ID A0A2G5B8S9_COERN Unreviewed; 615 AA.
AC A0A2G5B8S9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Creatinase/aminopeptidase {ECO:0000313|EMBL:PIA15419.1};
GN ORFNames=COEREDRAFT_44881 {ECO:0000313|EMBL:PIA15419.1};
OS Coemansia reversa (strain ATCC 12441 / NRRL 1564).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX NCBI_TaxID=763665 {ECO:0000313|EMBL:PIA15419.1, ECO:0000313|Proteomes:UP000242474};
RN [1] {ECO:0000313|EMBL:PIA15419.1, ECO:0000313|Proteomes:UP000242474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1564 {ECO:0000313|EMBL:PIA15419.1,
RC ECO:0000313|Proteomes:UP000242474};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766, ECO:0000256|RuleBase:RU000590}.
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DR EMBL; KZ303507; PIA15419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5B8S9; -.
DR STRING; 763665.A0A2G5B8S9; -.
DR OrthoDB; 869at2759; -.
DR Proteomes; UP000242474; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:PIA15419.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:PIA15419.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242474}.
FT DOMAIN 11..138
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 320..539
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 553..613
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 615 AA; 68408 MW; 58310F55A0184356 CRC64;
MISTPVSTSD RLGRLRELMA NPKYNISAYV VPSEDAHQSE YVASCDQRRA FISGFDGSAG
CAVITMDKAA MFTDGRYFLQ ARKQMDENWT LMKRGMPGVP SWQEYLVDHL PEGTRVGVDP
AVIVASEGDR LKKALQAKGS GGDLVSIEDN LVDKVWGTER PPQPKNKVFV QDIKYAGELH
VDKIARVREE IKKEGVDGLV ISALDEIAWL LNLRGSDIDY NPVFMAYVLV TKSDVTLYID
DSKLTKTVCE HLGAITVKPY QEIFNNLAEH STALLQSKRQ FSVSTTASLA LVQALGTDNV
KIGMPPVTSL KALKNAAEIE GMRQCHIRDG AAMANYFGWL ENELLRGDGN LRLTEVDVAD
KLEEFRRAEE HCVGLSFSTI SAVGANGAII HYSPQRDTDA KMDTSQMYLC DSGGQYLDGT
TDVTRTYHFG EPTKWQRECF TRVLKGHIAL DNAVFPSGTS GYALDPLARF SLWELGLDFR
HSTGHGVGSF LNVHEGPQLI GMRKSSMDFG LRPNMTITNE PGYYEDGNFG IRIENTCVVI
KVDTPYDYTG GAGFLKLDPV TMVPIQKKLV LPELFTDVER KWLNSYHQLV WEKVSPLLEK
GGLGYEWLKR ETALM
//
