GenomeNet

Database: UniProt
Entry: A0A100I7Y5_ASPNG
LinkDB: A0A100I7Y5_ASPNG
Original site: A0A100I7Y5_ASPNG 
ID   A0A100I7Y5_ASPNG        Unreviewed;       722 AA.
AC   A0A100I7Y5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=MIF domain protein {ECO:0000313|EMBL:GAQ36345.1};
GN   ORFNames=ABL_01621 {ECO:0000313|EMBL:GAQ36345.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ36345.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the CENP-X/MHF2 family.
CC       {ECO:0000256|ARBA:ARBA00009359}.
CC   -!- SIMILARITY: Belongs to the MIF family. {ECO:0000256|ARBA:ARBA00005851}.
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:GAQ36345.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BCMY01000002; GAQ36345.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100I7Y5; -.
DR   VEuPathDB; FungiDB:An01g10680; -.
DR   VEuPathDB; FungiDB:An01g10690; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1083140; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1132368; -.
DR   VEuPathDB; FungiDB:ATCC64974_14910; -.
DR   VEuPathDB; FungiDB:ATCC64974_14930; -.
DR   VEuPathDB; FungiDB:M747DRAFT_297830; -.
DR   VEuPathDB; FungiDB:M747DRAFT_333524; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 3.30.429.10; Macrophage Migration Inhibitory Factor; 1.
DR   InterPro; IPR018552; CENP-X.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR001398; Macrophage_inhib_fac.
DR   InterPro; IPR014347; Tautomerase/MIF_sf.
DR   PANTHER; PTHR28680; CENTROMERE PROTEIN X; 1.
DR   PANTHER; PTHR28680:SF1; CENTROMERE PROTEIN X; 1.
DR   Pfam; PF09415; CENP-X; 1.
DR   Pfam; PF01187; MIF; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   SUPFAM; SSF55331; Tautomerase/MIF; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          425..452
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   722 AA;  79437 MW;  95EE8F982810B601 CRC64;
     MTARRHRIDF SLRRRRNDLS NTSSGSISPP VPVLQSPVTF QAFASVNVSE ATLKQKNKLE
     RAPVRPSMFL EEKDDDEAPI SALTGGAPLD VKPAHVERKS VEEKPMTRTK SQYFEDAFST
     RGPLTSPRTQ ISQDSVVVVE IKVNTKVKEM ESLVSNISSH MARIFQKSET LMMTTIQDDA
     CIQFGRVNLP AYLMKVFALP YLIAPITNLR STILIQAALQ EILHVAPNRG VILYIPIPEE
     NFATNGVTMM GEIARLERSS PDHGSGLFKT VSRTMSRRLK STSSQSAPIS VATTSSWACG
     GTQAPSPGKE SLASDATDSD VKSKSDACNC RGTWGKGIAR VFRSNYPAAY EVYRSYCRQF
     SSKPRYDTVT TSDGTRKARL PEGTALIIPP QKRDHENDRR KRHWIICLFT SRGLGRMVSP
     ENIVLENTEL AIADMKKQLD RIEDQKGSLL ELWSCRFNSG LFDSKSPDHA SRTRASAQED
     QIPATNTPYH QLTTKVTNLD TKTQHTMPPE RKPAQKRRQL PFKPPSRTSS TAAAPASSSS
     TTSKPKGKAT TKSTTTTAAS KRGPKPKEAS AKASSSKSAR PRPSSPSPAD SDEDSNNDND
     NASSSPARSD ASSPEPEPEP DYILAEIIHK DQPSDDVLTN DPVIPPKLLT RLLHHHFQNE
     KTKIAKDANT VVAKYVDVFV REALARAAFE RTEAVGKGAS VGDGFLEVED LEKMAPQLVM
     DF
//
DBGET integrated database retrieval system