ID A0A395GIS6_9EURO Unreviewed; 1652 AA.
AC A0A395GIS6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=FHA domain-containing protein {ECO:0000259|PROSITE:PS50006};
GN ORFNames=BO80DRAFT_460211 {ECO:0000313|EMBL:RAK94938.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK94938.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK94938.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK94938.1,
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KZ824511; RAK94938.1; -; Genomic_DNA.
DR STRING; 1448316.A0A395GIS6; -.
DR VEuPathDB; FungiDB:BO80DRAFT_460211; -.
DR OrthoDB; 276824at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd22699; FHA_PLM2-like; 1.
DR Gene3D; 1.25.40.180; -; 3.
DR Gene3D; 4.10.80.160; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR InterPro; IPR039762; Nmd2/UPF2.
DR InterPro; IPR007193; Upf2/Nmd2_C.
DR PANTHER; PTHR12839; NONSENSE-MEDIATED MRNA DECAY PROTEIN 2 UP-FRAMESHIFT SUPPRESSOR 2; 1.
DR PANTHER; PTHR12839:SF7; REGULATOR OF NONSENSE TRANSCRIPTS 2; 1.
DR Pfam; PF02854; MIF4G; 2.
DR Pfam; PF04050; Upf2; 1.
DR SMART; SM00543; MIF4G; 2.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT DOMAIN 110..163
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 28..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1605..1652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1469
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1652 AA; 185695 MW; 0030BBCB6966DF33 CRC64;
MESSPPRSSS LAAPVAGVKR PAALLPAFEP LSSSPSLPRP QKRVARDNHG IVSTYPTPVP
TSSTHIMSSS PPRMALPRTV SRRTFTSSSS ERTPLSAVPT IMLSESGEPI LMGRSSASCH
HQLAANRMIS RVHVKATYKP APNPFDPDRV EIMCMGWNGI KLHCQGKTYD LAKGKTFTSD
IKDADIMIDV HDARVLVQWP QHDRKDYAST DSEQTWEEST PKRAAQSRQS LHESPNVERQ
RLASPVSPSP AAKSLVPPSS PLYTPTRSRN AVVVYEDEAS PVRRNNEDPL VQVTRKSSIV
EDLFQSSQSS DLSDLSKQDE FSDHDEENDP IIHSFGPFGD NILPRMASFT ADESPLRPAR
PRNQASAQPL QPAKRQPSKA SESVESLTTK LEPLDESFER VQNHAVNQLA FSRLSSTPFS
TILNNLPPTL WKRDSHHREG PSKDEIRAIL DTTKCIGKVA REGKDAAGKP LESEYYYIPD
YDEDDMRREA VVHDLRKPGL RNCRKQHKVR DLRLLNERVW AGESDVFPTS KSLDSALKKN
TAFIKRLRTG INAAAQQTFL TDIRTLSLHK YLSEIISACY EGLCKLKSPG EIATGVEITS
ALHQRFGPGE FTRQIGWLLG RGLSTPDKGQ LKALSQEVRE REEKERLSRH RVLLRVVTEL
WLVGVLKTLD DIEKPDDVGA KGKDGVVGIG AKATDGPVKR VPPAAGKDGD RDPEPFPLEV
LKDLLGHDRD HSNLPLAVLF VKSFSWDVLG VKMVEEGRKT VEADGATTSA SETVNGGGEG
VDETGDAEND PPLTSEKVQL RFKHILNRYL EDVKAHVVRD QRALAAQSRR NAEAYVKSGE
IFEDRQANFE RQTKSLERLV ANTQVLCEVL GVEMPALAEK EAADAGAGGG IGLVKASEYL
RGQGEGAGIW EDEEERRFYE NLVDLKGKVP AVLLEDGKKK KTETDEAGKR KDEGADEKPE
PTGQAQQSEE KTSDADDQSM AIASKTVGAQ VDALLAKLPD LQTKDQVDQL ALDFCFLNSK
ASRNRLIKAV SDVPKGRIDL LPLYSRLVAT LGQYMPDIPQ GLTTYLDEEF RSLQRRKSKE
FLGQVRMSNV RYLAELTKFG VVPEHIIFHC FKVSLDDFSR MNIEIIGHLL ENCGRYLLRN
PDTAPRMASF LETLGRKKTV QHLGQQERMI IENAVYYVDP PPRPAIQQKE RTPMESYIRR
LVYLDMNKRN YTKILKSIRK LHWEEQDVVD ILERVFSKPV KVKYGNIHLL AILVSALYRY
HQDFVIGVVD NILEQITLGL EQNDFKFNQK RVAEVKYLGE LYNYKMIDSP VIFDTLYRIV
TFGHENGTPM PGKINPLDLP DDFFRVRLVC TLLDTCGHCF DRGSAKKKLD FFLTFFQYYM
HTKDPLPMDI DFLVQDTFSM TRPQWKLATD LAEATQTFSD AVAQNFKTQD SERPAEPDED
DAESSSSDEG LEEDAIPEAE EDQESSDEEV SGPNEQNGDS ESEEEIFVTR QEEERDPEAE
AEFDREFEKM MAESMESRKF ERKGVFDIPL PMKRSGREAL LENAPSEAPK PIANTMAFSL
MTKKGNKQQT RTIDLPSDST FAVAMRSQQQ ADREEQQRIK NLVLNYEMTN ETETNTEAAE
KRSPHRDTRM DKSSANRTAF RSRKLQLSDV NW
//
