ID A0A067BXU4_SAPPC Unreviewed; 413 AA.
AC A0A067BXU4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA damage-inducible protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=SPRG_11662 {ECO:0000313|EMBL:KDO23349.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO23349.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO23349.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO23349.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
CC -!- SIMILARITY: Belongs to the DDI1 family.
CC {ECO:0000256|ARBA:ARBA00009136}.
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DR EMBL; KK583255; KDO23349.1; -; Genomic_DNA.
DR RefSeq; XP_012205998.1; XM_012350608.1.
DR AlphaFoldDB; A0A067BXU4; -.
DR STRING; 695850.A0A067BXU4; -.
DR EnsemblProtists; KDO23349; KDO23349; SPRG_11662.
DR GeneID; 24133684; -.
DR KEGG; spar:SPRG_11662; -.
DR VEuPathDB; FungiDB:SPRG_11662; -.
DR OMA; QIGNDHL; -.
DR OrthoDB; 1332686at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05479; RP_DDI; 1.
DR CDD; cd01796; Ubl_Ddi1_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR033882; DDI1_N.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12917; ASPARTYL PROTEASE DDI-RELATED; 1.
DR PANTHER; PTHR12917:SF1; AT13091P; 1.
DR Pfam; PF09668; Asp_protease; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030745}.
FT DOMAIN 1..75
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 372..413
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 336..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 44422 MW; 916FE1F684B74C8F CRC64;
MQLTVTYEEH VLQVEVDAAD PIENLKAIIE AEINLPMARQ ILVLNGRQVN PDHTVGQAGI
QNNDLILVTT PATAAPPPAP AMGAARLGGP ATQARAGMTL QDIPPNCSAE LLIEIMRLNP
QLLRQVESGN APMAAAIRAN NVSEVRMLLM KQYMEAASRK YQEEQELIAL NANPFSEEAQ
AKIEEAIRLG NVQQNMEIAM EEMPEAFGRV SMLYIPTVVN GTPVKAFVDS GAQSTIMSSS
CAERCGIMRL VDRRYAGQAV GVGTAKIIGR VHMAELKIGS IFYNCSFTIL DQQGVDFLFG
LDMLKRHQCC IDLHRNLLVL RDPTGSHEVS FLPEHEIPVS GHDAPPTTPL PSTPTPAPAA
PSTPAPTTPG LSPDQAAKVA QLVAFGFPEG PALQALQSCS WNVDIAAGLL FEN
//
