ID A0A0C9MKN4_9FUNG Unreviewed; 922 AA.
AC A0A0C9MKN4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA damage-inducible protein 1 {ECO:0000256|ARBA:ARBA00021491};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=MAM1_0021d01861 {ECO:0000313|EMBL:GAN02418.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN02418.1};
RN [1] {ECO:0000313|EMBL:GAN02418.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN02418.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable aspartic protease. May be involved in the regulation
CC of exocytosis. Acts as a linker between the 19S proteasome and
CC polyubiquitinated proteins via UBA domain interactions with ubiquitin
CC for their subsequent degradation. Required for S-phase checkpoint
CC control. {ECO:0000256|ARBA:ARBA00003231}.
CC -!- SUBUNIT: Binds ubiquitin and polyubiquitinated proteins.
CC {ECO:0000256|ARBA:ARBA00011128}.
CC -!- SIMILARITY: Belongs to the DDI1 family.
CC {ECO:0000256|ARBA:ARBA00009136}.
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DR EMBL; DF836310; GAN02418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MKN4; -.
DR STRING; 91626.A0A0C9MKN4; -.
DR OrthoDB; 152877at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd05479; RP_DDI; 1.
DR CDD; cd06609; STKc_MST3_like; 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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033882; DDI1_N.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR036353; XPC-bd_sf.
DR PANTHER; PTHR48012:SF10; SERINE_THREONINE-PROTEIN KINASE KIC1; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF09668; Asp_protease; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF101238; XPC-binding domain; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000313|EMBL:GAN02418.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Protease {ECO:0000256|ARBA:ARBA00022750};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Transferase {ECO:0000313|EMBL:GAN02418.1}.
FT DOMAIN 1..70
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 207..287
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 378..413
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 422..672
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 73..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 448..475
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 699..714
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 922 AA; 102310 MW; 93B1305AD9ABF931 CRC64;
MLLTVTTDGE EIYNLDIDNQ MSIEDLKALL EAESGVPPQS QHLFFSGKKL NEAKKTLEEY
GVGENEIIHM QQLAPQQQGQ RQQGQASSSG DSNFDLMRQH VLRDPRLLQQ LESTNPELAH
AARNDPARFS AMVQQIEQNR RSAEVQKSQL AALNDDPFDV EAQKRIEDAI RQENIAANLE
AAMEYNPESF ARVTRLYINV EINNKHLVAL VDSGAQSTVI SPETAESCGL MRLLDTRFSG
VAKGVGTAKI LGRIHSAQMR LSQNLFLTCS FIVVEGKGSE LLFGLDMLKK HRACIDLRKN
ALTFDSCDIP FLAEHELPEK QRRMEIHGSD EDETAIEGRT VVPQVSTPPP VPSASPAGSV
STTTAIPTLN TASAPSSTYP EKDIKLLTDM GVSRQEALNA LEMAGGNPEN TANQSTDPEV
YYLKQERIGK GSFGEVFKGL DRRTNKPVAI KIIDLESAED EIDDIQQEIA ILSQLDSPFV
TKYHGSYLKG TGLWIIMEYC SGGSCSDLMK MGTIREEYIA IIIKELLKGL DYLHNEGKLH
RDIKAANILL SSTGEVKLAD FGVSGQITAT LTKKNTFVGT PFWMAPEVIK QSGYDYKADI
WSLGITAIEL ANGEPPYAKM HPMKVLFHIP KNEPPTLGPP HSKAFRDFVS MCLQTSPANR
PTAKDLLKHK FIKSSKKVAY LTELIEGHER WISANGRDDD STEEEDNVEE DDADGWDFGT
VKQAPPQLSK PPLQQMHHSP SQYSVNSFST ENKYQQQPPQ QLPRTVSRNQ VTPQQQQQPP
PSSRVNEVTN KLQQTGFRHS TSEYEDVNQS TVRAAEIGAY PRSNKRSSMI QQPVVSNPLP
PLPNKSPSTR SISTVASSRQ QQQANDTAFL EMILPMLDRL QKNCKNHKSL AAVESLQKSL
VSVERELPGT VKALFEDVSQ LL
//
