ID N1S457_FUSC4 Unreviewed; 537 AA.
AC N1S457;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=D-aminopeptidase {ECO:0000313|EMBL:EMT72889.1};
GN ORFNames=FOC4_g10004380 {ECO:0000313|EMBL:EMT72889.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT72889.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- SIMILARITY: Belongs to the peptidase S12 family.
CC {ECO:0000256|ARBA:ARBA00038215}.
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DR EMBL; KB726264; EMT72889.1; -; Genomic_DNA.
DR AlphaFoldDB; N1S457; -.
DR MEROPS; S12.002; -.
DR HOGENOM; CLU_020027_0_4_1; -.
DR Proteomes; UP000016929; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.50; -; 2.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR027279; D_amino_pept/lipop_sf.
DR InterPro; IPR012856; DAP_B_dom.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR Pfam; PF07930; DAP_B; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF50886; D-aminopeptidase, middle and C-terminal domains; 2.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EMT72889.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:EMT72889.1};
KW Protease {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:EMT72889.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016929}.
FT DOMAIN 9..334
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT DOMAIN 355..534
FT /note="D-aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF07930"
SQ SEQUENCE 537 AA; 58852 MW; 051665BD94A9B2F7 CRC64;
MPVSKEIVQD ILKAIPARIR GPGGAVAVLS DGALVDQRVW GYADFNRRIP MTDDTLIPIC
SISKQMLCGL VADLEKNPTP KLAEKGDVKT QFEEKLKEIL PELAKTGELK IDHLCNNRSG
IRDYWAITLL WGAKPEDPYS IAEHNEKVLK TIKSTHFTPG TEYSYCNTNF NIVARVVEAT
TGESLSDLLN ARIFGPAGMK TAQLGADTAK LPPPCVGYEG DEDRGYIPAE NRIDEWAGDA
GIIASLGDMI AYESFLDRSL FDPNSWYRAI FKPTSFTDGV PSIYSQGLGH SQYGSVSGIG
HGGALRGFRL YRAHVPEERL SVVAMFNHEA DAATLVEHII QTTLALQKPP PPTLVDASPA
WPGIYLDDGT QLAVTIKNGK KGQIVVNYAN YAEPVNLTDP ERGESRAMVA VVDGDNLRIH
RLKENRTLNA KRLKIGDTPV DNSAFTGDFY SEEIGSIFHC VDQGGLMFGT FEGFLGHSPA
QFMRYLGGDV WALANPRGMD AKPPGDWTLV FHRDEKGAVV GVTIGCWLAR KIEFVKK
//
