ID S0E2L2_GIBF5 Unreviewed; 1050 AA.
AC S0E2L2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Related to metalloprotease 1 {ECO:0000313|EMBL:CCT66923.1};
GN ORFNames=FFUJ_13093 {ECO:0000313|EMBL:CCT66923.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT66923.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
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; HF679026; CCT66923.1; -; Genomic_DNA.
DR AlphaFoldDB; S0E2L2; -.
DR STRING; 1279085.S0E2L2; -.
DR EnsemblFungi; CCT66923; CCT66923; FFUJ_13093.
DR VEuPathDB; FungiDB:FFUJ_13093; -.
DR HOGENOM; CLU_006065_0_0_1; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000016800; Chromosome 4.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43016:SF16; METALLOPROTEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07610)-RELATED; 1.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CCT66923.1};
KW Metalloprotease {ECO:0000313|EMBL:CCT66923.1};
KW Protease {ECO:0000313|EMBL:CCT66923.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 61..145
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 200..383
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1013..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1050
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 118200 MW; 353A5E1A56A7C3B4 CRC64;
MSPEPSKSHF RKIQSFKTDY APCTITQYVS DRSGMQVVVA DRKGPKLNGY FTLATEIFDD
SGAPHTLEHL IFMGSKSYQY KGLLDKLSSR AYSHTNAWTA TDHTAYTLET AGWDGFAQVL
PVYLEHVILP TITDESIVTE VWHIDGEGND AGVVYSEMQA VQFRSSELMD IKARRLLYPE
NVGFRYETGG MTDALRVLAP ERIRQFHRDM YQPRNLCLVL VGEVNQDELI QILEDFEESI
KDEIPSLDTP FKRPWIDSAQ PPKLNETQIV TVEFPEEDES VGEVLVGFFG PNCNDLIQSS
ALNVLLTYLC GSSVSILENV MVEKEELASS VSYWTDPRPD MVIWLQPTGV ATEKLEFVEK
RLFELLKEVA SKPIDMDYMR ECIRREKRQV KYHAETSESF YATNIITDYL FGKRDGSTLK
DLKDLEEYDV LEKWTDQQWR DFLSKWMADA PHISILGKPS HELATKMKKD EEARIAKRKE
DLGAEGLEKL AKRLEDAKKK NDEPIPASVV DRWSVPSTDS IHFIESDTAR SGHARAVGLG
SGSAQKLIDG TTQGKLPLFI QFEDVPTNFV HITIHIGTSQ VPNELKPLMP IFSDNFFNTH
IMRDGKQVGF EQVVMELERD TISYSLHSAR YISDPDGIMI QFQVEPEKYA AAVEWIRTMM
FDSIFDPQRL KASVTKALAD IPESKRDGKS MASEVNAAIH MEKSSLAVAK RVLVRAVYLK
RLKKLLEKEP EKVVGWFNTV RDSLFTFRNL RFLVTANLET LPDPLTTWDT LSKSLTVAEN
MIEIPKPVSL LNDEGRNPGS VGAIIVPMTT LESSYSVSTA QGLASFDDPR LASIMVAIGY
LEAAEGPLWN AVRGAGYAYG VYFSRDINSG IISYHVYRSP DAYKAIKASK EAITKIAKGE
VEIDRHLLEG TISQIVVMFA DEQSTMPSAA QQNFVQGVVR GLPKDWGKEV LRRVRAVTED
EIKTALLETV LPCFEPGKSN IVVTAAKIMQ EGMETAFKGM GYKVQTHELS YFHDDYGLKP
EEGEEEESSE EDEGLEGSEG SYDSDESYDD
//
