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Database: UniProt
Entry: Q0CZN7_ASPTN
LinkDB: Q0CZN7_ASPTN
Original site: Q0CZN7_ASPTN 
ID   Q0CZN7_ASPTN            Unreviewed;      1823 AA.
AC   Q0CZN7;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=DMAP1-binding domain-containing protein {ECO:0000259|PROSITE:PS51912};
GN   ORFNames=ATEG_00847 {ECO:0000313|EMBL:EAU39493.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU39493.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CH476594; EAU39493.1; -; Genomic_DNA.
DR   RefSeq; XP_001210933.1; XM_001210933.1.
DR   STRING; 341663.Q0CZN7; -.
DR   EnsemblFungi; EAU39493; EAU39493; ATEG_00847.
DR   GeneID; 4355608; -.
DR   VEuPathDB; FungiDB:ATEG_00847; -.
DR   eggNOG; KOG3628; Eukaryota.
DR   HOGENOM; CLU_000737_0_0_1; -.
DR   OMA; LVWTYWT; -.
DR   OrthoDB; 2784789at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 3.
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:UP000007963}.
FT   DOMAIN          1..96
FT                   /note="DMAP1-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51912"
FT   REGION          51..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1621..1727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..670
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1632..1651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1681..1719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1823 AA;  200810 MW;  49B5C02E7505BBC8 CRC64;
     MADENPELQA ALRDLDRELE DGDITEKGYQ KRRTLLLSQF FGPNRALDVN AASTMDPSRS
     LTSSNNVPPA ILSVRPPTAD SNHGASPQPF AAGYENIQGN GSFGYDRRIS GDTQNSMVRE
     SLSLQQLDRM PSSASYDSLF LPKPPPGPGG AQEDSRTATL LSQNYAFNPG APQEHFEDPT
     GGYEVTPSAP TRQSTMLDSQ QGYFSDFAGQ QQDDYRDSYG GGGFHRYSQS DAFSPTANMA
     PPLIPASELH GPAIEHLLPL EPRDIPFAVN DPHDKNTPMS NFDNIPTVLR HRARVHSKQA
     AYWVLDQKGK EIASITWEKL ASRAEKVAQV IRDKSNLYRG DRVALIYRDS EIIEFAVALM
     GCFIAGVVAV PINSLEDYQS LNLVLTSTQA HLALTTENNL KNFQRDITTQ KLSWPRGVEW
     WKTNEFGSYH PKKKDDTPPL VVPDLAYIEF SRAPTGDLRG VVMSHRTIMH QMACLSAIIS
     NVPTSPRNVR PHGETLISYL DPRQGIGMIL GVLLTVYGGH TTVWIEDRTV ETPGLYAHLI
     TKYRATLMAA DYPGLKIAAY NYQQDPMSTR HYKKNTEPNF GSVKLCLIDT LTVDAEFHEI
     LADRWLRPMR NPRAREIVAP MLCLPEHGGM VISVRDWLGG EERMGCPLTH EMDPNNERRD
     SKKEERQAGK TNDGFGSSLL GGAPAPAPKE QKQNELGEVL LDKEALKSNE VVVLAMGEDA
     RRFAGTMPNA VRVGAFGYPI PDATLAVVDP ETNLLCTSNV IGEIWVDSPS LSGGFWALPK
     HTEAIFHARP YRFEEGNPTP VLVEPEFLRT GLLGCVIEGK VFILGLYEDR LRQKVEWVEH
     GQEIVEHRYF FVQHMIVTLL KNLPKIHDCT AFDVFVNDEH LPIVVLESYA ASTAPTTSGG
     PPRQLDSALL ESLAERCMEV LYQEHHLRVY CVLLTAPNTL PRVTKNGRQE IGNMLCRKDF
     DAGNLPCVHV KFGVERSVMN LPIGVDPVGG IWSPLSLMSR QEMVGMQEKQ YSGVDYRDVI
     MDDRTSTPLN NFNTIVDLLQ WRVSRQAEEL AYCSIDGRGK EGKGITWKKF DLKVAAVATY
     LRNKVKVRPG DHLVLMYTHS EDYVYAVHAC FCLGVVAIPL APIDQNRLSE DAPAFLHIIS
     DFHVKAIIVN SDVDHVMRQK VVSQHIKQSA QVLRIGVPAI YNTSKPSKQS HGCRDLGFTV
     KETWLSGNQP AMVWTYWTPD QRRISVHLGH DTIMGMCKVQ KETCQMTSSR PVLGSVRSTL
     GLGFLHTCLM GIYVGAPTYL VSPVDFAQNP MTLFLTLSRY KIKDTYATSQ MLDYAMTALA
     AKGFQLQELK NLMISAEGRP RVDISINIVY SHVLNPMVVT RSYMCIEPVE LWLDLRALRR
     GLIVPVDLDS DPSALLVQDS GMVPVNTQIA IVNPETCTLA HVGEYGEIWI QSDACAKAFY
     GSKQDFDQER FNGRIVDGDP NVAYVRTGDL GFLHTVTRPI GPGGQPVEMQ VLFVLGSIGE
     TFEVNGLNHF PMDIENSVER CHRNIVAGGC AVFQAGGLIV VVVEVTRKAY LASIVPVIVN
     AVLNEHQVVA DIVAFVSHGD FPRSRLGEKQ RGKVLASWVT RKLRTIAQFS IRDMEGAENQ
     FAEAPAPQHR VSRSSKPGSI MGNSTRRSTV VPDTEAAPRS PAPVLVEHPE APGGTYQPTP
     GDGAPLTSPT GSMPSVPQIA EPRPATSSTS GNTPVRSDAP ANPGNPDLGF DFGDFANTAT
     TASHGDNSVP ATAAELPYRP ATGHDSTYSQ QPYANYPDGA VAGYHDVVAD GGDWPQEALM
     YQSAMADDGQ ASGGIQRKPA PQL
//
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