ID V9KW99_CALMI Unreviewed; 477 AA.
AC V9KW99;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Mitochondrial-processing peptidase subunit beta {ECO:0000256|ARBA:ARBA00020510};
DE EC=3.4.24.64 {ECO:0000256|ARBA:ARBA00012299};
DE AltName: Full=Beta-MPP {ECO:0000256|ARBA:ARBA00031018};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP02560.1};
RN [1] {ECO:0000313|EMBL:AFP02560.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Spleen {ECO:0000313|EMBL:AFP02560.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal transit peptides from precursor proteins
CC imported into the mitochondrion, typically with Arg in position P2.;
CC EC=3.4.24.64; Evidence={ECO:0000256|ARBA:ARBA00001098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Heterodimer of PMPCA (alpha) and PMPCB (beta) subunits,
CC forming the mitochondrial processing protease (MPP) in which PMPCA is
CC involved in substrate recognition and binding and PMPCB is the
CC catalytic subunit. {ECO:0000256|ARBA:ARBA00011587}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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DR EMBL; JW870042; AFP02560.1; -; mRNA.
DR AlphaFoldDB; V9KW99; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF103; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT BETA; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 2: Evidence at transcript level;
FT DOMAIN 59..203
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 209..394
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT NON_TER 477
FT /evidence="ECO:0000313|EMBL:AFP02560.1"
SQ SEQUENCE 477 AA; 53299 MW; D277A24EB5A99902 CRC64;
MAARLSRGIA GGHRLLRGVW APQRQPILQR FRATQATAVQ VLNIPETKVT TLDNGLRVSS
EDSGLPTCTV GLWIDAGSRY ENEKNNGTAH FLEHMAFKGT KKRSQLDLEL EIENMGAHLN
AYTSREQTVY YAKAFSKDLP RAVEILADII QNSTLGEAEI ERERGVILRE MQEVETNLQE
VVFDYLHATA YQDTALGRTI LGPTENIKSI NQGDLVEYIT THYKGPRIVL AAAGGVEHEE
LTDLAKHHFG NLSSTYDGDT TPVLPVCRFT GSEIRVRDDK MPLAHIAVAI EAVGWSNSDT
IPLMVANTLI GNWDRSFGGG VNLSSKLAQV TCQGNLCHSF QSFNTCYTDT GLWGLYMVCE
PNTIEEMLHF VQREWMRLCT SVTEAEVARA RNLLKTNMLL QLDGSTPICE DIGRQMLCYN
RRIPLPELDA RIDAVDAKTI RDVCTKYLYD KCPAIAAVGP IEQLPDYNRI RSAMYWL
//
