ID A0A0C7N7I2_9SACH Unreviewed; 1468 AA.
AC A0A0C7N7I2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=LALA0S05e06744g1_1 {ECO:0000313|EMBL:CEP62487.1};
GN ORFNames=LALA0_S05e06744g {ECO:0000313|EMBL:CEP62487.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP62487.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP62487.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP62487.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LN736364; CEP62487.1; -; Genomic_DNA.
DR STRING; 1245769.A0A0C7N7I2; -.
DR HOGENOM; CLU_250352_0_0_1; -.
DR OrthoDB; 2734339at2759; -.
DR Proteomes; UP000054304; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16100; ARID; 1.
DR CDD; cd15518; PHD_Ecm5p_Lid2p_like; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF113; PROTEIN JUMONJI; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 4: Predicted;
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};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 186..284
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 497..714
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1468 AA; 167225 MW; A28CCA5C6BD8ADF5 CRC64;
MTLPKLPEQS QNQKLPSNGD PDASKLPPLG KWNIPSKTTS MSNSQNIPTI PKTSRFQKLR
EHRSCPSLSV EKGLEKLYEI PHVETRKIEW IGKSATISET YTTKSGWQYI LKEGSVPCFE
MLRSELPDPL VFYEEVEPIG RHFGAVVLQV IEGPHRSQER SVTALDPNRL QFKARKQSLR
PIHVERQRKL DFYRKLYQYH SMRGDNIMDS NSQKIPSIDR RPLDLYRLRQ CVLLRGGYQA
VCSKKGWAQI GRELGYSKTA STSLLATLRS TYTKILADFD EHTLRAETTE NVIQQKIYSK
LQIVLPSSIT CEATDEKRKK KRAVPSTIIA DNSSKRQKIT KPKVYQVIGI GTEYSRLRDV
LQHKGFVTKF ESLTDRKKHI TKPSVSTLPN YDYSFWKNTT GIYDRSTYEA LDSPLYSLTQ
FSEKSHLHSK QVFDRCEQRL PHALSNYQKM DVDKFERLFY QVLSDIDVPC DVDCAVDLPS
RIYGSAFPKF SGEKNDTFAS NSWSLNSLPL SSKSALCFLN ADYGDHVSSR MDIGMLFSVK
GWAVEDNFLP AVDYNHVGSS KLWYIVSPQD LEKFEQLTFV SKQKVASSSI TTDAIKDTNF
RESAFYQCFD GTTQAESFSS ILPRIKTHSF SLPPGNNSES AFNQLSDDIL LHPEVLEANH
IKVRKVIQNP GSYIFKFPKT YSMNIHSGFS VSENVRFAPV SWLDYVMDSE LWLAKHGILS
TVNPFQLLHN IVSESRDKNL VLKARNILLP LIIDELNARD RLSRMSKNLI VCPNTFDFIS
DLDFSSTGAS KVLLANADDC VTLSLKQFLL NSSVRDGKLH YLGQNVENNL TCVSLHLLFL
NEDLDSLLQQ DRARKKAVQS FPGHENGGSK EEKTQILNAY VAQIITNGKR IGFEEINMYN
EALSQYDDLV SSNLKKTICE INIARSKCVR FLKGVETESH KPGPSSSHLR FSLPEIRVPE
FWHSATELFR LQREIQVLPV EFPEMHDIFN LCRKVKKYQT LCETAIQKND MKLVHDAYQS
GFSLGVSSRF QKLVAKKIGE TLWLEEYETI FSKRNRFHTH GTMTGGLEDL PLFLEFGLRY
VRKDEHLEKF REVKRAIISA QKVLHNVKSL FKKKNSKIPV ERLQELFSEM TENQNLVNPR
LSEVIKAVLD AFEGSKQSCA MAFARLNTND RFLSQLTTGA TVEALFDSGI MENFDGSAGD
KRLTQQEVPN RSIFSKHIKD CKAWLHALFS TVPKRQSWTK VVQATEQCFG TEAETRQGPT
IGTSDKDESY CFCRRGDFGS TMVACEICGE WYHMTCINKG KWSLGDTESS VFACPICCAH
DVPGLNVIHY DDLQKIVMES CRLKIIPDRH VLLEVFEIFK LATQFKRNLR ISVFNVNGTL
RSDVPLLQLK FYLRKLMGSG VKLESEEQVL RNACREHDVA RLRSFAEKGI NVVTGLEISK
DKPSNNIAIP SEKPTEQIKA SEETKVDV
//
