|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05279 |
PRK05279 |
N-acetylglutamate synthase; Validated |
1-442 |
0e+00 |
|
N-acetylglutamate synthase; Validated
Pssm-ID: 235386 [Multi-domain] Cd Length: 441 Bit Score: 896.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 1 MVKERKTELVEGFRHSVPYINTHRGKTFVIMLGGEAIEHENFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEP 80
Cdd:PRK05279 1 MMKERSTEFVDWFRHSAPYINAHRGKTFVIMLGGEAIAHGNFSNIVHDIALLHSLGIRLVLVHGARPQIEEQLAARGIEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 81 LYHKNIRVTDAKTLELVKQAAGTLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEDA 160
Cdd:PRK05279 81 RYHKGLRVTDAAALECVKQAAGELRLDIEARLSMGLPNTPMAGAHIRVVSGNFVTARPLGVDDGVDYQHTGEVRRIDAEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 161 IHRQLDSGAIVLMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNDDGDIVSELFPNEAQARVEAQEEk 240
Cdd:PRK05279 161 IRRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTESQGVLDEDGELIRELSPNEAQALLEALED- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 241 GDYNSGTVRFLRGAVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQIVMESAEQIRRATINDIGGILELIRPLEQQG 320
Cdd:PRK05279 240 GDYNSGTARFLRAAVKACRGGVRRSHLISYAEDGALLQELFTRDGIGTMIVMESLEQLRRATIDDVGGILELIRPLEEQG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 321 ILVRRSREQLEMEIDKFTIIQRDNTTIACAALYPFPEEKIGEMACVAVHPDYRSSSRGEVLLERIAAQAKQSGLSKLFVL 400
Cdd:PRK05279 320 ILVRRSREQLEREIDKFTVIERDGLIIGCAALYPFPEEKMGEMACLAVHPDYRGSGRGERLLKRIEQRARQLGLKRLFVL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15832929 401 TTRSIHWFQERGFTPVDIDLLPESKKQLYNYQRKSKVLMADL 442
Cdd:PRK05279 400 TTRTAHWFLERGFVPVDVDDLPEAKRQLYNYQRRSKVLVKDL 441
|
|
| N-Ac-Glu-synth |
TIGR01890 |
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ... |
9-442 |
0e+00 |
|
amino-acid N-acetyltransferase; This model represents a clade of amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the "acetylated" ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 273856 [Multi-domain] Cd Length: 429 Bit Score: 634.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 9 LVEGFRHSVPYINTHRGKTFVIMLGGEAIEHENFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRV 88
Cdd:TIGR01890 1 FVAWFREAAPYINAHRGKTFVVGLGGELVEGGNLGNIVADIALLHSLGVRLVLVHGARPQIERILAARGRTPHYHRGLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 89 TDAKTLELVKQAAGTLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEDAIHRQLDSG 168
Cdd:TIGR01890 81 TDEASLEQAQQAAGTLRLAIEARLSMSLSNTPMAGSRLPVVSGNFVTARPIGVIEGVDYEHTGVIRKIDTEGIRRQLDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 169 AIVLMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNDDGDIVSELFPNEAQARVEAQEEKgdynsGTV 248
Cdd:TIGR01890 161 SIVLLSPLGHSPTGETFNLDMEDVATSVAISLKADKLIYFTLSPGISDPDGTLAAELSPQEVESLAERLGSE-----TTR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 249 RFLRGAVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQIVMESAEQIRRATINDIGGILELIRPLEQQGILVRRSRE 328
Cdd:TIGR01890 236 RLLSAAVKACRGGVHRSHIVSYAEDGSLLQELFTRDGIGTSISKEAFESIRQATIDDIGGIAALIRPLEEQGILVRRSRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 329 QLEMEIDKFTIIQRDNTTIACAALYPFPEEKIGEMACVAVHPDYRSSSRGEVLLERIAAQAKQSGLSKLFVLTTRSIHWF 408
Cdd:TIGR01890 316 YLEREISEFSIIEHDGNIIGCAALYPYAEEDCGEMACLAVSPEYQDGGRGERLLAHIEDRARQMGISRLFVLTTRTGHWF 395
|
410 420 430
....*....|....*....|....*....|....
