ID A0A1J9QRE1_9PEZI Unreviewed; 1251 AA.
AC A0A1J9QRE1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Nuclear cohesin complex subunit {ECO:0000313|EMBL:OJD30578.1};
GN ORFNames=BKCO1_5800067 {ECO:0000313|EMBL:OJD30578.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD30578.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD30578.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD30578.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJD30578.1}.
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DR EMBL; MNUE01000058; OJD30578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9QRE1; -.
DR STRING; 236234.A0A1J9QRE1; -.
DR OrthoDB; 5354237at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:UniProt.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199:SF0; LD34181P-RELATED; 1.
DR PANTHER; PTHR11199; STROMAL ANTIGEN; 1.
DR Pfam; PF21581; SCD; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS51425; SCD; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000183809}.
FT DOMAIN 365..450
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 661..688
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1062
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1251 AA; 137477 MW; 06411DCC4A4471CA CRC64;
MEPSSPDADA QQTRSSPADN NETSAATRRK SGRVTRKPET IYSSAATPAT KRKRGADREA
DASDDDDIED EDDEDEDESS EGDADDEELR DKRRKKKRQS AAKAKSTPQR KPATKKSKPN
GDTMSLAIRP ATKAKKPRKP RPSKVAAAGE VGGLYGDVFA GNQSLNDVAA QWVRRFGEDN
SEEMAALVNF VLRCAGCDLK IDAHDVENPD GVPGKLGDIQ EEYQAQNIVE YPLIQKGKGS
ANFRHNLIEF FTSLIETLAQ SELLWTNPII VENIGLWINT MSSANSRPFR HTATLVSVTI
SSALCMVGAK LIEANANAMM LKETEAKKSG KNKARLAEME KKIEAGNERV EALNGMIKNS
FDEVFIHRYR DVDPRIRTEC VTGLGNWIMN YPDYYFDGQH LRYLGWVLSD VHAPNRLEVV
KQLQRLFDDA DKLGGLRTFT ERFRSRLVEM ATQDADAHVR AATVELLDIL REAGLIEPND
IDSVGRLIFD ADPRVRKAVV DFFAENIAEI TEQKIDELGG KEALDEALEG DEDYENPRLE
WLVLKSLVES LAAYDEDHTL PSQIERVPMS NSYMLIAGGM ASRIGVAAEA LYDELPEIQE
WEVIAGYLLF DHSQSSAGAQ QNGTTDDPEA LLKQVCKLNE KEETVLLDIL NASVKLKLTR
AVEAGKDKKK TKRERQELEE EQDTAARHLA ALIPRLLNKF GAVPDAASAV LRLEHVLNLD
VFEELRQDST TYSRLLDDIN KQFMSHGSEA VLVEASRALL HAKSYEELSE ITEGKVQALW
EDTVAALHAL KKGKGLMTRG NLSANVLSAV SNTVLRISKL ASISDCTEQL EAPPPVVAPK
KQRSRKSQDA NPAENAIVIL IELLRRGVPN SSTDTSLSAL EDAVVTNSAR SLLFYFMWKV
RSWDRSILTT GTVPPKDVEA IAERRDGCVA ALEEVIRKRQ GADELRLAAA GVLLDLCTLF
TTLRDAQAKR DAKRLRTANG DAAAGGMDVD EDESRDDFMA LLLGLNKDTQ KSLLQLLAAT
EKHFAKKSRR NIDVAEDDDP IDVDDDPESS DEEDDAADEE GAEGASAQEI LLAEQRLCEL
ASKLVLAILG GVVDGSSDDD EEDEEEAADR DDGPGPVRRR LERNRNKLGP NFKEVVAYLD
VGTEKGPKKG KGGGAAARAK NRSVSAPAPN QQKSAAASGG GKKSEKSNEF VGEETDEEDE
EEHHDEEEEL RREGLVENPD QEMEDEGAAG EEGDGANAGA QEADEESVIG D
//