ID F4WCL6_ACREC Unreviewed; 845 AA.
AC F4WCL6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Peregrin {ECO:0000313|EMBL:EGI68196.1};
GN ORFNames=G5I_03292 {ECO:0000313|EMBL:EGI68196.1};
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:EGI68196.1}
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GL888070; EGI68196.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WCL6; -.
DR STRING; 103372.F4WCL6; -.
DR eggNOG; KOG0955; Eukaryota.
DR InParanoid; F4WCL6; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15670; ePHD_BRPF; 1.
DR CDD; cd15572; PHD_BRPF; 1.
DR CDD; cd05839; PWWP_BRPF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_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; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 199..249
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 253..373
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 538..593
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 722..794
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 95348 MW; 49A7F13E51F5A837 CRC64;
MNTPQSNKKN KKIGRNRIGI PNESASPTNT ETLSSQEAAK YVLVNPIGED GNKSIKLAIL
DAIPIISMDS NMFDEKMQKS NTASLEKEKE DKNNLNTLPT AFVKPIEGYE NQLGEAKPLP
NSYIRFMERS GEELDGEVEY DLDEEDNAWL SIVNERRLAS GLTPPLEPDT FELLMDRLEK
ESYFQQQTNG GGGIAADEDA VCCICMDGEC QNSNAILFCD MCNLAVHQDC YGVPYIPEGQ
WLCRRCLQSP SRAVDCILCP NRGGAFKQTD RPATWAHVVC ALWVPEVRFA NTVFLEPIDS
IESIPQARWK LMCYICKRKG AGACIQCHKS NCYSAFHVTC AQQAGLCMRM RTVQPTNGEP
MLVQKTAFCE THTPADYQPS TNPVDARRRA IANKKSTSAP VISIPTIPPE RIREIASLAE
GIPKRSQLIQ RLIAYWTLKR QYRNGVPLLR RLQSSHPQSR PPPLGEHPSS PTHDGELRGE
LYRHLKYWQC LRQDLERARL LFVLNQCPRD QLQRKEKCLW LQLRPFESVL RTLLEAIKAK
DTNDVFGQPV NIKEVPDYLE IVSHPMDLST MQAKLEKHEY HTLSALETDF NLMTRKDFPE
VNPVSEPEQI GSKSRKRERS NRNRVETESQ SNEKEIGGGV NRRTAVLFTR KARARNAKSS
QMSGTMDSDV GEGESQSSSC SSCPTSRSTS PDPEEQKQRQ ETIDTKKENE TKQTNTGSGL
EALQLVWAKC RGYPWYPALI IDPNTPRGTI HKGVPIPAPP DDVLALADNY KEPVFLVLFF
DTKRTWQWLP GEKLEKLGVS HEVDEAKLIE SRKPTDRKAV KKAYQEALHY RKQTHNAVVD
STSTG
//
