ID A0A0F7ZP74_9HYPO Unreviewed; 1163 AA.
AC A0A0F7ZP74;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Mitochondrial presequence protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=HIM_05491 {ECO:0000313|EMBL:KJZ75005.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ75005.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ75005.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ75005.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
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DR EMBL; KQ030520; KJZ75005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZP74; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000054481; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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 PANTHER; PTHR43016:SF16; METALLOPROTEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07610)-RELATED; 1.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054481};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 175..255
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 312..497
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 129756 MW; 545C67FCAADCA774 CRC64;
MAGVIRGTPS NGKEQHHNGW RRLNWPSADR LVHPWGTRQL SAGHICSSPQ NPHPQKVASA
GALASAAFRL ASSPSKRLVV PWQKSLPCKL PSVRTRPSGG HWRSSLAALR SSVTMASGHP
KSHFRKVQSF KTDYAPCTIT QYVSERSGMQ VVVADREGPK INGYFTLATE IFDDSGAPHT
LEHLIFMGSK NYRYKGLLDK LSSRAYSSTN AWTATDHTAY TLETAGWDGF AQVLPVYLEH
IILPVITDDA VVTEVWHIDG EGNDAGVVYS EMQGVQFRSS EIMDLKARRL LYPEDVGFRY
ETGGMTEALR VLTPERIRQF HRDMYQPRNL CLVIVGETNH EDMLKILDEF EDSIKDDIPP
LTAPFKRPWV ESAQPPALKE TTITTAEFPE EDESVGEILV GFFGPDCTDL IATSALNVLL
TYLCGSSVSI LENALVEREE LASSISHWWD SRPDSVIWLQ PTGVATEKLE FVEKRLFELL
KEVAAKPLDM EYMRECIRRE KRQVQFHAET SESFYATNII TDYLFGKRDG STLKDLETLS
EYATLEQWTD EQWRDFLRKW ISDAHHVSIL GKPSHELAIK MKNEEADRLA KRKEKLGAEG
LQALGKRLEE AKEKNDAPIP VEVIDRWSVP STESIHFIES DTARCGRARS VGLGKGSAQK
LIDGATAGNL PLFIQFEDVP TNFVHITIHV GTSQVPVELK PLMPIFSDNF FNTHIKRDGK
IINFEQVVME LERDSVGYGI GSSRSLGDPD GFMIQFQVEP EKYVAAVNWL RTMMFDSVFD
PQRLRAAVTK SLADIPEGKR DGRGMASEVD AAIHMEKSSL SVAKRVLVRA VYLKRLKKLL
KNEPEKVVEW FDTVRSSLFT FQNMRFLVTA NLKKLANPVT TWDPLAEALS PRQEMVPIPK
LSSLLNDEGR KPGSVGAIVI PMTTLDSSYS VSSAPSITSL SDPRFPAIMV AIGYLEAVEG
PLWNAVRGAG YAYGSYFSRS VDSGILSYRV YRSPDVSKAI IASRDAIRNI AEGQVSIDKH
LLEGTMSQIV VMFADEQSTM PSAAQQNFVQ GVVRGLSSDW NKEILRRVRA VTEDEMKAVM
KELILPCFNP GTSNVVVTCA KLMAEGMETA FQGMGYKVQT RELSYFHDDY GLEAGADDED
DEEDEDDEGS EGSDDGDSDE SDD
//
