ID A0A0D1DSG9_USTMA Unreviewed; 1023 AA.
AC A0A0D1DSG9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=UMAG_04376 {ECO:0000313|EMBL:KIS67274.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS67274.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS67274.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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DR EMBL; CM003153; KIS67274.1; -; Genomic_DNA.
DR RefSeq; XP_011391079.1; XM_011392777.1.
DR AlphaFoldDB; A0A0D1DSG9; -.
DR SMR; A0A0D1DSG9; -.
DR STRING; 237631.A0A0D1DSG9; -.
DR EnsemblFungi; KIS67274; KIS67274; UMAG_04376.
DR GeneID; 23564578; -.
DR KEGG; uma:UMAG_04376; -.
DR VEuPathDB; FungiDB:UMAG_04376; -.
DR eggNOG; KOG2194; Eukaryota.
DR InParanoid; A0A0D1DSG9; -.
DR OMA; HFWIEAE; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000000561; Chromosome 14.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF54; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1-RELATED; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT TRANSMEM 82..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 508..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 648..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..432
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 111350 MW; 2454DA76EF379C16 CRC64;
MPSNKRRGNT PKKAATPTAA PAVASSRTPS NGVTLADATS TNGAPMTSDQ AAVAAQYRQY
AQAKRARQVD PKNYTRTPKS GLLVLFVLGL LSLLGSITLY FHYKLPSPRG PTAVIASGVT
PADAAAYHPP IAGSEAANTS GESPKFYHLF SEANAVSVMH HLSVDIGYRI VGTKEHLDAE
NWLENVLRRY EGHHNTGTAD SPGQTQVEVY KQIGDGAHRF DFMSNVVWKR YYSMSNLVVR
ISDGTDESKA NSLLLNAHLD STCPSPGGAD DGIGVAILME ALRVLTLPNT GRRLYNSVVL
LFNDGEESLQ DASHLYITQH NQTNAGVKAV VNLEACGTSG PELLFQATSA EMIEAYSHVP
HPFGTVLAND VFSTGLILSD TDFRQFVEYG NNLSGLDMAL VGNSYFYHTR KDIPQYLEPG
ATQHFGENTL AIIEHLCLKN SSHTLLRNIE PHQTRHTLPI YFSIANRFFV LISNKAFKSI
VMGLSAFVNF QLSSVVRSES AISALNLTIL SALSAIVSII GGVLGANVVA VIMTRAFGKG
MSWYSHEFFA ILLYAPPAVA GVLIVQLLTA KLCKPYQRPY LERSSLSGLG IFFNLGLLGM
NAFGIGSAYL MALSSLTFTL ATTLNDFVLI GVGQIEDKLI APDKRVSAYI YPLMTIIPGI
VGAEGMASFL DLFVPLTGRM GEISPADHII ASIVAVLSFL SLPFAIPLAH RYTSENLQRT
ILGLLAVTAA VMAVFASPGW KPFDEAHPKR LFVHQVENIT SNQWFMNVGA ADPAPGFKAL
SDELQSQFGI SSESQASLME MNDYNPDFDI LYPVSAFLTP YKFQLPGPPA SFSTKYADPA
PETYHFTVKA VNEVIDLEAR TRSLTLEMNH PGVIWSVVAF DAEILSWNLP SAPPAGYQRH
HLKSVARHGI YSWSIDLVLR LEPDQLAAAK PRTSSRIIDK LKKSAPSSGR LVKLDSTEPR
DASKLWIDAS GLVADEMFPQ HKSNTAADRP AMNTFIQMDR YMQDNHPEID VMMLTVVAGV
FEA
//
