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Database: UniProt
Entry: E2ALJ9_CAMFO
LinkDB: E2ALJ9_CAMFO
Original site: E2ALJ9_CAMFO 
ID   E2ALJ9_CAMFO            Unreviewed;       440 AA.
AC   E2ALJ9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=26S protease regulatory subunit 4 {ECO:0000313|EMBL:EFN65701.1};
GN   ORFNames=EAG_10958 {ECO:0000313|EMBL:EFN65701.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN65701.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR   EMBL; GL440609; EFN65701.1; -; Genomic_DNA.
DR   RefSeq; XP_011260462.1; XM_011262160.2.
DR   AlphaFoldDB; E2ALJ9; -.
DR   STRING; 104421.E2ALJ9; -.
DR   EnsemblMetazoa; XM_011262160.3; XP_011260462.1; LOC105253839.
DR   GeneID; 105253839; -.
DR   KEGG; cfo:105253839; -.
DR   InParanoid; E2ALJ9; -.
DR   OMA; QDDTDPM; -.
DR   OrthoDB; 1707207at2759; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19502; RecA-like_PAN_like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR   PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR23073:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Hydrolase {ECO:0000313|EMBL:EFN65701.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:EFN65701.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311}.
FT   DOMAIN          218..357
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  49232 MW;  D110C0BBB8F3E7C1 CRC64;
     MGQNQSGSGG SGGDKKDDKD KKKKYEPPIP TRVGKKKRRT KGPDAALKLP QVTPHTRCRL
     KLLKLERIKD YLLMEEEFIR NQERLKPQEE KNEEERSKVD DLRGTPMSVG TLEEIIDDNH
     AIVSTSVGSE HYVSILSFVD KDQLEPGCSV LLNHKVHAVV GVLGDDTDPM VTVMKLEKAP
     QETYTDIGGL DTQIQEIKES VELPLTHPEY YEEMGIKPPK GVILYGPPGT GKTLLAKAVA
     NQTSATFLRV VGSELIQKYL GDGPKLVREL FRVAEEHAPS IVFIDEIDAV GTKRYDSNSG
     GEREIQRTML ELLNQLDGFD SRGDVKVVMA TNRIETLDPA LIRPGRIDRK IEFPLPDEKT
     KRRIFNIHTS RMTLAPDVNL AELIMAKDDL SGADIKAICT EAGLMALRER RMKVTSDDFK
     KSKESVLYRK KEGSPEGLYL
//
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