ID E3KQI8_PUCGT Unreviewed; 888 AA.
AC E3KQI8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=AFG3 family protein {ECO:0000313|EMBL:EFP86563.1};
GN ORFNames=PGTG_12945 {ECO:0000313|EMBL:EFP86563.1};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP86563.1, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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; DS178301; EFP86563.1; -; Genomic_DNA.
DR RefSeq; XP_003330982.1; XM_003330934.2.
DR AlphaFoldDB; E3KQI8; -.
DR STRING; 418459.E3KQI8; -.
DR MEROPS; M41.A10; -.
DR EnsemblFungi; EFP86563; EFP86563; PGTG_12945.
DR GeneID; 10540662; -.
DR KEGG; pgr:PGTG_12945; -.
DR VEuPathDB; FungiDB:PGTG_12945; -.
DR HOGENOM; CLU_000688_23_0_1; -.
DR InParanoid; E3KQI8; -.
DR OMA; ARQKGNF; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
DR GO; GO:0097002; C:mitochondrial inner boundary membrane; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:EnsemblFungi.
DR GO; GO:0006465; P:signal peptide processing; IEA:EnsemblFungi.
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; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT DOMAIN 366..506
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 37..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 96292 MW; 8020B66A7E38098C CRC64;
MSIRRIPNLI LNHPHHLRTQ FLNNRYPNRL GLFQSISSST RSSDSQPSSS SSSSPSPSNS
EKPRNPRRNS TKNQPPKKDQ QQEEDQNPFS DFINLSKLFG QPSKPNSSEH PKFNNESDHG
KGNKSGKGAS STSGSEQQQS PGAANGLVFW ALGAYALYHI LAGDSLSNRE ISWQEFRTGV
LDKGLVEKLE VINRSKVKVY LHPNAFKLTG INPNGSSSAP SGSIASPSAG ASYFFSIGSV
EAFERKLDKA QDELGIPSHE RVPVSYHEQA SLMNLFWNFA PTLTLAGLLF YVSRRATGMG
GAGGGAGGPG GIFNIGKSKA KMFNHESEVK TKFKDVAGMD EAKEEIMEFV KFLKEPEKYE
RLGAKIPKGA MISGPPGTGK TLLAKATAGE AGVPFLSVSG SEFVEMFVGV GPSRVRDLFA
TAKKNSPCIV FVDEIDAIGK ARGKSGAMGG NDERESTLNQ LLVEMDGFDT SQHVVVLAGT
NRADVLDKAL LRPGRFDRHI AVDRPDVSGR RQIFLVHLRP LVLEGAIKTK EDLKSSGSDP
LPEEDEDFEG PESVEKVIPD WLVKLSHKLA AHTPGFSGAD IANVCNEAAL IAARLSAEFV
TEKHFDMAIE RVVAGLERRS RVLSPEEKRT VAYHEAGHAI MGWFLEHADP LLKVSIIPRG
VGALGYASYL PQERFLYTTE QLIDRMCMTF GGRVAEEIFF GKITTGAQDD LQKITKLAFE
LVGNYGMSRD FGPISFGRSD SQQESFQKPY SEKTGEHLDS TVRALINQAH KRTTELLTEK
KELVDKVAQR LLDREVLSRQ DMIDLIGRRP FDRPDAYDDA MGSSGKPGPP PAPGSPSGGQ
NRPTPKPATD GPNPLGEGIE GGGGVPLPTP ALSSPAVLPE QSHSGLAN
//
