ID A0A0C7NC69_9SACH Unreviewed; 757 AA.
AC A0A0C7NC69;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=LALA0S07e04456g1_1 {ECO:0000313|EMBL:CEP63189.1};
GN ORFNames=LALA0_S07e04456g {ECO:0000313|EMBL:CEP63189.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP63189.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP63189.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP63189.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; LN736366; CEP63189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7NC69; -.
DR STRING; 1245769.A0A0C7NC69; -.
DR HOGENOM; CLU_368036_0_0_1; -.
DR OrthoDB; 2011339at2759; -.
DR Proteomes; UP000054304; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR46169; DNA REPLICATION-RELATED ELEMENT FACTOR, ISOFORM A; 1.
DR PANTHER; PTHR46169:SF15; DNA REPLICATION-RELATED ELEMENT FACTOR, ISOFORM A; 1.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR Pfam; PF02892; zf-BED; 1.
DR SMART; SM00614; ZnF_BED; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054304};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 69..98
FT /note="BED-type"
FT /evidence="ECO:0000259|Pfam:PF02892"
FT DOMAIN 640..719
FT /note="HAT C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF05699"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 86606 MW; FA3A5D7488BA248B CRC64;
MSNQVAISSK IQAQESASDY EAEAVNLRNG SKDDQHDVTT TESKSKESKW MARSGIRNHF
EISVQNGIKV ATCTHCGKTF QESKSTGNLV KHVKKLHPAE FNTRKTKEPK GRILDVFDLR
SSSTQLPEPL VFEMEHNPGA FTMVALVIEK LLPFSFVNAY ALKWLGDLLP EMSFFRSETA
VRDKLETYST WLDEGLITSL QGTGFVNLEL DVWTDGDERS YLSIFASFAP NLSDEQPNAL
GTEATHNKFN EPFQSHLLDL VDVSGSPQTA EYLYEITSSV IKKFKIVGKI RSITSDNGAS
NILRHSDMLC DLMKLSRPET SMKTKHLYHV NCARHILNAL LRTIGQTMKE NEKFHNGLQH
ITKLTRILKK SSLLRDSLAV AGLPEIPPAL ESSWVSVWDQ IAKYLDHYDA YLKWFESFQE
SSKHRNIAAR MAPHLQLSSE TREVLEYFVD CCSIFKYLHD SLQNETFNQL PNAISFYYTL
KEYFDLCSNA DVESIIPSSE GCFDFTFING KVGLSRMTKA IVLAAVRSAK PKFKEFFDMF
WNNEVYFVAA YLDPTSKLDC FSQLLVGSER EHQLQKVERY MKHYLAQCEP QTKQAPLPFS
QLQSQPKQNY RVFKIPRLDR REKKPLFRSV EPSVQMLEEW ENYKSDSQLS ADSITDVLEW
WQSRRLTYPN LFPLAVSMIY TQFSTSEMEQ KLSIDNKAMH KDRYNFASTD VRRVMILRSR
FYNLGLFGKY LETVLPSGAD QSSIILSDSS GSSSDEL
//