gi 15832929 409 QERGFTPVDIDLLPESKKQLYNYQRKSKVLMADL 442
Cdd:TIGR01890 396 RERGFQTASVDELPEARRKLYNYQRNSKILMKRL 429
|
|
| AAK_NAGS-ABP |
cd04237 |
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ... |
8-290 |
6.13e-168 |
|
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. Domain architecture of these NAGS consisted of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal NAG synthase, acetyltransferase (ArgA) domain. Both bacterial and plant sequences in this CD have a conserved N-terminal extension; a similar sequence in the NAG kinases of the cyclic arginine-biosynthesis pathway has been implicated in feedback inhibition sensing. Plant sequences also have an N-terminal chloroplast transit peptide and an insert (approx. 70 residues) in the C-terminal region of ArgB. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239770 [Multi-domain] Cd Length: 280 Bit Score: 472.81 E-value: 6.13e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 8 ELVEGFRHSVPYINTHRGKTFVIMLGGEAIEHENFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIR 87
Cdd:cd04237 1 QFVDWFREAAPYINAHRGKTFVIAFGGEAVAHPNFDNIVHDIALLHSLGIRLVLVHGARPQIDQRLAERGLEPRYHRGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 88 VTDAKTLELVKQAAGTLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEDAIHRQLDS 167
Cdd:cd04237 81 ITDAAALECVKEAAGAVRLEIEALLSMGLPNSPMAGARIRVVSGNFVTARPLGVVDGVDFGHTGEVRRIDADAIRRQLDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 168 GAIVLMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNDDGDIVSELFPNEAQARVEAQEEKgdyNSGT 247
Cdd:cd04237 161 GSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADKLIFLTDGPGLLDDDGELIRELTAQEAEALLETGALL---TNDT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15832929 248 VRFLRGAVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQI 290
Cdd:cd04237 238 ARLLQAAIEACRGGVPRVHLISYAEDGALLLELFTRDGVGTLI 280
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
4-291 |
2.42e-133 |
|
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440314 [Multi-domain] Cd Length: 283 Bit Score: 385.15 E-value: 2.42e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 4 ERKTELVEGFRHSVPYINTHRGKTFVIMLGGEAIEHENF-SSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLY 82
Cdd:COG0548 2 ESAIEKAEWLREALPYIQAFRGKTFVIKYGGEAMEDEELkAALAQDIALLKSLGIRPVLVHGGGPQINELLKRLGIESEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 83 HKNIRVTDAKTLELVKQA-AGTLQLDITARLSMSLNNtplqGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEDAI 161
Cdd:COG0548 82 VNGLRVTDEETLEVVEMVlAGKVNKEIVALLSQGGGN----AVGLSGKDGNLITARPLGVGDGVDLGHVGEVRRVDPELI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 162 HRQLDSGAIVLMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNDDGDIVSELFPNEAQARVeaqeEKG 241
Cdd:COG0548 158 RALLDAGYIPVISPIGYSPTGEVYNINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTAAEAEELI----ADG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15832929 242 DYNSGTVRFLRGAVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQIV 291
Cdd:COG0548 234 VISGGMIPKLEAALDAVRGGVKRVHIIDGRVPHALLLELFTDDGIGTMIV 283
|
|
| PLN02825 |
PLN02825 |
amino-acid N-acetyltransferase |
10-442 |
9.47e-112 |
|
amino-acid N-acetyltransferase
Pssm-ID: 215441 [Multi-domain] Cd Length: 515 Bit Score: 338.29 E-value: 9.47e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 10 VEGFRHSVPYINTHRGKTFVIMLGGEAIEHENFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVT 89
Cdd:PLN02825 2 VRWFREAWPYIQGHRGSTFVVVISGEVVAGPHLDNILQDISLLHGLGIKFVLVPGTHVQIDKLLAERGREPKYVGAYRIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 90 DAKTLELVKQAAGTLQLDITARLS---MSLN------NTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEDA 160
Cdd:PLN02825 82 DSAALQASMEAAGKIRVMIEAKLSpgpSIPNlrrhgdNSRWHEVGVSVASGNFLAAKRRGVVNGVDFGATGEVKKIDVSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 161 IHRQLDSGAIVLMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTN------------------------ 216
Cdd:PLN02825 162 IKERLDSNCIVLLSNLGYSSSGEVLNCNTYEVATACALAIGADKLICIVDGPILDEngrlirfmtleeadmlirkrakqs 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 217 ----------DDGDIVSELFPNEAQARVEAQEEKGDYNSG--TVRFLRG------------------------------- 253
Cdd:PLN02825 242 eiaanyvkavGGEDYSYSLGLDSVNTTPFNNNGRGFWGSGsaTDSFQNGvgfdngnglsgeqgfaiggeerlsrlngyls 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 254 ----AVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQIVMESAEQIRRATINDIGGILELIRPLEQQGILVRRSREQ 329
Cdd:PLN02825 322 elaaAAFVCRGGVQRVHLLDGTIEGVLLLELFTRDGMGTMIASDMYEGTRMARVEDLAGIRQIIRPLEESGILVRRTDEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 330 LEMEIDKFTIIQRDNTTIACAALYPFPEEKIGEMACVAVHPDYRSSSRGEVLLERIAAQAKQSGLSKLFVLTTRSIHWFQ 409
Cdd:PLN02825 402 LLRALDSFVVVEREGSIIACAALFPFFEEKCGEVAAIAVSPECRGQGQGDKLLDYIEKKAASLGLEKLFLLTTRTADWFV 481
|
490 500 510
....*....|....*....|....*....|...
