ID A0A3F3PRM5_9EURO Unreviewed; 758 AA.
AC A0A3F3PRM5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=BDQ94DRAFT_161878 {ECO:0000313|EMBL:RDH29600.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH29600.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH29600.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH29600.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000256|ARBA:ARBA00005378}.
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DR EMBL; KZ852066; RDH29600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3PRM5; -.
DR STRING; 1341132.A0A3F3PRM5; -.
DR OrthoDB; 275853at2759; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0090618; P:DNA clamp unloading; IEA:UniProt.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; 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 InterPro; IPR005606; Sec20.
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 Pfam; PF03908; Sec20; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 227..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 436..575
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 338..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 46..73
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 354..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 84955 MW; D3E8630AB2F783B7 CRC64;
MASIADLQAR LKELSTALSH IQPLVSRLKG FTTAVGQGDQ PRLELGTEIH TRLKEAEEQL
ELLKVEVEAL EAAADTRRKG VDNEKESERE RVIALAGRLA DDLKRTRGDF RNAQLQAKRN
AEVARRKERE LLFTRSQSAE RKKQSSEKLT QDDIVMNASN DVTAALRRTH QLMQAELSRS
QFAQETLDQS TAALSSLSES YTDLDSLISS SRNLIGSLLR SQKSDTWYLE TAFYILVGTI
IWLVFRRILY GPLWWLVWLP LRLFARFTFA ILGAVGITSK AVQSSEPSTM LEYVPQETPM
VEQKVEPNIQ SAEGEAVWDQ VPVTDEAEED RLIDEIGKMV EESEEQEETN IDDISEEERQ
RQAELPRNPK KRMFEATDAR AAAAAANPSK PKPTDNKEEQ AKQQPWVEKY RPKTLDDVAA
QDHTTKVLQR TLQASNLPHM LFYGPPGTGK TSTILALAKS LFGPSLYRSR ILELNASDER
GIGIVREKIK NFARAQLTHS TGLGEEYLAQ YPCPPFKIII LDEADSMTQD AQSALRRTME
QYSRITRFCL VCNYVTRIIE PLASRCSKFR FKALDNTAAG ERLEHIAKVE NLRLEDGVVD
KLIACSEGDM RRAITYMQSA AKLVGAGRAG KKDEDEDEEM TDQESEVITV RTIEEIAGVV
PESVLDALVQ AMQPKKIGSS YEAVAKVVTD IIADGWSATQ LLLQLYRRVV FNDAIPDIQK
NKIVMVFSDM DRRLVDGADE HLSILDVALK ISGILGGA
//
