ID A0A2G4T8B5_RHIZD Unreviewed; 586 AA.
AC A0A2G4T8B5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PHZ17264.1};
GN ORFNames=RHIMIDRAFT_243360 {ECO:0000313|EMBL:PHZ17264.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ17264.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ17264.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ17264.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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DR EMBL; KZ303842; PHZ17264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4T8B5; -.
DR STRING; 1340429.A0A2G4T8B5; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000242254; 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; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF93; CASEINOLYTIC PEPTIDASE B PROTEIN HOMOLOG; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000242254}.
FT REPEAT 48..80
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 126..158
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 254..394
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 470..562
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 586 AA; 67039 MW; A5E9F3A4D31EF493 CRC64;
MTHKEVFALE ENEPTGDAIC QAIVQNDMRA LKRLADHPNF NPNIYHRYGW TPLQVAVIQD
NEQMVKLLLE KGAGIDYIMN GVIGLNHSPI RVDPNLQDQY YPRSHQAANT RQVEFSEDLL
PYRDYREYTA LHYAVIICNP QIVKLLLDHM ADPFARNSHG LTAREYLYYV ERYTGEQNLE
IEDMLYKKEA SYPKDKAEHE ERMRKAQLQK EKEYRKKHPL EDALKTRIVG QLGPIYALAS
AIRRKQNGWH DEEHPLVFLF CGSSGVGKTE LAKALAQNLH GKQIDKGFIR IDMSEFQHKH
DVSRFIGSPP GYVGYDEGGQ LTEKLKECPN AVVLLDEVEK AHPDVLTIML QLFDEGRITD
GKGTTVECKD AIFIMTSNLA QHEIADEAEL LRLEASVSSD AQTKGVATVT STDPAPEKNL
SDLQEEQLKH GQISLSRRFI EHTIYPILYQ HFKRDEFLGR INEVLFFLPF SDDELKEITS
RELSKWAEKA RKRHGITMTW DADVVDVLAQ GYNIRYGARS IKYEVERKVV NLIAKAHEND
EVLDGGRVHI VVDKSIDKKA RICKIEIPER GGDDKKKSGG WFSSKI
//
