ID A0A395RXB2_FUSSP Unreviewed; 700 AA.
AC A0A395RXB2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=Penicillin-binding {ECO:0000313|EMBL:RGP64773.1};
GN ORFNames=FSPOR_7709 {ECO:0000313|EMBL:RGP64773.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP64773.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP64773.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP64773.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SIMILARITY: Belongs to the peptidase S12 family.
CC {ECO:0000256|ARBA:ARBA00038215}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGP64773.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PXOF01000110; RGP64773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395RXB2; -.
DR STRING; 5514.A0A395RXB2; -.
DR Proteomes; UP000266152; Unassembled WGS sequence.
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; IPR049511; PGH-like_rpt.
DR PANTHER; PTHR46825:SF15; BETA-LACTAMASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR Pfam; PF17660; BTRD1; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..700
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017187977"
FT DOMAIN 323..583
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 700 AA; 78895 MW; 8F7E45FB801B4BE8 CRC64;
MRLNILGCLL AFLPLLLHAQ EEEDPNEISE MPTDSRPTVA WYIDNTAQSH TDRARELKID
GFRPMSLSGY GNPTETRYAA TWIKDGRAGH SWQMAWGLKK KDFDEWVRKW RNGGFRLAII
SANGPAGKAE FHGVMTLALD QLKWTYKCEI EDLDKYMAGK DNNGISRVVS FRMYGELDNR
RYCVVLHENN GNERWALQHA EPGLLPNESW ISEFNYPHVS RQFLRPAKLF MSHDGVITPL
MTDMNVGGWS VAVRLNQTAM ASEISRQGNQ WFMPVDIQGA SGFGKTQFNA IFVERTRYQP
RLWAEHGEVS GFKNNKEAKK EVDGIMKDFL KENGIRQAQV AIGARGHAML ERSYTWAEMA
YGTVKPHDVF LIGGVSKMFL HAAVKWCVVQ LLITYDTPVY KLLGYRNAFD KRVEDISIQH
LLDHTAGYDS EASGEAAFEF GKIGLKLPHN GTEPATIHDV IKYKLKQRLD YNPGERMVHS
HYGSLLLGAV VANLTEMSYM DFLNKHILDG LDVSLFETDS RAHLRDKIVQ QGLQIGVDAR
YPAKGEYVSG VYGGDGAIKE ETAAAFSLRS SATSLVKFAG QHSVARIGKR RDGYRRGGIE
GGYAYVETHG DFDWAMVFNT REFASKSAVL DLADKIRKVV DRTIAENKYG PFTLTCNPGP
EILRKGYPGL DGVSQDSLDH LPECTEEELD EIMHDRKDLD
//
