ID A0A1B9GZB7_9TREE Unreviewed; 824 AA.
AC A0A1B9GZB7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=AFG3 family protein {ECO:0000313|EMBL:OCF36366.1};
GN ORFNames=I316_01613 {ECO:0000313|EMBL:OCF36366.1};
OS Kwoniella heveanensis BCC8398.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF36366.1, ECO:0000313|Proteomes:UP000092666};
RN [1] {ECO:0000313|EMBL:OCF36366.1, ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|EMBL:OCF36366.1,
RC ECO:0000313|Proteomes:UP000092666};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; KI669495; OCF36366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B9GZB7; -.
DR STRING; 1296120.A0A1B9GZB7; -.
DR Proteomes; UP000092666; 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: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; 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; 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:UP000092666}.
FT DOMAIN 367..507
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 88433 MW; 3F5155A571F6A7D3 CRC64;
MSLRAISLRR VPRQISSSVV RPLRSRSYAT PQSPKPSRNP PPPSGLESVF GGSGGKGGTT
VAPKPAGAEP PSGPSQPKRP DVGLPGLGEQ EAIPEDQKEN KNEESPRRHR LSELEGRAGK
KVGTGGGGGG SGGGNGGPAG GPGGFGGMTP NQLLLAAVST YALWSMTQPD DVRSKEITWQ
EFRNSLLARG MVSSLEVVNR SKVRVHLHNP ISPSGSQTPN ATGVSNLPSP SHGPAPYTFT
IGSLEAFETL LISTQDELGI PPAERIPVSY REEISTFSTI MHFAPTLLIG GLILWMARRG
GSAMGGGGPG GGIFGVGKSR AKMFNKDEQV SVRFKDVAGM DEAKEEIMEF VKFLKEPQKY
EKLGAKIPRG AILSGPPGTG KTLLAKATAG EAGVPFLSVS GSEFVEMFVG VGPSRVRDLF
ANAKKNAPCI IFVDEIDAIG KSRGKGGSFG GNDERESTLN QLLVEMDGFG TNEHVVVLAG
TNRADVLDNA LMRPGRFDRH IAIDRPDIGG RRQIFGVHLS PLTLAPEVSK EQIAEKLALL
TPGFSGADIA NVCNESALRA ARRGGDSVTE EDFDGAIERV IAGLERKSRV LGKDEKKTVA
YHEAGHAVCG WFLEHADPLL KVSIIPRGVG ALGYAQYLPK ERFLFSTEQL IDRMSMTLGG
RVSEEIFFGK ITTGAQDDLQ KITKMAFEVC ANYGMNPEIG PISYGGRDQQ SEGFQKPFSE
ATAEALDKAV KKMVVDAHTR TTELLTKHKA DVEKVAHLLL EKEVITREDM RLLLGPRPFE
HKDEMDEYIE AQLDRKKEKE AAPQDTDGPT PALAYKPIDI KEID
//
