ID A0A9P6QVG6_9FUNG Unreviewed; 1314 AA.
AC A0A9P6QVG6;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 08-OCT-2025, entry version 11.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=BGZ97_002126 {ECO:0000313|EMBL:KAG0302892.1};
OS Linnemannia gamsii.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=64522 {ECO:0000313|EMBL:KAG0302892.1, ECO:0000313|Proteomes:UP000823405};
RN [1] {ECO:0000313|EMBL:KAG0302892.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NVP60 {ECO:0000313|EMBL:KAG0302892.1};
RX PubMed=33364917;
RA Vandepol N., Liber J., Desiro A., Na H., Kennedy M., Barry K.,
RA Grigoriev I.V., Miller A.N., O'Donnell K., Stajich J.E., Bonito G.;
RT "Resolving the Mortierellaceae phylogeny through synthesis of multi-gene
RT phylogenetics and phylogenomics.";
RL Fungal Divers. 104:267-289(2020).
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:KAG0302892.1}.
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DR EMBL; JAAAIN010001457; KAG0302892.1; -; Genomic_DNA.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000823405; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-ARBA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd00027; BRCT; 1.
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; IPR013939; Regulatory_Dfp1/Him1.
DR InterPro; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_sf.
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:UP000823405};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 598..647
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 49..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1067
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1314 AA; 144456 MW; B37B7B3B6F0CE1CC CRC64;
MADRPLNPTL QRAPLQESRA HSNINQLRQH HGMNTLNTHQ GLVAKSGQDA GFTRSSSTNI
PMKPIMAPHS EKDPSRQRIA LQQKPFSVSH AQNIKALPGS ARVASNSMLK IKPVPFPGFA
STTPSYTRSD VNIEIQSRPH SQHAVDHAHH LPQPQDTEPR SHARHKNRVS AEYGSAEWTQ
QMANVLPRCR FYFDSVEPAM IKKISDVVRR HKGTMTSFFS NEVTHVITTR PVPDESVLER
IKSQDNAGQL LTTQPDPRRT TTRPLSQHIP NAEMGILVKA LSLGIKIWTL ELTLKLLAPL
APGLVKQTDD RKLKDMLQYE KVHGVATVHI DNSTKPDFYA FQGKYVLVDD TTGYYRTIMA
YDFTAKPSST GKQPWPRLYI QESDRSPFCF IEPVVKASER PAGARGDKGQ GIKVDKDHTN
VVRDAQPADD QKLSPSAMAS GLVNSVTSNI ISTTTSTAPK PAAVNPQQDR RMEQLEKRAL
NATKVDAGVP NDFAQKPEFA RPLDIIRPDT GDATVGNATQ YIVTGREAIT GSGSKMQPPT
LPTRQHSGLA ISANNERAVA QGPDTMDPMR REPTDARPAH LIAEALVSHT AKHKEAKDYR
KQRYCENCRG FFENFEKHIE SPAHRKYAHD ASKFAQLDIL LAKLQRKPKI TSGLSELPTN
ASVPPKSELK DFSSSTATSE MPVTLASEPV CEDNTQEAMD ITPPTHELPV AVNMAATHTV
QEGSQGRDEI VQETQGTAEK SHVRRDDEED EGIVEDMDEE SIQGDMEDQN TVTLQPSRNA
EEIDDIADEL SSEMSQLGLA ERGADLFNDQ AVDAESGVPF IGQEEEETVV VKETPSTLLE
GDMAAAPTSL QKVLRHEFRL PHSDRSGHSD SNITSQLETD TTQPDDRFLE CSASVTASAD
DGLSTPVRLR FDTSSTVASP NAPRTINRAH FSPEALHESD REGSDDAVTL VKSPSAGRGL
FGRNQGVGLR NGLFAPNRFA EDSSSFSPSK DITSGLYKGA LKRKLENVLA EERAADRAQF
RVGVAVETPD TPRLSGLPAC MSVLPDIGAL SQQLSDSSST LSTPQRSENW ANHAPSRPPT
LPSSPMSPMQ QNEPLELLFQ ATPPPASQSH QPAVDRSHQR QAQLVSGYFH PSLSSQLECE
SPQSCRTELR RNDHSTGPQQ TPPPLQSQRR LQQAGTPIIP FQDYLMKGDA LEMGTKPRRT
EPVVTSRREP EAPVSQSSPI AFSSPEGSHS PVDAVNFMGP SYGFSSPTQS PSRRAQRTYF
PVMTHAEQEK ERVYQHYHGN QLPEPAGGQK KMRSSSSLAE AYEEYGEGAM VFIE
//
