ID N4TK43_FUSC1 Unreviewed; 536 AA.
AC N4TK43;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=D-aminopeptidase {ECO:0000313|EMBL:ENH63903.1};
GN ORFNames=FOC1_g10008045 {ECO:0000313|EMBL:ENH63903.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH63903.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
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:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
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; KB730535; ENH63903.1; -; Genomic_DNA.
DR AlphaFoldDB; N4TK43; -.
DR MEROPS; S12.002; -.
DR VEuPathDB; FungiDB:FOC1_g10008045; -.
DR HOGENOM; CLU_020027_0_4_1; -.
DR OMA; QFVCALL; -.
DR Proteomes; UP000016928; 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:ENH63903.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:ENH63903.1};
KW Protease {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:ENH63903.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016928}.
FT DOMAIN 9..343
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT DOMAIN 354..533
FT /note="D-aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF07930"
SQ SEQUENCE 536 AA; 58758 MW; 1DDAE141FDE45639 CRC64;
MPVSKEIVQD ILKAIPARIR GPGGAVAVLS DGALVDQRVW GYADFNRRIP MTDDTLIPIC
SISKQMLCGL VADLEKNPTP KLAEKGDVKT QFEEKLKEIL PELAKTGELK IDHLCNNRSG
IRDYWAITLL WGAKPEDPYS IAEHNEKVLK TIKSTHFTPG TEYSYCNTNF NIVARVVEAT
TGESLSDLLN ARIFGPAGMK TAQLGADTAK LPPPCVGYEG DEDRGYIPAE NRIEWAGDAG
IIASLGDMIA YESFLDRSLF DPNSWYRAIF KPTSFTDGVP SIYSQGLGHS QYGSVSGIGH
GGALRGFRLY RAHVPEERLS VVAMFNHEAD AATLVEHIIQ TALALQKPPP PTLVDTSPTW
PGIYLDDGTQ LAVTIKNGKK GQIVVNYANY AEPVNLTDPE RGESRAMVAV VDGDNLRIQR
LKENRTLNAK RLKIGDTPVD NSAFTGDFYS EEIGSIFHCV DQGGLMFGTF EGFLGHSPAQ
FMRYLGGDVW ALANPRGMDA KPPGDWTLVF HRDEKGAVVG VTIGCWLARK IEFVKK
//
