ID A0A0C9M8M8_9FUNG Unreviewed; 615 AA.
AC A0A0C9M8M8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:GAN03524.1};
GN ORFNames=MAM1_0042d02979 {ECO:0000313|EMBL:GAN03524.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN03524.1};
RN [1] {ECO:0000313|EMBL:GAN03524.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN03524.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; DF836331; GAN03524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9M8M8; -.
DR STRING; 91626.A0A0C9M8M8; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd08022; M28_PSMA_like; 1.
DR CDD; cd02121; PA_GCPII_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 1.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:GAN03524.1};
KW Hydrolase {ECO:0000313|EMBL:GAN03524.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:GAN03524.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 128..206
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 247..430
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 490..609
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 193..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 68463 MW; 6A2F1FA84B72FF6B CRC64;
MTGAISLPLD DGSHGGSIKQ SWNQARLWFD KQWNGEDETT PLLYNERGTA ADQNQQARRK
KTTFRLLVTG IALVLALALL GVSFGFWYTK RHAQEPAKLT EDPVEDDETS RDPSVVPLFH
GYSKNGTVQG RIVYANYGRL QDFQFLKDQG IDLNGTIALM RYGGNFRGLK VKAAETFGCA
GALIYSDPID DGPLNKDNSS NPVESYPDGP WRSKSSAQRG SVQYFSIIAG DPLTPGYPAT
ENATRIKYED SPGAIILGNH RDAWVYGAVD PSSGSASLLE LARIFGELLK TGWRPRRTIV
LASWDAEEYG LVGSTEWVED NAEWLDKEAA VYVNVDTAVS GSHFGVQASP SLNRILYEVT
SEIHDPRTGK SVFDAWSADE KLVGHEHPEV YRLGSGSDFA PFLDHAGIAS VNFAFRGDYG
VYHSNYDSFR WMEKYGDPGF YYHQALVKLW GLLALRLSDS PILPLYLNDY SAEIVKYAAE
ITDLAAPQTF PELEVAVNKL QNITGDFEEH RQGLEKRISQ YKSLDDIPLQ LAKDLKKVND
HLAFFERGFI DPKGNKDRDF FKHVIFAPGL WQGYAAQIFP AIADGIENSN RKQARHAGKR
AAWAIEKTVG LFTGY
//
