ID A3LTR7_PICST Unreviewed; 693 AA.
AC A3LTR7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=DNA polymerase II complex component {ECO:0000313|EMBL:ABN66463.2};
DE EC=2.7.7.7 {ECO:0000313|EMBL:ABN66463.2};
GN Name=DPB11 {ECO:0000313|EMBL:ABN66463.2};
GN ORFNames=PICST_83141 {ECO:0000313|EMBL:ABN66463.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN66463.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN66463.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CP000498; ABN66463.2; -; Genomic_DNA.
DR RefSeq; XP_001384492.2; XM_001384455.1.
DR AlphaFoldDB; A3LTR7; -.
DR STRING; 322104.A3LTR7; -.
DR GeneID; 4838760; -.
DR KEGG; pic:PICST_83141; -.
DR eggNOG; KOG1929; Eukaryota.
DR HOGENOM; CLU_397390_0_0_1; -.
DR InParanoid; A3LTR7; -.
DR OMA; ERCLHYK; -.
DR OrthoDB; 20296at2759; -.
DR Proteomes; UP000002258; Chromosome 4.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.10190; BRCT domain; 4.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR PANTHER; PTHR13561; DNA REPLICATION REGULATOR DPB11-RELATED; 1.
DR PANTHER; PTHR13561:SF20; DNA TOPOISOMERASE 2-BINDING PROTEIN 1; 1.
DR Pfam; PF00533; BRCT; 2.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR SMART; SM00292; BRCT; 4.
DR SUPFAM; SSF52113; BRCT domain; 4.
DR PROSITE; PS50172; BRCT; 3.
PE 4: Predicted;
KW Nucleotidyltransferase {ECO:0000313|EMBL:ABN66463.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transferase {ECO:0000313|EMBL:ABN66463.2}.
FT DOMAIN 2..77
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 98..203
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 303..388
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 571..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 78635 MW; D7D54AC8A6C9BD0A CRC64;
MANKKPLDGL SFCCTGIKAK KREEIAEKIA ALGGIHYSDL MSDVRFLLVG DRDTAKYQFC
IKERYDVTFL TEDSILELYD CWIRGDDDDS EKLQILSYKQ PVFSGLSICI SRIESSDSFR
KKPASKESLS DYFMYRSLAS EVAKNGGKPA DSLTNSNSCI VTTQTGGKRY SKAVEWRIPV
VHPLWIHDSL IRGAALDMED YKLSEDTKTL YESGSKVWKQ LILAKTQPEQ STVASVAVDA
NEFQAEKTKK PLKKNAEIWN SIMDHTRQQT RRFVRDSLWD DEPESDLSVP KSSIIEKETI
QLQQRSLFSG YNFLLIGFTD HQANLLSQAI ANHGGEISTD TMDSTITHII LPAANGSQSS
MMLKILAPSI KSKISDGDIK VVTEWFIERS IFYSSAVIDR WSQPLKGMIS SNKKFKICIT
GFTGIELLHI EKLINNLGFE FCETLTSKRD LLIININLFK TNLSKNSPKL FQYKYPDITN
CPTYQSGTSS VSVISSKNKI NAAKKWEIPI VSISYLWEIL ELSVNREVPV MPDLLDLTWC
IFAPKNYSRP KSLLEYVQNM HPEEAEQTID NGDDSIMKLP SPRRNSTKKQ KYGRLVGRQS
PESITAKLTR VAEAAQQSED EKMMDDNDVT NIEDDEVLTQ VRYQDYDSLR NNEELLKKLG
ESEVQSELDK ENNTRSKSKT SRRSSRMTGK YSK
//