ID F4X2K9_ACREC Unreviewed; 937 AA.
AC F4X2K9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Tankyrase-1 {ECO:0000313|EMBL:EGI59334.1};
GN ORFNames=G5I_12539 {ECO:0000313|EMBL:EGI59334.1};
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:EGI59334.1}
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.
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DR EMBL; GL888584; EGI59334.1; -; Genomic_DNA.
DR AlphaFoldDB; F4X2K9; -.
DR STRING; 103372.F4X2K9; -.
DR eggNOG; ENOG502RPUM; Eukaryota.
DR InParanoid; F4X2K9; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR PANTHER; PTHR24171:SF8; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 48..80
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 132..164
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 165..197
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 262..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 104241 MW; E917FC2979C5F970 CRC64;
MQGICDNIRT AIEHGRTDII RSLLDACENG NTTEGITRDK ILNQPVLEEG TFLLYASKTN
QADIVRTLLN CGADPAVQNA DGHNAVDVAS SDAIRRIYIE EMLRATAASE VDRVVQLLDA
GLDVNSWDSQ GSKNTPLHWA ACYGNKHIIA CLLDKGADVN AENGCGATPL HDAVNRGDIA
ICQELLQAGA NPLVRAIKGT FAGKTPYELS RKKQSLHCFL QRFISNFMLN ENETIHSATM
SYPDTSYCQK SLTCNMSQLS VESNKSSDPA YDVPSRDAGK ESPSKSIIDK GSIYNLLWPQ
PKTVNELKNF TAPFIAGKEL LISIIQGSES VHKILDVWEI SRTHLLELGH DVKIGEVQPS
CGKLLNDNMI ECIVNRNLFN IADSYQLHIT HNSIKVSAGS LAGLHYAVCT FVQILRLSKN
QSRSEVCEIE PVFIKDEPRF THRGILLDIS PRGRVPILEY LLHIVDLLSS FKISHLHLYS
RLVQNCDWQL CYSKSEMVTL DRYCRDRHLD IVPTLDVDSN VSQHHLMQMW PIFQDLLAVF
PSLNYVHVGP RLTTLLVQAD SFDLSVSVND TLETDMSEVF KSYSCLQELW HILNLSSNTT
LLLCSNSLHS KSEFHNIPTN IIFVEYGFQA DYDFSEWTEP FRLGGGNVLP SSGTASYNSL
AGCPASTYAN TKNAIKTSLE QNSIGIIVAH WSGSHHLTPH PFAWIGYLIA AGLAWNSTTE
IDLGPDDNYD IPELSVSVRE RYITKLLDIH VFQDSEYKIG NAILELGRLD TLVLTLSKNQ
AVKDLQQIPD NHGSTLYRLL TDPDNVNLEY LSADLFAKMT KQIKRISHSL YEANLSSKFA
SMEIQELQLT SDLMLTACKI GRTLIGVGVN PNSNMGLAVI NLGVCNLPPT FRTDIANKML
AHIEQYKGSW LQRHFPQGLQ DSLLVLTSAL HRFVPAT
//