ID A0A3F3Q2B8_9EURO Unreviewed; 1033 AA.
AC A0A3F3Q2B8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=NIF-domain-containing protein {ECO:0000313|EMBL:RDH33127.1};
GN ORFNames=BDQ94DRAFT_159785 {ECO:0000313|EMBL:RDH33127.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH33127.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH33127.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH33127.1,
RC ECO:0000313|Proteomes:UP000253729};
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 (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ852048; RDH33127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3Q2B8; -.
DR STRING; 1341132.A0A3F3Q2B8; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR46652; LEUCINE-RICH REPEAT AND IQ DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46652:SF3; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 9 ISOFORM X1; 1.
DR Pfam; PF12799; LRR_4; 3.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00364; LRR_BAC; 3.
DR SMART; SM00365; LRR_SD22; 9.
DR SMART; SM00369; LRR_TYP; 6.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50969; FCP1; 1.
DR PROSITE; PS51450; LRR; 9.
PE 4: Predicted;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 411..566
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1033 AA; 115149 MW; 2D6424ACB0848179 CRC64;
MLGGSLERDS SPSNSKPTTG EAPMPIATSP PDSNPEPSPQ DQPATTDASP LSNNVEPTNA
AQESVAPAQG SVDESAATSA DAPKKHHLLL PISSRASLKA DRQSTLDKSQ DTAHDDSENT
LRGSKRSIFK GRRDRSRGSS MRSRRQNQEG ASMEEDKSAS PDLRDPAKPE RRSKVSYRLF
AFLSCCSSPS DDSEDPAIPV KRTSRQPSVP HTQATPEKAD ANAGDSSTAE SKDPSYYRDE
KPNMTVTSNQ SMSQVDEERT VTTSEQGAQL DGATVPSGPA ETEKVPALPQ DSADSQGLGV
GQSTQPSTTT AEASAVASEA GEPSQKTEEQ IISTSTEKAQ DAPTAPIELD ELPKPPASEN
SYDDEKYTSH DEEATVLPAE LPPPTGPSGH HVDTMLEETQ QQFLLPPPLP HLRDRKCLVL
DLDETLVHSS FKVLERADFT IPVEIEGQYH NIYVIKRPGV DQFMKRVGEL YEVVVFTASV
SKYGDPLLDQ LDIHNVVHHR LFRDSCYNHQ GNYVKVLGRD LRDTIIIDNS PTSYIFHPQH
AIPISSWFSD AHDNELLDLI PVLEDLAGAQ VKDSCFLVFE VSFLVAYRRR QSWTSLHTRA
HTPSLNMKDK NGWDGKLRVE PKATITNPEA LEDPDYSDSD APPVEEIEAD EDLLEDEDPD
AERLCFRQNQ ISRIEFPTEV AKSLTELDLY DNLISHVKGL DEFENLTSLD LSFNKIKHVK
NISHLVKLTD LYFVQNKISK IEGVETFTSL RNLELGANRI REIENLDNLK ALEELWLGKN
KITELKNLDG LSNLRILSIQ SNRLTNISGL ANLKNLEELY VSHNAITDLS GLEENTSLRV
LDFSNNQVSK LEHLSHLKNL EELWASNNQL SSFDEVEREL RDKENLQTVY FEGNPLQTRA
PALYRNKVRL AIPHIMQVDA SKSYRLYLLM LTEILTKTKS RYTYMYNPPT QPKPMQYYTE
YENKSYNHQS TSLHFVPSPS PSPSPLSFPF SLSIPNRYNP IKLFPPNLHT SRSSILFTRS
GTCAFLLIGP SAK
//
