ID A0A175WC01_9PEZI Unreviewed; 645 AA.
AC A0A175WC01;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE SubName: Full=Hsk1-interacting molecule 1 {ECO:0000313|EMBL:KXX80760.1};
GN ORFNames=MMYC01_203919 {ECO:0000313|EMBL:KXX80760.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX80760.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|EMBL:KXX80760.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RX PubMed=27231361;
RA Smit S., Derks M.F., Bervoets S., Fahal A., van Leeuwen W., van Belkum A.,
RA van de Sande W.W.;
RT "Genome Sequence of Madurella mycetomatis mm55, Isolated from a Human
RT Mycetoma Case in Sudan.";
RL Genome Announc. 4:0-0(2016).
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:KXX80760.1}.
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DR EMBL; LCTW02000051; KXX80760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175WC01; -.
DR STRING; 100816.A0A175WC01; -.
DR VEuPathDB; FungiDB:MMYC01_203919; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000078237; Unassembled WGS sequence.
DR GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IEA:TreeGrafter.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IEA:TreeGrafter.
DR GO; GO:1901987; P:regulation of cell cycle phase transition; IEA:TreeGrafter.
DR FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 6.10.250.3410; DBF zinc finger; 1.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR055116; DBF4_BRCT.
DR InterPro; IPR013939; Regulatory_Dfp1/Him1.
DR InterPro; IPR051590; Replication_Regulatory_Kinase.
DR InterPro; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_sf.
DR PANTHER; PTHR15375; ACTIVATOR OF S-PHASE KINASE-RELATED; 1.
DR PANTHER; PTHR15375:SF26; PROTEIN CHIFFON; 1.
DR Pfam; PF22437; DBF4_BRCT; 1.
DR Pfam; PF08630; Dfp1_Him1_M; 1.
DR Pfam; PF07535; zf-DBF; 1.
DR SMART; SM00586; ZnF_DBF; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR PROSITE; PS51265; ZF_DBF4; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000078237};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 582..631
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..21
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..102
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 72152 MW; 2D5793AEBDE3D11A CRC64;
MSTSIRRIPL SSNPNAANSP MRASAAALLA AKKGHSHAEV LREEPYGQPP PAKRQMIERS
VASPTPSRST RILVRRAVSR AASRATVGTG TSTSTTQRTS RAISRKSTEE DVNAMRQWHS
NIRARFPNMV FYFESIPDDV CSKLAKQVAR LGAREEKFFS IDITHVVTSR PIPSEKAPQD
GNEANADAER PQTIDPSLLN RNIDSTNSVR RKPVFDTVSK RRPIIQDQEV KPPKARNTDV
LHRARDMGKK IWSLEKLQKI LPMALDPEPN LSAFLGHGRE TVQSASKVSE KDDVLQLIRN
ERVPTFSSKD LYQLKEPYIY VYDIDEKTRP IMVREYQKVA DPKDGDWPQF RSASHGRCPF
VQDNYDFRGR ANREEARAKG RVAKVVAETA AADTKPAEAT QTNPKPATGK RTLTQMEDGH
NRGVAALRAN EPFDRSRVSN PPSLDFRSQN AFMSHAKVGR FLAGEPVASG VQPSNVTSAI
RSQMISSTTG GLGAKAGTSK EIHGLQRRVV LQKASTPALS QDLSSRRMAE MSHDSNTFTR
SASASMTTNR KLDTVDEEET ARQREKLRRT ASAPTTLPKQ NRDPKPGYCE NCQDKFPDFE
AHIVSRRHRR FADNDDNWAQ LDALLAQLKR VPRCRRHAEE TPIWQ
//
