ID A0A1E3PBG5_WICAA Unreviewed; 870 AA.
AC A0A1E3PBG5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Lon protease homolog {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|RuleBase:RU000592};
GN ORFNames=WICANDRAFT_39209 {ECO:0000313|EMBL:ODQ62718.1};
OS Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL
OS Y-366-8) (Yeast) (Hansenula anomala).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=683960 {ECO:0000313|EMBL:ODQ62718.1, ECO:0000313|Proteomes:UP000094112};
RN [1] {ECO:0000313|EMBL:ODQ62718.1, ECO:0000313|Proteomes:UP000094112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8
RC {ECO:0000313|Proteomes:UP000094112};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- SIMILARITY: Belongs to the peptidase S16 family.
CC {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
CC ECO:0000256|RuleBase:RU000591}.
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DR EMBL; KV454208; ODQ62718.1; -; Genomic_DNA.
DR RefSeq; XP_019041925.1; XM_019182543.1.
DR AlphaFoldDB; A0A1E3PBG5; -.
DR STRING; 683960.A0A1E3PBG5; -.
DR GeneID; 30199789; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000094112; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 3.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001174};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001174,
KW ECO:0000256|PIRSR:PIRSR001174-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001174};
KW Reference proteome {ECO:0000313|Proteomes:UP000094112};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001174}.
FT DOMAIN 1..244
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 678..855
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 85..130
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 249..276
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 762
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 804
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 398..405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 870 AA; 97860 MW; 887FD1877177B14F CRC64;
MNAVNRLVDE NKPYIGVFAF KKEDADSDTI SSKDEVFETG VFAQITSCHM TKDVHGKENM
TIVVYPHFRI KIDEVLPPKP LGEVITSETI NKDKLEKEVE QELLEEGKAL EEESVKNEKE
ERLIKKIDEE SEYNPTEFLS EYEVSRVNIS LASSEPFDKS SPVVNALSSE ILRVFKDAAQ
YNHHIKEQLT VFSDRDGGSV FDNAGELADF TASLCVGKVG EIQEVLDELN VEKRLEMALT
LLKREVLQVQ LYDKIVKEVE QKITKKQQEY VLMEKLKQIK KELGMDDGRQ KVIDTITERI
KDYDIPESVQ KIIDDEITKL QTLEPHMSEF GVTRNYLDWI SYIPFGKFTP ETFNIASAKK
ILEEDHYGLK DVKDRILEFI AIAKLLGSVK GKIICFVGPP GVGKTSIGKS IGRALNRNFF
RISVGGLSDV SEIKGHRRTY VGALPGRIIQ ALKKTRTMNP MILIDEIDKI STHPAINGDP
SAALLELLDP EQNNEFLDQY MDFPVDLSKA LFVCTANTLD TIPRPLLDRM EVIEIPGYVQ
EEKVQIAKNY LIPSAKKESG LEDVNIKIED ETVDAIVKHY AKENGVRRLK QLVEKIYRKA
AFKAVTDTVE KDELVSEEKV QPNIDHREPK ADRETVKKED IPVEKVVLPE SFALDITPEN
LKDYIGPPVY TSDRLYEVTP AGVIMGLAWT QIGGTSLYVE STGEPVEKGG DFRVTGRLGE
TMKESSNVAF ALAKSFVKTD YFKKHNVYVH CPEGAIPKDG PSAGITMTTS LISLALNKPL
PPIAMTGEVT LTGKVLRIGG LKEKLIAAKR NGIKKVILPK NNENDFDDLE AKLKEDFEPL
FVDNYSEIFE ELFSDCANEP VLETKESKND
//
