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Database: UniProt
Entry: A0A5C5FUC4_9BASI
LinkDB: A0A5C5FUC4_9BASI
Original site: A0A5C5FUC4_9BASI 
ID   A0A5C5FUC4_9BASI        Unreviewed;       913 AA.
AC   A0A5C5FUC4;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:TNY19584.1};
GN   ORFNames=DMC30DRAFT_378773 {ECO:0000313|EMBL:TNY19584.1};
OS   Rhodotorula diobovata.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5288 {ECO:0000313|EMBL:TNY19584.1, ECO:0000313|Proteomes:UP000311382};
RN   [1] {ECO:0000313|EMBL:TNY19584.1, ECO:0000313|Proteomes:UP000311382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-FST 08-225 {ECO:0000313|EMBL:TNY19584.1,
RC   ECO:0000313|Proteomes:UP000311382};
RA   Fakankun I.U., Fristensky B., Levin D.B.;
RT   "Rhodosporidium diobovatum UCD-FST 08-225 genome sequencing, assembly, and
RT   annotation.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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:TNY19584.1}.
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DR   EMBL; SOZI01000091; TNY19584.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C5FUC4; -.
DR   STRING; 5288.A0A5C5FUC4; -.
DR   Proteomes; UP000311382; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:TNY19584.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000311382};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          886..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          418..544
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        890..913
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   913 AA;  100464 MW;  46BFDDF58FFB5F4F CRC64;
     MDKLTEASAQ ALQQAVELAK ENAHPQVAPV HLFSALLSPT TSATGQTQQT LLHSILNKAG
     AQPELVQRGL AKYIVRLPSQ EPPPDDVSLT PASAKVLKEA ERIMKDKGDS FVAQDHLILG
     CIQDPSIVSI LKEAGTTPDA VKKAAQQVRG GKKVDSKGAD ADGFEALKKY AKDLTAEAEA
     GRLDPVIGRD DVIRRCIRIL SRRTKNNPVL IGEPGVGKTA VAEGLAQRIV DRDVPPNLLG
     RLWSLDMGAL MAGASYKGQY EERIKSVLDE CEKSETGVIL FIDEVHLLMA GQGSSGGGMD
     AANLLKPAMA RGKIRVIAAT TLNEYRQYIE KDAAFERRFQ QVIVNEPTVP ESISILRGIK
     EKYEVHHGVT ILDSALVAAA TLAHRYLTSR RLPDSAIDCI DEACSAVRIA RESAPEDVDR
     LERAKLQLEI EMHALQGELA RDKKDEVAKA KIEEVKQAIA KIEDELAPIK ARFEAEKAKT
     EELNRVRKRI DELTAKAADA ERKYDLATAA DLRHYAIPEL NNRLAKLEEE KKAEERQLRA
     EGGEALAGDT VTPEAIQAVV SQWSGIPVSN MKTTEKQKLL RMEKSLRKEV VGQDEAVSAV
     ADAIRLNRSG LSNQDRPIAS FLFVGPTGTG KTLLAKALAK FLFDSSDAML RIDASEYSEK
     HAISRLIGSP PGYVGHESGG QLTEYIRRKP YSVVLIDEIE KAAREFHQLF LQVLDDGRLT
     DSQGRVVNFK NTVIIMTSNI GASYLNELPD EVETIPPETR EQVHTALRTA LPVEFVNRVD
     SIILYERLSR KNVRNIVDIR IGEVQQRLRK NGRDIKLEAT PAALDFLASV GYHPLFGARP
     LNRAIQTELL NPLSRYILNE SIRDGETARI DCDAKANRLV VVPNHEPSVP IDEDDDDTDA
     EMADGDVEVE ELD
//
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