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Q55E72

- PKS1_DICDI

UniProt

Q55E72 - PKS1_DICDI

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Protein

Probable polyketide synthase 1

Gene
stlA, pks1, DDB_G0269364
Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probable polyketide synthase By similarity. Produces only acylpyrones; in vitro.1 Publication

Catalytic activityi

3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2.

Cofactori

Binds 1 phosphopantetheine covalently By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei180 – 1801For beta-ketoacyl synthase activity By similarity
Active sitei682 – 6821For acyl/malonyl transferase activity By similarity
Active sitei2930 – 29301 By similarity

GO - Molecular functioni

  1. naringenin-chalcone synthase activity Source: UniProtKB-EC
  2. oxidoreductase activity Source: InterPro

GO - Biological processi

  1. flavonoid biosynthetic process Source: UniProtKB-UniPathway
  2. polyketide biosynthetic process Source: dictyBase
  3. resorcinol metabolic process Source: dictyBase
  4. sorocarp spore cell differentiation Source: dictyBase
  5. sorocarp stalk cell differentiation Source: dictyBase
  6. sorus development Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Flavonoid biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00154.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable polyketide synthase 1
Short name:
dipks1
Including the following 2 domains:
Polyketide synthase stlA (EC:2.3.1.-)
Chalcone synthase stlA (EC:2.3.1.74)
Alternative name(s):
Steely1
Gene namesi
Name:stlA
Synonyms:pks1
ORF Names:DDB_G0269364
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195: Chromosome 1, UP000002195: Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0269364. stlA.

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: dictyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31473147Probable polyketide synthase 1PRO_0000377901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2605 – 26051O-(pantetheine 4'-phosphoryl)serine By similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEiQ55E72.

Expressioni

Developmental stagei

Expressed during development. Expressed maximally in early development before cellular aggregation.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi44689.DDBDRAFT_0190208.

Structurei

Secondary structure

1
3147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2788 – 27958
Beta strandi2797 – 27993
Helixi2803 – 281311
Helixi2818 – 282912
Helixi2845 – 28473
Helixi2849 – 28546
Helixi2857 – 288327
Helixi2887 – 28893
Beta strandi2892 – 28998
Helixi2906 – 29149
Beta strandi2921 – 29277
Helixi2929 – 29313
Helixi2932 – 294413
Beta strandi2951 – 29588
Helixi2961 – 29633
Beta strandi2967 – 29693
Helixi2970 – 29789
Beta strandi2982 – 299110
Beta strandi3000 – 300910
Beta strandi3016 – 30227
Beta strandi3025 – 30306
Helixi3034 – 305320
Turni3054 – 30563
Beta strandi3063 – 30708
Helixi3075 – 308410
Helixi3089 – 30924
Helixi3093 – 310210
Helixi3108 – 311811
Beta strandi3125 – 31339
Turni3134 – 31363
Beta strandi3137 – 31459

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H84X-ray2.90A/B2776-3147[»]
ProteinModelPortaliQ55E72.
SMRiQ55E72. Positions 2785-3147.

Miscellaneous databases

EvolutionaryTraceiQ55E72.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2573 – 264270Acyl carrierAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni161 – 21454Beta-ketoacyl synthaseAdd
BLAST
Regioni672 – 70534Acyl/malonyl transferaseAdd
BLAST
Regioni2789 – 3147359Chalcone synthaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi355 – 3628Poly-Asp
Compositional biasi470 – 4789Poly-Asn
Compositional biasi561 – 5644Poly-Ser
Compositional biasi576 – 5816Poly-Thr
Compositional biasi1684 – 16885Poly-Ser
Compositional biasi2097 – 21004Poly-Gln
Compositional biasi2647 – 26559Poly-Asn
Compositional biasi2770 – 27745Poly-Gln

Domaini

Modular protein possessing six classical catalytic domains and a type III polyketide synthase domain. May facilitate covalent transfer of steely N-terminal acyl products directly to the C-terminal type III PKS active sites, which catalyze both iterative polyketide extension and cyclization.

Sequence similaritiesi

In the C-terminal section; belongs to the chalcone/stilbene synthases family.

