ID A0A151IM67_9HYME Unreviewed; 1244 AA.
AC A0A151IM67;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 03-MAY-2023, entry version 23.
DE SubName: Full=ATPase family AAA domain-containing protein 2 {ECO:0000313|EMBL:KYN05963.1};
DE Flags: Fragment;
GN ORFNames=ALC62_03056 {ECO:0000313|EMBL:KYN05963.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN05963.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN05963.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN05963.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN05963.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
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DR EMBL; KQ977063; KYN05963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151IM67; -.
DR STRING; 456900.A0A151IM67; -.
DR Proteomes; UP000078542; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd05528; Bromo_AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR045199; ATAD2-like.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23069; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23069:SF0; TAT-BINDING HOMOLOG 7; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Reference proteome {ECO:0000313|Proteomes:UP000078542}.
FT DOMAIN 873..943
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 39..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KYN05963.1"
SQ SEQUENCE 1244 AA; 142730 MW; 5740D4CCE244925C CRC64;
IMLDDDAALD SMDTEEEIFS PRNHSLDSNV RRPKSLRKLR SHSGSNSHIT RNNLSVRRST
RNRMQTYDNL NTSWILGTQT LKGYPMFQQH PSSSDKEMVD DVPGRKRDVR DRMPLKSREN
HPPNKTPTRH LRDRTEHDRQ NSRELRTQFD VECFYITRKS DSPNRFREGP VTRLCGNVVE
KTEKPKVEQE EADDVSSHES EKPDNNDNSE NEDGFEDMYT RIKRTRRTTQ RQLPRVVDSD
LSESSDSPGP RKYSLRQKKP TVDRFQANVE PVRRSIRALR SVLSNSMRRR KHRSKSTSSA
DSSDSEPQRY DKKKVKKARQ SAIPQGGPPD RKADINPITL DTNIRFNDVG GLETHIHCLK
EMVIFPMMYP DVFERYDVTP PKGVLFHGPP GTGKTLIARA LANECSQGNK KMAFFMRKGA
DCLSKWVGES ERQLRLLFEQ AQQMKPSIIF FDEIDGLAPV RSTKQDQIHA SIVSTLLALM
DGLSDRGQVI VIGATNRIDA IDPALRRPGR FDRELFFPLP AMKERLEILK IHVSKWKNPP
SDQLLEILAE KATGYCGSDL RALCTEAVLQ GLRRTYPQIY MTNDRLLLDP ERVEVKKRDF
MQANAMLIPS SHRVAPCAGR KLQPFMEPLL APPLKELLNL IRGIFPQGVN PAMAKMRNAK
GIHRPRLLIS GGSLSEGQGP HLAQALLYCM EHLPVQILDV STLFAESARS PEETCVQVFN
EAVRNVPSII YIRSINQWWP LVPETVKAVF LCRIAALDPS LPILILATSD ATYQDLPNQL
KSLFSELRGE VYSMKTPTTE QRKKFFRPIF VIQSLRQPQI KSNKIEVLET LPLAPDPLPK
KLTEEEKQIM YEKDEISLRE LRIFLREICA KLARNRQFFM FTKPVDTEEV PDYNLIIKQP
MDLETMMTKI DMNCYLCARE FLDDIDLICR NALEYNPDRD PADKLIRHRA CSLRDNAYAL
IKAELDSDFE DKCREISKTR RILESNCDNE RNKNSKLESS STNERTEKKE SINSSHSLVV
NGKKFGSSRK RKIPAWARGY VKKVHKKRKI AFGENATETV ANKSVNNETT TSIDLEKFQE
FETEANNVLN GHMGLFDNTD SENDSQNENS KGSQNCTATD QRIDNLDQME ICFIEEEKPI
GNGDSSSSSR RESMDELSFA IESDTSRDKI EENEKIVVDK SELDNAWHFT VEITKDFPVE
VLCDIYVQLS RCIGKYAQKY DRKSLPKDLL KEVEKFTEYK SQRQ
//
