKKAGKPQ KTGSKNIRRT LSFRKRMHTI LSPPSPSYNA EAEDCDYNYS DVMSKLGFLS
ERSTSPVNTS PPRCWSPTDP KAEEILTKLD REALFSRAPN MYNSKTVNSS VGKNSRAKTQ
VKKCKKKFAS PAVSTKKKKK INQADKTADD GKKKPRTKER QKNAEKASSR KRVVFKDEKG
HTRSAAEVKF VLKHQDLPEI SYNSVNLQPL HNWKDSPLPG YSVGYLPSAQ LPSAADAQGN
SSGCFNSLME IDKPVDTQCL PAPREDPHSS FASTPVASGR EVPKMSSQRP RTQSAIFRMK
ESAVVQNIFD PSNQSTQVTQ NVRISKDKTS AKAEEVKNLQ NRYLPSAGKL NEARDSLNTA
KMDQLHATNY LHCKDNNQQQ IFCLPEASKH SDPCSSILKS SEESPGPHQL PKNCFVTSLK
SPVKQLNWDQ NQRGFIFDMS HFKPETVKQR SLSETTMQPK PISQYKNRTI VAPSAFSEGQ
SGLAVLKELL QKRQQKAQNA SVTQEPLQAK TQLSRTVPCP LEQNKAIKRS RSVASPRKSR
APRNTKPKEK TPKLSKMESL SQQFTSRIDH SVSDDSPVFF SDPGFESCYS LEDSLSPDHN
YNFDINTIGQ TGFCSFYSAS QFVPADQNLP QKFLSDAVQD LGSGQTTEND FMCHDDQKSE
EEKQHSSSTS KWIRSGSLSP ELFEKTSLDS NENHCRSQWR KNVHPSTSRS SSIDTSCTQE
TEVCLNEKFK LNRNTVNKER FLNLPQPTSS DWIQSHIRKE TTFEPCQPLD SVNTSFTSIL
SSPDGELIDA ASEDLELYVS RNNEALTPTP DSSPRSTSSP SQSKNGSFTP RTAHILKPLM
SPPSREEIMA TLLDHDLAET IYQEPFCSNP SDAPEKPREI GGRLLTVETR LPNDLLEFEG
DFSLEGLRLW KTAFSAMTEG PRPGSPHYGH STVNRREGNS HKTSEDKKIV IMPCKCAPSQ
QQVQIWLHAK DEYEHFKKLP KNHPAELAKA SENFSSAVFL EDERPVVPTK NSPASVAEAT
KTQTKETCDR PISTIGTSIN TKNDMDSNKT PSESKTLTTS TLEHDKEEEE DDYYVNYSSP
DSPVLPPWQQ VASPDPKQSN LEDTEWNSQN IILSSVEGND VVPVGSAQNA LSTQEDVRTS
FDTSPFQVND DPGNSESAFL HSTPIVQRKN QDGVPEVLGF TPLSTEPKAQ KLSHKRGNNA
DGLRRVLLTT QMKNQFAGLG APKKETSQIE GPSLNNTYGF KISVENLQEA KSLHEVQHLT
LISMELHART RRDLEPDPEF DPICALFYCI SSDTALPNTD KKEITGAIVI DRDRTLSSQG
SRDQAPLLTR SGVTGLEVSY ATDERTLFQE VVNIVKRYDP DILLGYEVQM HSWGYLLQRA
AALNVDLCQM ISRVPDEKKE NRFAAELDEY GSDTMSEINI VGRIILNVWR MMRNEVNLMN
YTFENVGFHV LHQRFPLFTF RVLSDWFDNK ADVYRWKMVD HYVSRVRGNL QLLDKLDLID
RTSEMARLFG IQFLHVLTRG SQYRVESMML RIAKPMNYIP VTPSIQQRAQ MKALQCVPLI
MEPESRFYSN AVLVLDFQSL YPSIVIAYNY CFSTCLGHVE NLGKYDAFKF GCTSLRVPPD
LLYQIRHDIT VSPSGVAFVK PSIRKGVLPR MLEEILKTRI MVKQSMKAYK HDKAITRMLE
ARQLGLKFIA NFTFGYTAAN FSGRMPCTEV GDSIVHKARE TLERAIKLVN DTKKWGAHVV
YGDTDSMFVL LKGATKEQSF KIGQEIAEAV TATNPKPVKL KFEKVYLPCV LQTKKRYVGY
MYETLDQKDP VFDAKGIETV RRDSCPAVSK ILECSIKLLF ETRDISQIKQ YVQNQCMKLL
EGKASMQDFI FAKEYRGSSA YRPGSCVPAL EITRRMLAYD RRSEPRVGER VPYVIVYGMP
GLPLIQLVRR PIEVLQDPSL RLNATYYITK QILPPLARVF SLIGIDVFSW YHELPRIQKA
ASAARSELEG RKGTISQYFT TLHCPVCDEL TQYGICNKCR SQPQHVAVIL NQEIRELERK
QEQLVKICKN CTGCFDRQIP CVSLNCPVLF KLSRVSRELS KAPYLRQLLD QF
//
