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Database: UniProt
Entry: A0A109FCQ9_9BASI
LinkDB: A0A109FCQ9_9BASI
Original site: A0A109FCQ9_9BASI 
ID   A0A109FCQ9_9BASI        Unreviewed;       915 AA.
AC   A0A109FCQ9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KWU42084.1};
GN   ORFNames=RHOSPDRAFT_21828 {ECO:0000313|EMBL:KWU42084.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU42084.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU42084.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU42084.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; KQ954516; KWU42084.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FCQ9; -.
DR   STRING; 1305733.A0A109FCQ9; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000062823; 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:KWU42084.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          3..153
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          880..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          412..446
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          477..545
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        893..915
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   915 AA;  101225 MW;  1CFCE839864A80D8 CRC64;
     MDPSKLTEAA AGSLQAAVQL AKDNQQGVVA PAHLFSALLD PATNETGRSQ QTLLHSILNK
     AGAQPELVQR GLAKFIVRLP SQEPPPDDVS LSPALAKVLR EAEKLMKEKN DSFVAQDHLI
     LACVQDPSIL NILKEAGTTP EAIKTAAQQV RGGKQVNSRG AEEGFEALKK YAKDMTAEAE
     EGRLDPVIGR DAEIRRCIRI LSRRTKNNPV LIGEPGTGKT AVVEGLAQRI INRDVPPNLL
     CRLWSLDFGA LHAGAKYKGE FEERMKAVIE ECENVESNVV LFIDELHSLV AGQGATGGGI
     DAANLLKPAM ARGKIRVIGA TTLAEYRQYI EKDAALERRF QQVLVNEPSV PETISILRGI
     KEKYEVHHGV TILDSALVAA ATLAHRYLTA RKLPDAAIDC VDEACSAVRI ARESQPEEID
     QLERQKLQLE IELHALQGEL KRDKNDEVAK QKIEECKQAI SRIDDQLAPI KARFEAEKAK
     SDELNHVRKR IDELTAKAAD AERRYDLATA ADLRHYAIPE LHSRLQQLEQ QKKDEERQLR
     AEGGESLAGD TVTAEAIQQV VAQWSGIPVS NMKMTEKQKL LKMEKTLRKE VVGQDEAVSA
     VANAIRLNRS GLSNQDRPIA SFLFVGPSGT GKTQLAKALA KFLFDSPDAM LRIDASEYSE
     KHAISRLIGA PPGYVGFEDS AQLTEYIRRK PYSVILIDEI EKAAREFHQL FLQVLDDGRL
     TDSHGRVVNF KNTVIIMTSN IGASYLNDLP DDAETIPKET RELINSALRT TLPIEFVNRI
     DSITLFNRLT RADVRGIVAI RIAEVQKRLR ANGRDITLQL SDAALDYLGS VGYSPIFGAR
     PLNREIQTSL LNPLSKMILE ECIRDGETAR VDFDAPRNRL VVTPNHEPTV QMEQDDDDLD
     DDMDEDDVAI EEVDE
//
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