ID A0A158NLE3_ATTCE Unreviewed; 981 AA.
AC A0A158NLE3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=PR domain zinc finger protein 1 {ECO:0008006|Google:ProtNLM};
GN Name=105621494 {ECO:0000313|EnsemblMetazoa:XP_012058351.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012058351.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012058351.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; ADTU01019339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012058351.1; XM_012202961.1.
DR AlphaFoldDB; A0A158NLE3; -.
DR STRING; 12957.A0A158NLE3; -.
DR EnsemblMetazoa; XM_012202961.1; XP_012058351.1; LOC105621494.
DR GeneID; 105621494; -.
DR KEGG; acep:105621494; -.
DR eggNOG; KOG2461; Eukaryota.
DR InParanoid; A0A158NLE3; -.
DR OrthoDB; 2880949at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd19187; PR-SET_PRDM1; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR044413; PRDM1_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR16515:SF26; PR DOMAIN ZINC FINGER PROTEIN 1; 1.
DR Pfam; PF21549; PRDM2_PR; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 43..159
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 763..790
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 791..818
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 819..846
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 847..874
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 209..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 107787 MW; F224C7B275FA901C CRC64;
MEASEWDHAT LREEEFEQHA VYLVPDVSAS PGDTNRAESS LPRNLVLKPS QALNDVLGVW
STSYIPKGTR FGPLVGQVYT KDSVPADANR KYFWRVYKNN ELFYYIDGYD VQKSNWMRYV
NPAYSSESQN LIACQYKMNI YFYTIKPILP HQELLVWYCR EFAERLNYPL TGELMLQRIR
QQVQQSTLPT EISPAVDVIS PLKDPAIYER RQMTPTDGSV RSDEGYHSNG YHDEILTPPE
ESSESDSENN YVLDFSKNAK SSVCNDEILK QDNTAVKNEY RKVKIKISKT YGNFQATKGI
TDGPKDKEQE LSSRAVTPEL QKPVSPVILQ KSTVLSTVTE DEISEKNMKP FYEPEVKGGN
LPMSGRSAYI ANPSSSILEN ILLRNSTDNN NNSHNHHHNG GSQQHHQHHQ LHHQTHVDSV
TPPPSSPTEM AYSYKKSHRY GNILPCSPDS SSNLPLQTDS CVNSTSSNGG TLSSMQSPTG
NLHSSTGGLH SSTGGNNGSL PPHPGSLHSS SNAGGGIHSS TSVLSSNAML TSTSPHSAST
TANGCLPKRK TKSPSPSSSQ NGVSTPTTIL YSGSSGAAGC QIESASPVYP NSAGSSNSST
SSNQSISPIS PIQSPSSYSP YGSLYGHQNS SLHHNMSSSL SINCTAYSPT PSSNVVYERT
TDGRRLEATS SGGHQLPTSS TMQIDGNQAL ITGTHNLHLG HHPGLTIHPN SSSSLNRYSP
ASSLSPDDHG CSQSGSLSPN SQGSRGYRSL PYPLKKKDGK MHYECNVCCK TFGQLSNLKV
HLRTHSGERP FKCNVCTKSF TQLAHLQKHH LVHTGEKPHQ CEICKKRFSS TSNLKTHLRL
HSGQKPYACD LCPAKFTQFV HLKLHKRLHT NERPYTCQGC DKKYISASGL RTHWKTTSCR
PNNIEDELAL AAAVGSPTYY EYGPDMNVGN MPKECELEHI DNYDRHGSTH GPHSTSLHNL
ENSVGRPSVI ETSQPHIIEC T
//
