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Database: UniProt
Entry: A0A0J6YGA6_COCIT
LinkDB: A0A0J6YGA6_COCIT
Original site: A0A0J6YGA6_COCIT 
ID   A0A0J6YGA6_COCIT        Unreviewed;      1059 AA.
AC   A0A0J6YGA6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE   AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN   ORFNames=CIRG_05624 {ECO:0000313|EMBL:KMP05943.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP05943.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
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; DS028096; KMP05943.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6YGA6; -.
DR   STRING; 404692.A0A0J6YGA6; -.
DR   Proteomes; UP000054565; 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:0008233; F:peptidase 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:0000256|ARBA:ARBA00023049};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000313|EMBL:KMP05943.1}.
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;  117394 MW;  B72767F950B6ACDF 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
     IKLKTGGVSS 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
//
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