ID C9STL3_VERA1 Unreviewed; 852 AA.
AC C9STL3;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=Lon protease homolog {ECO:0000256|PIRNR:PIRNR001174};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR001174};
GN ORFNames=VDBG_08284 {ECO:0000313|EMBL:EEY22174.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SIMILARITY: Belongs to the peptidase S16 family.
CC {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122}.
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DR EMBL; DS985225; EEY22174.1; -; Genomic_DNA.
DR RefSeq; XP_003001239.1; XM_003001193.1.
DR AlphaFoldDB; C9STL3; -.
DR STRING; 526221.C9STL3; -.
DR GeneID; 9529285; -.
DR KEGG; val:VDBG_08284; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_0_1; -.
DR OMA; MVNIEDK; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000008698; 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: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 Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 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; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001174};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001174};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001174};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW Serine protease {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 9..258
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 649..836
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 404..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 742
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 785
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 852 AA; 93222 MW; 94C79BB51BA43B5C CRC64;
MARTPDSTVP VIPLARGTIL LPGITHRVPV SASRPDIPAL LANVYTRAAA AGPNARIDAV
PIVCVPVASP FVGPNGQLLI DSAESVDESQ IKQINPGSAT KEDLFNYGVA ARITGIEGRG
TAEFALRVEG VARVRVEKVT QERPYFEATV KHYPDVVTAD AQLQELFGLM KLRSRELVLT
LRISSLLPTP RNAENPGLSP LIIRRLEMFI MKKEVKDAGS LADFMTNIVE ASYEQKLEVL
AALDIKVRMA KVIELLDRQV SGLKNSFKIT AFTNVPVQVL DKLHDRAPKR RGTGPGGVPV
PPNGFFPPGA NGMMAAALKK MMPGNQEFQV TRTWLEVLSE IPWSATTDDR LGPETLVRAR
KQLDDDHYGL DKVKKRLVEY LAVLRLKQSV NDEVDEQIRK AEEESVALST GKETEENKPA
NDADLEEKVS NAHAKRKRTP LSPHDRQVAH YAARRTSRGL RKGGVANPVF LLDEIDKLGM
SNMHGDPSAA MLEVLDPEQN INFTDHYVGM PIDLSKIVFI ATANSLDTIP APLLDRMETI
YLPGYTTLEK RHIAMQHLVP KQIRVNGLAE DQINFNKEVV SKIIESYTRE AGVRNLEREI
GSVCRAKAVD FAEAKDGGQL ETYRAQLTVD DIETILGIER FEEEIAETTS RPGIVTGLVA
YSSGGNGSIL FIEVADMPGD GRLQLTGKLG DVLKESVEVA LSWVKAHAFE LGLTSDPTTN
IMKERSIHVH CPSGAIPKDG PSSGIGQAIA LISLFSGKSV PPTMAMTGEI SLRGRVTAVG
GIKEKLIGAL RAGVKTVLLP AQNRKDVKDL PQEVKDGLEI LHVSHIWEAV RLVWPESQWP
GLEHYAAIES RL
//