Phylogenomic databases

eggNOGiCOG3424.
InParanoidiQ55E72.
OMAiNDDSINH.
PhylomeDBiQ55E72.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 4 hits.
3.40.50.150. 1 hit.
3.40.50.720. 2 hits.
3.90.180.10. 1 hit.
InterProiIPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013154. ADH_GroES-like.
IPR012328. Chalcone/stilbene_synth_C.
IPR001099. Chalcone/stilbene_synthase_N.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR013217. Methyltransf_12.
IPR016040. NAD(P)-bd_dom.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR029063. SAM-dependent_MTases-like.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF08240. ADH_N. 1 hit.
PF02797. Chal_sti_synt_C. 1 hit.
PF00195. Chal_sti_synt_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF08242. Methyltransf_12. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF53901. SSF53901. 5 hits.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q55E72-1 [UniParc]FASTAAdd to Basket

« Hide

MNKNSKIQSP NSSDVAVIGV GFRFPGNSND PESLWNNLLD GFDAITQVPK     50
ERWATSFREM GLIKNKFGGF LKDSEWKNFD PLFFGIGPKE APFIDPQQRL 100
LLSIVWESLE DAYIRPDELR GSNTGVFIGV SNNDYTKLGF QDNYSISPYT 150
MTGSNSSLNS NRISYCFDFR GPSITVDTAC SSSLVSVNLG VQSIQMGECK 200
IAICGGVNAL FDPSTSVAFS KLGVLSENGR CNSFSDQASG YVRSEGAGVV 250
VLKSLEQAKL DGDRIYGVIK GVSSNEDGAS NGDKNSLTTP SCEAQSINIS 300
KAMEKASLSP SDIYYIEAHG TGTPVGDPIE VKALSKIFSN SNNNQLNNFS 350
TDGNDNDDDD DDNTSPEPLL IGSFKSNIGH LESAAGIASL IKCCLMLKNR 400
MLVPSINCSN LNPSIPFDQY NISVIREIRQ FPTDKLVNIG INSFGFGGSN 450
CHLIIQEYNN NFKNNSTICN NNNNNNNNID YLIPISSKTK KSLDKYLILI 500
KTNSNYHKDI SFDDFVKFQI KSKQYNLSNR MTTIANDWNS FIKGSNEFHN 550
LIESKDGEGG SSSSNRGIDS ANQINTTTTS TINDIEPLLV FVFCGQGPQW 600
NGMIKTLYNS ENVFKNTVDH VDSILYKYFG YSILNVLSKI DDNDDSINHP 650
IVAQPSLFLL QIGLVELFKY WGIYPSISVG HSFGEVSSYY LSGIISLETA 700
CKIVYVRSSN QNKTMGSGKM LVVSMGFKQW NDQFSAEWSD IEIACYNAPD 750
SIVVTGNEER LKELSIKLSD ESNQIFNTFL RSPCSFHSSH QEVIKGSMFE 800
ELSNLQSTGE TEIPLFSTVT GRQVLSGHVT AQHIYDNVRE PVLFQKTIES 850
ITSYIKSHYP SNQKVIYVEI APHPTLFSLI KKSIPSSNKN SSSVLCPLNR 900
KENSNNSYKK FVSQLYFNGV NVDFNFQLNS ICDNVNNDHH LNNVKQNSFK 950
ETTNSLPRYQ WEQDEYWSEP LISRKNRLEG PTTSLLGHRI IYSFPVFQSV 1000
LDLQSDNYKY LLDHLVNGKP VFPGAGYLDI IIEFFDYQKQ QLNSSDSSNS 1050
YIINVDKIQF LNPIHLTENK LQTLQSSFEP IVTKKSAFSV NFFIKDTVED 1100
QSKVKSMSDE TWTNTCKATI SLEQQQPSPS STLTLSKKQD LQILRNRCDI 1150
SKLDKFELYD KISKNLGLQY NSLFQVVDTI ETGKDCSFAT LSLPEDTLFT 1200
TILNPCLLDN CFHGLLTLIN EKGSFVVESI SSVSIYLENI GSFNQTSVGN 1250
VQFYLYTTIS KATSFSSEGT CKLFTKDGSL ILSIGKFIIK STNPKSTKTN 1300
