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Database: UniProt
Entry: I1BV93_RHIO9
LinkDB: I1BV93_RHIO9
Original site: I1BV93_RHIO9 
ID   I1BV93_RHIO9            Unreviewed;       645 AA.
AC   I1BV93;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=RO3G_04828 {ECO:0000313|EMBL:EIE80123.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE80123.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE80123.1, ECO:0000313|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000313|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000256|ARBA:ARBA00010044}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC       family. {ECO:0000256|ARBA:ARBA00010550}.
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DR   EMBL; CH476734; EIE80123.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1BV93; -.
DR   STRING; 246409.I1BV93; -.
DR   MEROPS; M41.007; -.
DR   VEuPathDB; FungiDB:RO3G_04828; -.
DR   eggNOG; KOG0731; Eukaryota.
DR   InParanoid; I1BV93; -.
DR   OMA; YDKQGGG; -.
DR   OrthoDB; 9585at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19501; RecA-like_FtsH; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.1690.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.760; Peptidase M41; 1.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; FtsH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   NCBIfam; TIGR01241; FtsH_fam; 1.
DR   PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR   PANTHER; PTHR43655:SF2; SD01613P; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF06480; FtsH_ext; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT   DOMAIN          197..340
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          620..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  71081 MW;  46223AD2825D7360 CRC64;
     MPSSNVLIAT ALGSYVLYRL TAPTDRGREL TWQAFRSQLL DRGLVDRLEV INRNQVLVYL
     RNEASTLGVP GVFYFSIGSV DAFERQLEKA QRELGIPPNE RIPVAYHDRT SLGETLIGFA
     PTILLIGMLF YLTRKSSGGS QGIFSIGKSK AKRFSEEERV KISFKDVAGA DEAKVEVMEF
     VNFLKNPSIY EKLGATIPKG AILSGPPGTG KTLLAKATAG EAGVPFYSVS GSEFVEMFVG
     VGSSRVRDLF ATAKKNAPCI IFVDEIDAIG KARGKAGGQF GGGGNDERES TLNQLLVEMD
     GFDSDQHVVV LAGTNRPDVL DPALLRPGRF DRHITIDRPD IGGRAQIFEV HLRPIKTVVE
     KPVLARKLAA LTPGFAGADI HNVCNEAALI AARRSKDTVE EKDFEDAIER VIAGLEKKSR
     VLSPEEKKTV AYHEAGHAIA GWYLQYADPL LKVSVIPRGS AALGYAQYLP KDQYLYSRKQ
     LLDRMCMTLG GRVSEQIFFK TITTGAQDDL QKVTKMAYAQ ITAYGMNEKI GPLSFSDPQN
     ENSFQKPFSE QTGTMIDNEA RALVSEAYDR TLQLLTEKKN DIEKVAQLLL SKEVLTREDM
     ENLLGKRPFN EVTVYDEYVR RKPSDTSAPP DFSKPSDDDS VDSKK
//
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