ID A0A395GZA9_9EURO Unreviewed; 574 AA.
AC A0A395GZA9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=NIMA interactive protein {ECO:0000313|EMBL:RAK99363.1};
GN ORFNames=BO80DRAFT_410638 {ECO:0000313|EMBL:RAK99363.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK99363.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK99363.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK99363.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ADIP family.
CC {ECO:0000256|ARBA:ARBA00009291}.
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DR EMBL; KZ824447; RAK99363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395GZA9; -.
DR STRING; 1448316.A0A395GZA9; -.
DR VEuPathDB; FungiDB:BO80DRAFT_410638; -.
DR OrthoDB; 2726628at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR InterPro; IPR021622; Afadin/alpha-actinin-bd.
DR PANTHER; PTHR46507; AFADIN- AND ALPHA-ACTININ-BINDING PROTEIN; 1.
DR PANTHER; PTHR46507:SF4; SSX FAMILY MEMBER 2 INTERACTING PROTEIN; 1.
DR Pfam; PF11559; ADIP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT REGION 246..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..142
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 393..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 63782 MW; E54D97019434CCE9 CRC64;
MEPQNLEAAS TYINNVLLAR GLLKGGRPIE FANPEDEDGG SAATMGRIIN LVNDLVLRRD
REAEHRENLA TTIRTLRVED SQKTAELEKV KTKASELSRS LALAEAQERA LKSNVASADA
TIRGLKEQVQ RMKTTIQQVR AQCANDIRKR DLEMQKLKSH LAERQRGKRE GLSMTTININ
PAASQTSRSR LTAGGEGIND PGYSLKQETN DFLTELCQTL SDENDTLISL ARNTVETLKD
LQGLSQAEED DKYSTGVASV GPSRSVQGSV TALPTSCDEL STQMDHVLEH LRTLLTNPSF
VPLEEVEMRD EEIKRLREGW EKMEGRWSQA VTMMDGWHKR MADGGHSVQA EELRRGMDLD
LRLDIAKALS KDGEREPTIQ SPIFEDQQAE EEEEKAAEKS TTESNRRSPT PKKAPRSTRE
TRSKRASQAL KERSDNIMTG RSPRKVSFTT GLQDSPSVPS VDDETLQVKA HQSEAVTRRS
SRRKPESKVL SRPQPKDSRL ATAVQGSTSQ ARLSVPQKLA AVESEARAAE QARKEGESRK
RGRALKGSSK GHRDRRRSTL TSDELGELMG MPAK
//
