ID J9VRM7_CRYNH Unreviewed; 943 AA.
AC J9VRM7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=DNA polymerase lambda {ECO:0000256|ARBA:ARBA00016513};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=CNAG_07766 {ECO:0000313|EMBL:AFR97122.2};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR97122.2, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR97122.2, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; CP003828; AFR97122.2; -; Genomic_DNA.
DR RefSeq; XP_012051516.1; XM_012196126.1.
DR AlphaFoldDB; J9VRM7; -.
DR GeneID; 23890584; -.
DR KEGG; cng:CNAG_07766; -.
DR VEuPathDB; FungiDB:CNAG_07766; -.
DR HOGENOM; CLU_354876_0_0_1; -.
DR OrthoDB; 49764at2759; -.
DR Proteomes; UP000010091; Chromosome 9.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00027; BRCT; 1.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR002008; DNA_pol_X_beta-like.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR PANTHER; PTHR11276:SF43; DNA POLYMERASE IV; 1.
DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 345..445
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
SQ SEQUENCE 943 AA; 104881 MW; 0AA383E1C8652239 CRC64;
MAPAIKREAL SAKFWKVFDD LDDSGILEET GEERREYDES VRNEIDWKIQ PVFKSEGPTT
VVHVTETLMD DDPFIEHDTC SIPLPPRVAS INVARTAHAF PFAESQPPPS FHPSLMGKTS
TPRAHRLLRQ ESIESVSDEV CQPDEELPLK PKNETRMGSE LSRHSVFTES PVPLASCITS
IPVATSSATH LPSFRQSQFG GVSTPHTANV TFPNIPTPSF DEATPAGPSA RPIAIKNSKH
PPMTASPRRR AHTIDTPEYI PSPVDTPDTS RPAVGTFGRS PRDCIATPGP LGLLPLKGEA
NKKFQNLSKH FQAFVAKKDC GSVGGKNAAK RKVKQPVEKI SGHSLGDGVF RGLRICLPPG
EKPMSIQRQA WDQIIELGGT VVLYPDKATT HVIYDSHNRT KAKLAKLLRL QSLDELPLGT
ECVIWEWISQ SKLNGVLLPV ENFRSFRVDS LFSRAMSAGS LDQRNPRLAG TADQRLTGRT
ALESETESEE SLPKKIRLQA SVAQFYSNNP LRNAVTLSTA GPSKLRDSVP HHAVETEHTV
SKGPGWKQGK EDQRDALDEM IEGVKDGILP EDEIVDDEQA AYSPSDDRGI EDDVDSAARF
SKGGQEKSSK SEKGPNEWLA EKFDQLHDLY NGQVGKNPHS IRQYRNAAAA MRRTTFPITS
GAQARKINGI GEALAERINE FISGVPGRAF YEDNEHARCV ALFKDIYGVG RQYANELYQM
GARTITDLRT GRFPLSPGQQ IGLALYEDLR SLIPREECKQ IFELIKLEAK TVDEKLWVEI
MGSYRRGSET SGDVDILITR DDTDGKTHKG AIKKLVDKLK AKGVITHELS APHDWNALEA
KWMGVGRVGQ SAIYRRIDIL CVPYESWGAS LIYFTGNELF NRSLRLYARK LGYNLNQRGL
YRNVVRAIDG TKVLEGDRVA SRTEEEIFQE LGLRWRHPHH RRP
//
