ID C5FSP4_ARTOC Unreviewed; 394 AA.
AC C5FSP4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=MCYG_05716 {ECO:0000313|EMBL:EEQ32897.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ32897.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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DR EMBL; DS995705; EEQ32897.1; -; Genomic_DNA.
DR RefSeq; XP_002845847.1; XM_002845801.1.
DR AlphaFoldDB; C5FSP4; -.
DR STRING; 554155.C5FSP4; -.
DR GeneID; 9224146; -.
DR VEuPathDB; FungiDB:MCYG_05716; -.
DR eggNOG; KOG3946; Eukaryota.
DR HOGENOM; CLU_045003_0_0_1; -.
DR OMA; GIQDDHI; -.
DR OrthoDB; 3091175at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
DR GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03880; M28_QC_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR037457; M28_QC.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR040234; QC/QCL.
DR PANTHER; PTHR12283; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR PANTHER; PTHR12283:SF6; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361240}; Protease {ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEQ32897.1};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 30..394
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005125210"
FT DOMAIN 128..364
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 394 AA; 44131 MW; E1E80C6D217250A8 CRC64;
MLGRSSASTL LVVVSYLSFL ALLFSPINAY SPLSDNTLRS LPRPGNDFDI HNGAILAPIL
RPRVPGTPGS TAVLEHFVNF FQNNLPDWRL EFQNSTSKTP VTGDKQIPFV NLIAIRDPPF
TRVGDVSRLT LAAHYDSKLT PEGFIGAIDS AAPCAMLLHA VRSIDAALTK KWKAMEASPT
DNLDMVAQQG VQIFLLDGEE AFGEWTATDS LYGARSLAEH MEHEYYPALS TFTTSLAAIR
LFVLLDLLGN KDPIMPSFFA TTHWAYKHMA TLEQRLRKLG QFKSDPDPKK GAAKVWFTEG
NRPSDKKFMS FISDDHIPFM QRGVEILHLI PWPFPEDIWH KIADDADHLD PPTVEDWSTL
ITAFMAEWMD LEGFFNTKKP NQARIDDEKS ELVP
//
