ID A0A2P4ZI93_9HYPO Unreviewed; 901 AA.
AC A0A2P4ZI93;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=AFG3 family protein {ECO:0000313|EMBL:PON24004.1};
GN ORFNames=TGAM01_v207015 {ECO:0000313|EMBL:PON24004.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PON24004.1, ECO:0000313|Proteomes:UP000054821};
RN [1] {ECO:0000313|EMBL:PON24004.1, ECO:0000313|Proteomes:UP000054821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6085 {ECO:0000313|EMBL:PON24004.1,
RC ECO:0000313|Proteomes:UP000054821};
RX PubMed=26893428;
RA Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL Genome Announc. 4:e01747-15(2016).
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}.
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:PON24004.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPDN02000025; PON24004.1; -; Genomic_DNA.
DR RefSeq; XP_018662664.1; XM_018804235.1.
DR AlphaFoldDB; A0A2P4ZI93; -.
DR STRING; 398673.A0A2P4ZI93; -.
DR GeneID; 29984318; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000054821; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054821}.
FT DOMAIN 440..581
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 49..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 901 AA; 99747 MW; B0AAFAEF8352C7C4 CRC64;
MSRYLRQSSQ LAKLARFSTS VSLQRTQRLV ASSRTAPLRA LSAHNGILPR YYSSKTPHPD
ENKSSDSGKQ INHNDAKSET EGGPESQKVP LPPLPEGWIR LTKEEISQLQ AFQEMLPEGQ
RQTLKDILVG LQHTGAPAEI RDLLQKMRQG PGNLSIIDKG RLMRCVFVMA ERVAEWEIEQ
QQQGKKGMFD QNTNEMNEHS YGEKKEGAAQ SHKASSDSHS KEQGSDPKKP ERNSWMDALQ
TGLVLGITLW AIESFSRPFS EKEITWQELR KAFLDKGLVQ KLVVVNGSQV RVELHPDAVQ
STSDGSGARR TYIFSIGSVE SFEKKLEEAQ DQLGIPPSER IPVSYEAGGS TMGNLVLAFG
PTLLFIGLIL WTQRSMSGRA GGAGGMFNFG KSKAKKFNAE SAVKVKFSDV AGLEEAKVEI
MEFVSFLKQP EKFEKLGAKI PRGAILSGPP GTGKTLLAKA TAGESGVPFY SVSGSEFVEM
FVGVGPSRVR DLFAEGRKNA PCIIFIDEID AIGRARQESG RGFGGNDERE ATLNQILTEM
DGFNTREQVV VLAGTNRADV LDKALMRPGR FDRHIYIDRP TMKGRQEIFQ VYLKKIVTKE
DHEHLIGRLA TLTPGFSGAD ISNVVNEAAL IAARENADDV KMVHFERAIE RVIGGLERKS
LVLRPEEKKT VAYHEAGHAI CGWFLRHADP LLKVSIIPRG QGALGYAQYL PQDAYLMNTD
QLMDRMAMTM GGRVSEELHF PTVTTGASDD FKKVSSMARS MVTQWGMSDK VGPVHFENDP
NRMVKPFAEA TAQQIDQEVH RIVEEAYTRC RNLLAEKKEQ VGLIAEELLK KEVLSRDDMV
RILGKRPFDD NEDFEKFFGG KEASAPPPFP AETDTPKEDP PSGTPAPAFR DISNDGSGVK
R
//
