ID B6QS08_TALMQ Unreviewed; 898 AA.
AC B6QS08;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Mitochondrial inner membrane AAA protease Yta12, putative {ECO:0000313|EMBL:EEA20643.1};
GN ORFNames=PMAA_044710 {ECO:0000313|EMBL:EEA20643.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA20643.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995904; EEA20643.1; -; Genomic_DNA.
DR RefSeq; XP_002151643.1; XM_002151607.1.
DR AlphaFoldDB; B6QS08; -.
DR STRING; 441960.B6QS08; -.
DR MEROPS; M41.002; -.
DR VEuPathDB; FungiDB:PMAA_044710; -.
DR HOGENOM; CLU_000688_23_4_1; -.
DR OrthoDB; 9585at2759; -.
DR PhylomeDB; B6QS08; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EEA20643.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT DOMAIN 450..590
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 50..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 100576 MW; 1F391A6933EA5190 CRC64;
MASILRRPAH IARYSRSAAE LFTTSKSIYP HHTRPQLWSL ITARQARSYA SINPGDPKRP
DDKNKNKKVQ KSKDEELAEF FASLKKNGPE AKKSFNSAAD EKEFLEQSVQ FINKLISESG
LPQRESELLR LVQTLLTEAK YMPPEMEEFF RKHVDQKQPM TLEDWDKFSK FWLQHIGEEN
VRAAQFAKLS PDEVKALFKK ISEEKPEGGF TWGSQEQKKT NGQPGQKPKD GKDPKGPKVL
EFKFDPSSFI VTSILSYMLY TTFFPGETSR DITWQEFRSN FFDKGLVEKL TVLNRSRVRV
DLNREAVAGE MPDSQAAQRN FHYYFNIGSV DSFERKLEEA HNELGIPTSQ RVPVAYVEEV
PWLATALSFG PTLLLIGSVF YFSRRAGGGA GGQSSIFGIG KSRARRFNHE TDVKIKFADV
AGMDEAKMEI MEFVSFLKEA EKFQRLGAKI PRGAILSGPP GTGKTLLAKA TAGESGVPFF
SVSGSEFVEM FVGVGPSRVR DLFANARKNT PCIIFIDEID AIGKSRSKQN FGGGNDERES
TLNQILTEMD GFNTSEQVVV LAGTNRPDVL DKALMRPGRF DRHITIDRPT MKGREQIFRV
HLKKILTKED MDYLCGRLAA LTPGFAGADI ANCVNEAALV AAREQADSVK MKHFEQAIER
VIGGLEKKSL VLSPEEKRTV AYHEAGHAIC GWYLKWADPL LKVSIIPRGQ GALGYAQYLP
SSENYLMTVN QLMDRMAMTL GGRVSEELHF DTVTSGASDD FNKVTRMASA MVTKFGMSKA
IGPLHFEEDQ QQLHKPFSEE TARNIDLEIR RIVDEAYKRC QDLLTEKKKE VGLVAEELLS
KEVLSRDDMV RLLGPRPFPD TGEFTKYFGG GTIAPPEPPA SDESTMGKDG RDQSPLPT
//
