ID D9QRW8_ACEAZ Unreviewed; 356 AA.
AC D9QRW8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Peptidase M24 {ECO:0000313|EMBL:ADL13259.1};
GN OrderedLocusNames=Acear_1754 {ECO:0000313|EMBL:ADL13259.1};
OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Acetohalobium.
OX NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL13259.1, ECO:0000313|Proteomes:UP000001661};
RN [1] {ECO:0000313|EMBL:ADL13259.1, ECO:0000313|Proteomes:UP000001661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC {ECO:0000313|Proteomes:UP000001661};
RX PubMed=21304692;
RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT 7288).";
RL Stand. Genomic Sci. 3:57-65(2010).
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
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DR EMBL; CP002105; ADL13259.1; -; Genomic_DNA.
DR RefSeq; WP_013278704.1; NC_014378.1.
DR AlphaFoldDB; D9QRW8; -.
DR STRING; 574087.Acear_1754; -.
DR MEROPS; M24.008; -.
DR KEGG; aar:Acear_1754; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_2_9; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000001661; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01092; APP-like; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
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; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF3; AMINOPEPTIDASE YPDF; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Reference proteome {ECO:0000313|Proteomes:UP000001661}.
FT DOMAIN 4..129
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 137..340
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 356 AA; 39739 MW; B2E95CDA41FA169B CRC64;
MEERITALRE KLTELDLDGI MINNLQNKYY LSGFTGTAGT VIITDQEAVL ITDFRYIEQA
ENQAIDFKII EHGNPKIETI REELQRLEVE RLGFEAQQES YQQYQQYQKK LGSLELVPTK
DVVKELRIIK DESELNTIQE AVKIADDAFL HITEYIEPEM TEKEVSLELE YFMKQKGASA
KAFDFIVASG KRGAMPHGVA TDKEIAAGEL VTFDLGSVYQ QYNSDLTRNI IVGSEPTEKQ
QEVYETVLEA QLAAIKAIEP GKTGTEIDKV ARDVITKAGY GDNFGHGLGH GVGLEVHEGP
RLAQGKDEEL RPGMVVTVEP GIYLSGWGGI RIEDIVVVTE EGCNVITEAP KELIRV
//
