ID C1H3Y9_PARBA Unreviewed; 1855 AA.
AC C1H3Y9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Meiotically up-regulated gene 62 protein {ECO:0000313|EMBL:EEH34433.2};
GN ORFNames=PAAG_05482 {ECO:0000313|EMBL:EEH34433.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH34433.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH34433.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN294005; EEH34433.2; -; Genomic_DNA.
DR RefSeq; XP_002792753.2; XM_002792707.2.
DR AlphaFoldDB; C1H3Y9; -.
DR STRING; 502779.C1H3Y9; -.
DR GeneID; 9095988; -.
DR KEGG; pbl:PAAG_05482; -.
DR VEuPathDB; FungiDB:PAAG_05482; -.
DR eggNOG; KOG3628; Eukaryota.
DR HOGENOM; CLU_000737_0_0_1; -.
DR OMA; LVWTYWT; -.
DR OrthoDB; 2784789at2759; -.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 4.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR010506; DMAP1-bd.
DR PANTHER; PTHR22754:SF32; DISCO-INTERACTING PROTEIN 2; 1.
DR PANTHER; PTHR22754; DISCO-INTERACTING PROTEIN 2 DIP2 -RELATED; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF06464; DMAP_binding; 1.
DR SMART; SM01137; DMAP_binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR PROSITE; PS51912; DMAP1_BIND; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002059}.
FT DOMAIN 1..101
FT /note="DMAP1-binding"
FT /evidence="ECO:0000259|PROSITE:PS51912"
FT REGION 71..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1734..1855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1674..1716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1816..1832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1841..1855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1855 AA; 205989 MW; BC00CBDE57A874A9 CRC64;
MAEDNPELQV ALRQLDQEFD DGEITQKGYE KRRTLILSHY LSTNNGDPTD RGLRIANPGN
AANRRASHLG LYSPATSSQG SRPASSTLSD ERQQSESLSA NFIGGEQERV KGDQMAGMNA
MADAHYQMQA GNQLAQIRER ELGLSFGVER NPSSASNDSL FLPRGQAPSG NNYDTSRSGT
LTSHNYAFNP ADQPSYGEPR TSTYSPPGGN GGHMRQSTML DSQQAFFSDF AGQQMEDSRN
SYGGSFQRYS TQTEPFSPIA NMAPPLMNTA DLPQGMDVDH LLPLEPRDIP FDVHDPHDPS
MSMSKFDNLP AVLRHRARTH PKQPAYWVLD QRGKEIASIT WEKLGSRAEK VAQVIRDKSS
LYRGDRVALI YRDTEIIEFA VAILGCFTAG VVAVPINNLE DYASLNVILT STQAHLALTT
ENNLKTFQRD LTTQKLNWPR GVEWWKTNEF GSYHPKKKED IPALVVPDLA YIEFSRAPTG
DLRGVVMSHR TIMHQMTCLS AIVSSSNPGG NTRQARPHGE TLFSYLDPRQ SIGMILGVLF
TVYGGHTTVW LEALAVETPG LYASLITKYR ATLISADYPG LKRAVYNYQQ DPMATRNFKK
GSEPNFSSLK LCLIDALTVD PEFHEILADR WLRPLRNPRA RELVAPMLCL PEHGGMVISV
RDWLGGEERM GCPLTHEMDP APQVESAETK KEEKVESVKT GFGSSLIGGT AVPTQKQSKS
NRVELNQVLL DKEALKNNEV VVLAMGEEAR KQAETMPNTV RVGAFGYPLP DATLAIVDPE
TGLLCTPNII GEIWVDSPSL SGGFWALPKH TEAIFHARPY RFQGGSPTPV IVEPEFLRTG
LLGCIIEGKI FVLGLYEDRL RQKVEWVENG AKSTEHRYFF VQHLIISIMK NVPKIHDCSA
FDVFVNDEHL PVVLLESYAA STAPTTSGGP PRQLDIALLD SLAERCAEIL YQEHHLRVFC
IMITAPNTLP RVTKNGRQEI GNMLCRKEFD NGSLPCVHVK FGVERSVLNL PIGVDPVGGI
WSPMSSAARL GALVMQDKQY SGVDYRDVVM DDRTSTPLNN FTSIVDLLQW RVSRQTEELA
YCSIDGRGKE SKGITWKKFD SKVAAVAMYL KNKVKLKPGD HVILMYTHSE EFVFAVHACF
CLGVIGLPMA PIDQNRLSED APAFLHLIAD FRVRAILVNH DVNDLLKVKS IAQHIKQSAH
VLRINIPPAF NTGKPPKQSH GCRHLGLTMK KEWLDSGRPA MVWTYWTPDQ RRMSVQIGHD
TIMGMCKVQK ETCQMTSTRP VLGSVRSTIG LGFIHTCLMG CYVGAPTYLF SPLDFATNPV
SLFLALARYK IKDTYATSQM LDYAMGSIAG KGFQLHELKN LMIASEGRPR ADIYQKIRLH
FAAAGLDRTA INTIYSHVLN PMIVSRSYMC IEPIELWLDT KYLRQGLIYP VDPDSEPHSL
RVQDSGMVPV STQIAIVNPE TCCLAHVGEY GEIWVQSEAC AKAFYGTKQE FDLERFRGRT
VDGDPSAVYV RTGDLGFLHT VTRPIGPGGQ PVEMQVLFVL GGIGETFEIN GLNHFPVDIE
TTIEKCHRNV VPGGSAVFQA GGLVVTLIEV TRKAYLASLV PVILNAILNE HQVVADIIAF
VPRGDFPRSR LGEKQRGKIL ASWVTRKMQT IAQFNIRDGE GFDSHLIDLP ERTRTTSKVP
STTEVGSRHP TPQSDLESHT PQRQQEPAAP VEQTTPTERV NSFTLPAVAP SLSPQAASFR
ENDEESIKNY NPTDFDYRLS FGDRSKNDFD DYEDDDEPME KPTRLAIVNP EESDNDDNTN
QHSSPAPRPL ALVGGVDNSN DSNNNTDNVN DKPQLDYDFD YDSFFSSNTQ GQDQG
//