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Database: UniProt
Entry: A0A232F328_9HYME
LinkDB: A0A232F328_9HYME
Original site: A0A232F328_9HYME 
ID   A0A232F328_9HYME        Unreviewed;       367 AA.
AC   A0A232F328;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=TSAR_016418 {ECO:0000313|EMBL:OXU24863.1};
OS   Trichomalopsis sarcophagae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC   Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX   NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU24863.1, ECO:0000313|Proteomes:UP000215335};
RN   [1] {ECO:0000313|EMBL:OXU24863.1, ECO:0000313|Proteomes:UP000215335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alberta {ECO:0000313|EMBL:OXU24863.1,
RC   ECO:0000313|Proteomes:UP000215335};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXU24863.1};
RX   PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA   Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT   "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL   Curr. Biol. 27:2007-2013(2017).
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000256|ARBA:ARBA00005378}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXU24863.1}.
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DR   EMBL; NNAY01001176; OXU24863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A232F328; -.
DR   STRING; 543379.A0A232F328; -.
DR   Proteomes; UP000215335; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18140; HLD_clamp_RFC; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013748; Rep_factorC_C.
DR   InterPro; IPR047854; RFC_lid.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   PANTHER; PTHR11669:SF20; REPLICATION FACTOR C SUBUNIT 4; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215335}.
FT   DOMAIN          65..206
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  40977 MW;  A4B325C8C2778E51 CRC64;
     MHAFLKTGKL GAADAKKPST SKGKESNARA KATPWVEKYR PKTVEDVVEQ GEVVEVLRQC
     LSGGDFPNLL LYGPPGTGKT STILAAARQL FGSMFKERIL ELNASDERGI QVVREKVKKF
     AQLTAGNTRP EYVYSDCFAS GKPCPPFKII ILDEADSMTD AAQSALRRTM EKESQTTRFC
     LICNYVSRII EPLTSRCTKF RFKPLGEEKI IERLEYICGE EDLKAEKSVL KLVVDASGGD
     LRRAITCLQS VTRLKGIGIE VTNNDVLEVT GVVPTKWLDD LLRVCETKNY NEVEAYVDKF
     MLEAYSASQV VDQLNDIVIY SNTLTDKQKA YIGEKLGECS YRLLEGGSEY VQFMSLCCGI
     MQAYELR
//
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