ID A0A158NY43_ATTCE Unreviewed; 924 AA.
AC A0A158NY43;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS50157};
GN Name=105625740 {ECO:0000313|EnsemblMetazoa:XP_012062451.1};
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_012062451.1, 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_012062451.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
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DR EMBL; ADTU01003135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01003136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012062451.1; XM_012207061.1.
DR AlphaFoldDB; A0A158NY43; -.
DR EnsemblMetazoa; XM_012207061.1; XP_012062451.1; LOC105625740.
DR GeneID; 105625740; -.
DR KEGG; acep:105625740; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; A0A158NY43; -.
DR OrthoDB; 3291719at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24406:SF8; C2H2-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24406; TRANSCRIPTIONAL REPRESSOR CTCFL-RELATED; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
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 563..585
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 641..668
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 744..771
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 782..809
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 834..861
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 902..924
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 179..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 104921 MW; EDE554A924CF1DF9 CRC64;
MNADGRIAQN LDLCDGSKDR KAIPGDINKK SKLDTSSLEI ACDTGQIILD TISISDNDSS
PKLKKNAKNG EERTESKVYL GPIRARLLPA RRGRNIERRK ASTKRWVERK KALLAAIGED
VSDTDSIASD EMQLSPVQKA RAKDKEIERQ RKIAKVLKNL ETNLTEKYVL RDKNIDSDAR
RTRSTLQHNN KNTVKNLLNQ NNKKNTVGRN RSSVDSSIEN SPSLLTNNFT LNDEKKFEIQ
DDDQTFEPSS LKSELVIGDT TFCITSTLIL VNGNNEQAEC NNSTKDSKSF SPDESNRERN
TDIFDAVQLR RVNPVITTTS QKNNKPNNKF IERCLNIEVE GNELSVLKRV QRELADFVQK
EIKYKLFSTN DDDAKINKTD STQTESATFF REKLDQKLKD IIEKAIKKNI VLSEGNTSDA
YSSSPKVSML AKSPRYQPKV MVKRLDIAKE SKHYKINNAC TLNMSSSKRK LAGPFITRNK
RASIIPVRYG EYASLDSSDS EATNNNSIED PNEWYPTSKT TNSKTKTTPR QIIIGKSVEK
KQNEQKTGSE KIVKTANTKV ENHICGVCGS MFHSRTEVEA HVRTHQLAPG ASVVQVVLQN
KEIVPQQIKP QQIKQKMMRC KRCHEIVEAR FVKVHVCKTY HKCHICNSMF RAKNLLLKHL
ENHDTKFKLN VIENKKLNNT DTLQKIVAIT SVMPQKAQNQ AQGSETMIKT EIKNEKNDIQ
SDKITSTGVK LESTENVTKP KETYTCFVCD KIFTDEEVLK DHLQKHCDDE SEGEQNNSKE
QYQCAICGST LESDQALEEH VGKHLFDDED DNPNLISINQ GNENESKLKA NDSYQCGQCS
EMFDSEVLLE MHMHAHLEEV AIAEWEQQGL KIYQYQCMLC DELCNTEKEL SEHLDIHNAN
AHVCQLCDKP FRTLEDLQEH VATH
//
