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Database: UniProt
Entry: A0A367JC70_RHIAZ
LinkDB: A0A367JC70_RHIAZ
Original site: A0A367JC70_RHIAZ 
ID   A0A367JC70_RHIAZ        Unreviewed;       892 AA.
AC   A0A367JC70;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN   ORFNames=CU097_007651 {ECO:0000313|EMBL:RCH87485.1};
OS   Rhizopus azygosporus (Rhizopus microsporus var. azygosporus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=86630 {ECO:0000313|EMBL:RCH87485.1, ECO:0000313|Proteomes:UP000252139};
RN   [1] {ECO:0000313|EMBL:RCH87485.1, ECO:0000313|Proteomes:UP000252139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 357.93 {ECO:0000313|EMBL:RCH87485.1,
RC   ECO:0000313|Proteomes:UP000252139};
RX   PubMed=29674435; DOI=10.1534/g3.118.200235;
RA   Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA   Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA   Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA   Heitman J., Vilgalys R., Stajich J.E.;
RT   "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL   G3 (Bethesda) 8:2007-2018(2018).
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:RCH87485.1}.
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DR   EMBL; PJQL01001647; RCH87485.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367JC70; -.
DR   STRING; 86630.A0A367JC70; -.
DR   Proteomes; UP000252139; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252139};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          411..526
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   892 AA;  100289 MW;  6AE0AB7FEBACCCAD CRC64;
     MSGMNFTEKV EKIIARAQAL TREFGNSQIM PAHIACAMFD ETDGAALFRS IIEKTGAEPT
     TVERGYKKMM VQLPSQDPAP TDVTIGSQTS KLLRNAEKRM KDQKDTYISV DHIILALSDD
     DTTFKPMKDA GITKKALEAA VSQVRGNRRV DSKNAEEVYE ALSKYAIDLT QMAQNGKLDP
     VIGRDDEIRR VIRVLARRTK NNPVLIGEPG VGKTAIVEGL ARRIIERDVP QSLQCKLFSL
     DMGALIAGAK YRGEFEERLK AVLKEVKESE EGIILFIDEI HTVLGAGKGE GSMDAANLLK
     PMLARGELRC IGATTLTEYR EIEKDPAFER RFQKVDVGEP SVAATISILR GLKERYENYH
     GVKITDSALV SAAQLSDRYI TTRFLPDKAI DLIDEAAANT RVQLDSRPEE IDVLERKRFQ
     LEIEVKALSK EKNNKESNER LQAVREEMAR IDEELKPLKL KYELTKGRLD EIRDLKQKLD
     ELKSKAIQAR NNYDLDTAAD IEYYAIPDVE QRIAELQAEK QRKMSEDLAN DQPSDAIISE
     VVRPEQIMEV VSRWTGIPVQ NLAKSEREKL LTMETEIARH VVGQDAAIKA VCDAIRLSKA
     GLQDPRRPLA SFMFLGPTGV GKTLLCKTLA EFLFNDERAL IRIDMSELME QHSVAKLIGA
     PPGYVGHEEG GLFESVRRKP YSVVLLDELE KAHRDVANVL LQVLDEGFIH DSKGRRIDFR
     NTIIVMTSNL GANLLADNVK GEEMNILKEK IMEVVRKHFS PEFTNRIDEV VIFNRLTQTN
     ITNIVDVRLK EIEERLADRR ITLQVSQAAK EWLGAHGYEP IFGARPLNRL IQQKVLNQLA
     KLIIDGGIRN NEVAKVDISA DGSTIEIVRN HESEAGYVVE EPMDEDQDLD MD
//
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