ID F4WN55_ACREC Unreviewed; 801 AA.
AC F4WN55;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Zinc finger protein Xfin {ECO:0000313|EMBL:EGI64324.1};
GN ORFNames=G5I_07202 {ECO:0000313|EMBL:EGI64324.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI64324.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL888235; EGI64324.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WN55; -.
DR EnsemblMetazoa; XM_011057981.1; XP_011056283.1; LOC105147154.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; F4WN55; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1800.20; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24377:SF995; FI01202P-RELATED; 1.
DR PANTHER; PTHR24377; IP01015P-RELATED; 1.
DR Pfam; PF07776; zf-AD; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR Pfam; PF13912; zf-C2H2_6; 2.
DR SMART; SM00868; zf-AD; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS51915; ZAD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01263};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01263};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 4..79
FT /note="ZAD"
FT /evidence="ECO:0000259|PROSITE:PS51915"
FT DOMAIN 279..307
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 314..342
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 347..374
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 407..434
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 434..461
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 525..552
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 554..581
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 659..686
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 772..800
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT COILED 468..495
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
SQ SEQUENCE 801 AA; 92144 MW; 3C0056DEAF0BEA67 CRC64;
MWDKVCRLCS EERNEMLPIF GDEGLQRRVV QKLRACLPVL VYKSDPLPKQ ICQFCAARLD
DVYQFREFCI NVYRSMHAML LKCEQMESAQ IFLDAMMNSS DPCQVQLCKE KSRAPPPLVP
LSIVMPFDDP TTPINQVNQD HFQNTCMETL SELPCEVEIK EMNTDPIFNA ETATCEPLNK
KRKLSNIFDM DIQTKVESVL IADIEGAKAP KSNCQTKKEE KRTSILEQVL TGNLTMNNHQ
KLQPGTKLTS EWWCAPCNSY YKTKDSLMTH MQLHCPRVYT CRKCSESFES VEILAKHEAN
SHLKVKMDFT ENLNDCDQCD RQFVRWEMLK QHRLRDHLAE LTDGSNTRCS LCNRFFPTVE
SYQKHVQLHQ TNSAMSQKLP SSEFMVTKIP ERIREIKRDE QCCERSLKCP TCGKICTQQS
ALSNHMRTHE PKKHKCDICG RSFGLFIRLA GHRIAEHNEQ PMMSPVLSAV EQEEALNAER
EAREAREAKS RSIKKSYSEI MEKNDIPVDN ESVTKRISGG NKNVARCGIC SQWFSDHTTM
LTHLQTHSES HKSYTCNICK KSFKEQSQLL KHEASHKRQT LDNASLYTSA VYNKSLVDKA
QQKTHTVAKT YHCAKCNKIF FKEVSLLAHI CRDTAQLEKK IAEKKSRLKT SLHVGNKTHK
CSKCDATFAS SQSRNAHMKM HAEYMRGSTT QTHEIKVEAD DEPMPKLRPE TLEYISPIEP
KVEINEQGTP PPLKRTLIKT SNGYRCGVCQ SPFVLRELAV AHLRSAHPVM PYQCPYCKKR
FTTQYTFAHH IKTEHPDEPE K
//
