ID A0A0J8RYB5_COCIT Unreviewed; 1059 AA.
AC A0A0J8RYB5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN ORFNames=CIHG_07800 {ECO:0000313|EMBL:KMU89767.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU89767.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- FUNCTION: Degrades mitochondrial transit peptides after their cleavage
CC in the intermembrane space or in the matrix, and presequence peptides;
CC clearance of these peptides is required to keep the presequence
CC processing machinery running (By similarity). Preferentially cleaves
CC the N-terminal side of paired basic amino acid residues (By
CC similarity). Also degrades other unstructured peptides (By similarity).
CC May function as an ATP-dependent peptidase as opposed to a
CC metalloendopeptidase. {ECO:0000256|ARBA:ARBA00034467}.
CC -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000256|ARBA:ARBA00007575}.
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DR EMBL; DS017015; KMU89767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RYB5; -.
DR STRING; 396776.A0A0J8RYB5; -.
DR VEuPathDB; FungiDB:CIHG_07800; -.
DR eggNOG; KOG2019; Eukaryota.
DR Proteomes; UP000054563; Unassembled WGS sequence.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KMU89767.1};
KW Protease {ECO:0000313|EMBL:KMU89767.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563}.
FT DOMAIN 519..777
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
FT REGION 192..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 525..575
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1059 AA; 117382 MW; 25659FCD62796CE3 CRC64;
MLRSSSRALR HGTSTSLSLG FRNTTNLRRF PALQGLRAAS TVTDLNAYPS IGEKLHGFTV
QEKKHVPELH LTAVRLKHDN TDADYLHVAR DDKNNVFGVG FKTNPPDATG VPHILEHTTL
CGSEKYPVRD PFFKMLPRSL SNFMNAFTSS DHTTYPFATT NKKDFQNLLS VYLDATLHPL
LKEEDFRQEG WRLGPENPRA AEQSGKSPDE AAPGDDIVFK GVVYNEMKGQ ITDANYLYYI
KFKEHIFPAI NNSGGDPEYI TDLTHKQLVS FSKQNYHPSN AKVFTYGDMP LADHLKQIGA
VLDGFQKKSS KLDVKLPRDL SAGPLNFTVE GPMDPFTSED KQCKSSVSWR AGDSTDEVEV
FSLGILSSLL LDGYGSPMYR ALIESGLGSS FTPNTGLDTS GRIPIFSVGL NGVSESDVPA
VKQRVEQVFK ECMETGLNRE KVSGYLHQLE LALRHKTANF GLGVMEKTLS AWFNGFNPTR
ELAWNDIISE FEKRWGKTGY LENLMKKYFM NDECLTFTMN GSPTYNQALA EKEMARKEAK
MAELAAKFGS ADAAIEQLKK EELELLKVQE SAQNADVSCL PTLHIKDIPR EMERKPVRES
KIDDVEVVWR EAPTNGLSYI QALNVYSDIP DELRLLLPLF NEAVMRLGTA QRTMEQWEDL
TKLKTGGVSS STFSVSSPLV LGNFTEGLQF TGYAMDKNVP DMLEIITTLV TEADFSSEAA
PKMVQELLRS NTNGALDAVA GSGHRFAVNA AAAGLSKNFW VQEQKAGLSQ IQAVADLLRD
AENSPEKLRQ LIEKLRLIQS FAISKSPKLR IRVVCESGSS GENEAILQRW LSRLPKAIAP
PTTSGATSFS PSSSKILYDL PFQVSYSGLA LRTTPFTGPD SAPLSVLSQL LTHKYLHPEI
REKGGAYGAG ASNGPIQGLF SFSSYRDPNP MNTFKVFNNS GVFARDRTWI QRELDEAKLG
IFQSLDAPMS VDEEGQRYFL TGVTQDMDQR WREQVLDVTA QDVNRVAQKY LIEGTERVFC
LLGNKDNASN LDGWDVRNMS MGNDAESAAL AQDAASVDA
//
