ID A0A0J9X2V7_GEOCN Unreviewed; 666 AA.
AC A0A0J9X2V7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Similar to Saccharomyces cerevisiae YLL029W FRA1 Protein involved in negative regulation of transcription of iron regulon {ECO:0000313|EMBL:CDO51415.1};
GN ORFNames=BN980_GECA01s05873g {ECO:0000313|EMBL:CDO51415.1};
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO51415.1, ECO:0000313|Proteomes:UP000242525};
RN [1] {ECO:0000313|EMBL:CDO51415.1, ECO:0000313|Proteomes:UP000242525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO51415.1,
RC ECO:0000313|Proteomes:UP000242525};
RA Casaregola S.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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; CCBN010000001; CDO51415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9X2V7; -.
DR STRING; 1173061.A0A0J9X2V7; -.
DR OrthoDB; 869at2759; -.
DR Proteomes; UP000242525; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}.
FT DOMAIN 52..181
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 388..593
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 604..666
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 666 AA; 74231 MW; 02FA16F52B3CEEDC CRC64;
MSFRPFDKSS LNKLRVLNPR KYSTNFNFVA PSTGIPSQPT NINRMASTNA ARLAELRVKL
QSHGVGAYVV LTQDEHDSEY TSHADNRREF ISGFTGSAGT AVITVDKALL ATDGRYFLQA
EKELDSSNWE VLKQGVPGVP TWQQWLSQHV LKTGTKIGID PELISYSEYN GLIEALRKNQ
LSADYVVPVK PNLIDQIWGS EQPARSDSQV KILPLKYTGK SFEEKLKDLR ESIAKQHGAG
FLVAALDQIA WLYNLRGGDV PFNPVFRSFT YITSDKAVLY IEDDKVTPEI REYLRDKVEI
KPYRAIFDDA KIAKDIVIKA NSNAASFEDQ KKILVSSSTS WALYDAFGGA EAVSVIPSPV
ELAKAIKNPT EVEGFYTSHV KDGIALMRYF AWLENELKNG NTTLSDYNVG VKAEEFRAQM
PDYRGLSFET ISSSGPNAAV IHYAPAKDSK FYVDINQVYL CDSGAQYLDG TTDTTRTLYF
GENPTEEEII AYTSVLKGHI ALARIVFPEG VNGYMLDALA RQFLWAEGLD YRHGTGHGVG
SYLNVHEGPI GVGLRIHYTE NALQIGNVIS NEPGFYKDGS FGIRIENMVV VKEVKTPNNF
GGKKFLGFDT VTRVPYCRKL IDVGRLTEAE IKWVNEYHAQ VRADTESQLA GDELGLAWLL
RETEPL
//