ID A0A1X2HTR2_SYNRA Unreviewed; 650 AA.
AC A0A1X2HTR2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ATP-dependent protease La {ECO:0000313|EMBL:ORZ02956.1};
GN ORFNames=BCR43DRAFT_450062 {ECO:0000313|EMBL:ORZ02956.1};
OS Syncephalastrum racemosum (Filamentous fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX NCBI_TaxID=13706 {ECO:0000313|EMBL:ORZ02956.1, ECO:0000313|Proteomes:UP000242180};
RN [1] {ECO:0000313|EMBL:ORZ02956.1, ECO:0000313|Proteomes:UP000242180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORZ02956.1,
RC ECO:0000313|Proteomes:UP000242180};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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:ORZ02956.1}.
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DR EMBL; MCGN01000001; ORZ02956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2HTR2; -.
DR STRING; 13706.A0A1X2HTR2; -.
DR InParanoid; A0A1X2HTR2; -.
DR OMA; NAERFHI; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000242180; Unassembled WGS sequence.
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: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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
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 PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000242180};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 453..640
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 74..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 545
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 588
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 650 AA; 71478 MW; E46EC094E1395971 CRC64;
MQDIGVSPAA LRPLQHRVLR NKPMDIAHLM LCLTESSLQD KLHALEITDP DVCLEWAMKK
IRMHLQVYDI RLPASSSSSS SSSSSSSSSS SISTMTDDHL CLPANPEDDE ELADLIEQLN
QAQLPPHAQR LVRRDIQRLR KLPPSQPESG VIRAYLEVIA DLPWQEKSDA LVDITVARQQ
LDADHYGIEH VKRRILEYLS VVKVKQDLSP PILCLVGPPG VGKTTLARSI ATALRRKFHR
ISLGSVRDEA DIRGHRRTYV AAMPGQLING MRRCAVKNPV ILLDEIDKVI QNSQQGDPAA
AMLEVLDPGQ NATFVDHFLN MPFDLSQVLF IATANSLESI SGPLRDRMEV VHLSGYTSDE
KLAIARAHLL PKQIAAHGLS ALRISDDCLN TIIENYTQES GVRNLDRTIA AICRYQCHRL
CEKNQPMEAH VEEADLEAIL GMAPFVQDVA EENVAPGIVN GLAYMQSGTG GLLVAEANQM
PGRGRLRLTG SLGDVIKESA YIAVSWVKSN AYTLHLTQSA NQELLPDMDL HIHLPSGAIP
KDGPSAGVTM VMCILSLLSG RTVSRTTAMT GEITLRGQVR PVGGIREKVI AAHRAGMTRL
LIPAANRRDV QHDVPEKVRN AMTFVYCKTV WEAVQAAFEQ WAAVPVTSRL
//