ETIESPLDET FSIEWQSKDS PIPTPQQIQQ QSPLNSNPSF IRSTILKDIQ 1350
FEQYCSSIIH KELINHEKYK NQQSFDINSL ENHLNDDQLM ESLSISKEYL 1400
RFFTRIISII KQYPKILNEK ELKELKEIIE LKYPSEVQLL EFEVIEKVSM 1450
IIPKLLFEND KQSSMTLFQD NLLTRFYSNS NSTRFYLERV SEMVLESIRP 1500
IVREKRVFRI LEIGAGTGSL SNVVLTKLNT YLSTLNSNGG SGYNIIIEYT 1550
FTDISANFII GEIQETMCNL YPNVTFKFSV LDLEKEIINS SDFLMGDYDI 1600
VLMAYVIHAV SNIKFSIEQL YKLLSPRGWL LCIEPKSNVV FSDLVFGCFN 1650
QWWNYYDDIR TTHCSLSESQ WNQLLLNQSL NNESSSSSNC YGGFSNVSFI 1700
GGEKDVDSHS FILHCQKESI SQMKLATTIN NGLSSGSIVI VLNSQQLTNM 1750
KSYPKVIEYI QEATSLCKTI EIIDSKDVLN STNSVLEKIQ KSLLVFCLLG 1800
YDLLENNYQE QSFEYVKLLN LISTTASSSN DKKPPKVLLI TKQSERISRS 1850
FYSRSLIGIS RTSMNEYPNL SITSIDLDTN DYSLQSLLKP IFSNSKFSDN 1900
EFIFKKGLMF VSRIFKNKQL LESSNAFETD SSNLYCKASS DLSYKYAIKQ 1950
SMLTENQIEI KVECVGINFK DNLFYKGLLP QEIFRMGDIY NPPYGLECSG 2000
VITRIGSNVT EYSVGQNVFG FARHSLGSHV VTNKDLVILK PDTISFSEAA 2050
SIPVVYCTAW YSLFNIGQLS NEESILIHSA TGGVGLASLN LLKMKNQQQQ 2100
PLTNVYATVG SNEKKKFLID NFNNLFKEDG ENIFSTRDKE YSNQLESKID 2150
VILNTLSGEF VESNFKSLRS FGRLIDLSAT HVYANQQIGL GNFKFDHLYS 2200
AVDLERLIDE KPKLLQSILQ RITNSIVNGS LEKIPITIFP STETKDAIEL 2250
LSKRSHIGKV VVDCTDISKC NPVGDVITNF SMRLPKPNYQ LNLNSTLLIT 2300
GQSGLSIPLL NWLLSKSGGN VKNVVIISKS TMKWKLQTMI SHFVSGFGIH 2350
FNYVQVDISN YDALSEAIKQ LPSDLPPITS VFHLAAIYND VPMDQVTMST 2400
VESVHNPKVL GAVNLHRISV SFGWKLNHFV LFSSITAITG YPDQSIYNSA 2450
NSILDALSNF RRFMGLPSFS INLGPMKDEG KVSTNKSIKK LFKSRGLPSL 2500
SLNKLFGLLE VVINNPSNHV IPSQLICSPI DFKTYIESFS TMRPKLLHLQ 2550
PTISKQQSSI INDSTKASSN ISLQDKITSK VSDLLSIPIS KINFDHPLKH 2600
YGLDSLLTVQ FKSWIDKEFE KNLFTHIQLA TISINSFLEK VNGLSTNNNN 2650
NNNSNVKSSP SIVKEEIVTL DKDQQPLLLK EHQHIIISPD IRINKPKRES 2700
LIRTPILNKF NQITESIITP STPSLSQSDV LKTPPIKSLN NTKNSSLINT 2750
PPIQSVQQHQ KQQQKVQVIQ QQQQPLSRLS YKSNNNSFVL GIGISVPGEP 2800
ISQQSLKDSI SNDFSDKAET NEKVKRIFEQ SQIKTRHLVR DYTKPENSIK 2850
FRHLETITDV NNQFKKVVPD LAQQACLRAL KDWGGDKGDI THIVSVTSTG 2900
IIIPDVNFKL IDLLGLNKDV ERVSLNLMGC LAGLSSLRTA ASLAKASPRN 2950
RILVVCTEVC SLHFSNTDGG DQMVASSIFA DGSAAYIIGC NPRIEETPLY 3000
EVMCSINRSF PNTENAMVWD LEKEGWNLGL DASIPIVIGS GIEAFVDTLL 3050
DKAKLQTSTA ISAKDCEFLI HTGGKSILMN IENSLGIDPK QTKNTWDVYH 3100
AYGNMSSASV IFVMDHARKS KSLPTYSISL AFGPGLAFEG CFLKNVV 3147
Length:3,147
Mass (Da):352,195
Last modified:May 24, 2005 - v1
Checksum:i6B67391AB6596F46
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAFI02000005 Genomic DNA. Translation: EAL72032.1.
RefSeqiXP_645909.1. XM_640817.1.

Genome annotation databases

EnsemblProtistsiDDB0234164; DDB0234164; DDB_G0269364.
GeneIDi8616850.
KEGGiddi:DDB_G0269364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAFI02000005 Genomic DNA. Translation: EAL72032.1 .
RefSeqi XP_645909.1. XM_640817.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2H84 X-ray 2.90 A/B 2776-3147 [» ]
ProteinModelPortali Q55E72.
SMRi Q55E72. Positions 2785-3147.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 44689.DDBDRAFT_0190208.

Proteomic databases

PRIDEi Q55E72.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblProtistsi DDB0234164 ; DDB0234164 ; DDB_G0269364 .
GeneIDi 8616850.
KEGGi ddi:DDB_G0269364.

Organism-specific databases

dictyBasei DDB_G0269364. stlA.

Phylogenomic databases

eggNOGi COG3424.
InParanoidi Q55E72.
OMAi NDDSINH.
PhylomeDBi Q55E72.

Enzyme and pathway databases

UniPathwayi UPA00154 .

Miscellaneous databases

EvolutionaryTracei Q55E72.

Family and domain databases

Gene3Di 1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 4 hits.
3.40.50.150. 1 hit.
3.40.50.720. 2 hits.
3.90.180.10. 1 hit.
InterProi IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013154. ADH_GroES-like.
IPR012328. Chalcone/stilbene_synth_C.
IPR001099. Chalcone/stilbene_synthase_N.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR013217. Methyltransf_12.
IPR016040. NAD(P)-bd_dom.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR029063. SAM-dependent_MTases-like.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 1 hit.
PF08240. ADH_N. 1 hit.
PF02797. Chal_sti_synt_C. 1 hit.
PF00195. Chal_sti_synt_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF08242. Methyltransf_12. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view ]
SMARTi SM00827. PKS_AT. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 1 hit.
[Graphical view ]
SUPFAMi SSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF53901. SSF53901. 5 hits.
SSF55048. SSF55048. 1 hit.
PROSITEi PS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  2. "Polyketide synthase genes and the natural products potential of Dictyostelium discoideum."
    Zucko J., Skunca N., Curk T., Zupan B., Long P.F., Cullum J., Kessin R.H., Hranueli D.
    Bioinformatics 23:2543-2549(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  3. "Biosynthesis of Dictyostelium discoideum differentiation-inducing factor by a hybrid type I fatty acid-type III polyketide synthase."
    Austin M.B., Saito T., Bowman M.E., Haydock S., Kato A., Moore B.S., Kay R.R., Noel J.P.
    Nat. Chem. Biol. 2:494-502(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2776-3147, FUNCTION, DEVELOPMENTAL STAGE, SUBUNIT.

Entry informationi

Entry nameiPKS1_DICDI
AccessioniPrimary (citable) accession number: Q55E72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: May 24, 2005
Last modified: June 11, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

In reference to their hybrid nature and to their discovery in D.discoideum, authors (1 Publication) term these type I FAS-type III PKS fusion enzymes 'steely'.
Encoded by one of the numerous copies of polyketide synthase genes localized in chromosome 1.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3