gi 15832929 410 ERGFTPVDIDLLPESKKQLYNYQRKSKVLMADL 442
Cdd:PLN02825 482 RRGFSECSIESLPEARRKRINLSRGSKYYMKKL 514
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
18-291 |
1.13e-43 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 154.50 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 18 PYINTHRGKTFVIMLGGEAIEHENFS-SIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVTDAKTLEL 96
Cdd:PRK00942 16 PYIQRFMGKTIVIKYGGNAMTDEELKeAFARDIVLLKQVGINPVVVHGGGPQIDELLKKLGIESEFVNGLRVTDAETMEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 97 VKQA-AGTLQLDITARlsmslnntpLQGAHINVV-----SGNFIIAQPLGVDdgVDYCHSGRIRRIDEDAIHRQLDSGAI 170
Cdd:PRK00942 96 VEMVlAGKVNKELVSL---------INKHGGKAVglsgkDGGLITAKKLEED--EDLGFVGEVTPVNPALLEALLEAGYI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 171 VLMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNDDGDIVSELFPNEAQARVeaqeEKGDYNSGTVRF 250
Cdd:PRK00942 165 PVISPIGVGEDGETYNINADTAAGAIAAALGAEKLILLTDVPGVLDDKGQLISELTASEAEELI----EDGVITGGMIPK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15832929 251 LRGAVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQIV 291
Cdd:PRK00942 241 VEAALDAARGGVRSVHIIDGRVPHALLLELFTDEGIGTMIV 281
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
16-290 |
1.17e-40 |
|
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239783 [Multi-domain] Cd Length: 279 Bit Score: 146.11 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 16 SVPYINTHRGKTFVIMLGGEAIEHEN-FSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVTDAKTL 94
Cdd:cd04250 5 ALPYIQKFRGKTVVIKYGGNAMKDEElKESFARDIVLLKYVGINPVVVHGGGPEINEMLKKLGIESEFVNGLRVTDEETM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 95 ELVKQAagtLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPL---GVDDGVDYCHSGRIRRIDEDAIHRQLDSGAIV 171
Cdd:cd04250 85 EIVEMV---LVGKVNKEIVSLINRAGGKAVGLSGKDGNLIKAKKKdatVIEEIIDLGFVGEVTEVNPELLETLLEAGYIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 172 LMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGV---TNDDGDIVSELFPNEAQARVeaqeEKGDYNSGTV 248
Cdd:cd04250 162 VIAPVGVGEDGETYNINADTAAGAIAAALKAEKLILLTDVAGVlddPNDPGSLISEISLKEAEELI----ADGIISGGMI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15832929 249 RFLRGAVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQI 290
Cdd:cd04250 238 PKVEACIEALEGGVKAAHIIDGRVPHSLLLEIFTDEGIGTMI 279
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
28-290 |
7.42e-40 |
|
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239771 [Multi-domain] Cd Length: 256 Bit Score: 143.42 E-value: 7.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 28 FVIMLGGEAIEHEN-FSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVTDAKTLELVKQA-AGTLQ 105
Cdd:cd04238 1 VVIKYGGSAMKDEElKEAFADDIVLLKQVGINPVIVHGGGPEINELLKRLGIESEFVNGLRVTDKETMEIVEMVlAGKVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 106 LDITARlsmsLNNTPLQGAHINVVSGNFIIAQPLGVDDgVDYCHSGRIRRIDEDAIHRQLDSGAIVLMGPVAVSVTGESF 185
Cdd:cd04238 81 KELVSL----LNRAGGKAVGLSGKDGGLIKAEKKEEKD-IDLGFVGEVTEVNPELLETLLEAGYIPVIAPIAVDEDGETY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 186 NLTSEEIATQLAIKLKAEKMIgFCSS-QGVTNDDGDIVSELFPNEAQARVeaqeEKGDYNSGTVRFLRGAVKACRSGVRR 264
Cdd:cd04238 156 NVNADTAAGAIAAALKAEKLI-LLTDvPGVLDDPGSLISELTPKEAEELI----EDGVISGGMIPKVEAALEALEGGVRK 230
|
250 260
....*....|....*....|....*.
gi 15832929 265 CHLISYQEDGALLQELFSRDGIGTQI 290
Cdd:cd04238 231 VHIIDGRVPHSLLLELFTDEGIGTMI 256
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
26-269 |
2.04e-35 |
|
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.
Pssm-ID: 395565 [Multi-domain] Cd Length: 232 Bit Score: 130.95 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 26 KTFVIMLGGEAIEH-ENFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHkniRVTDAKTLELVK-QAAGT 103
Cdd:pfam00696 1 KRVVIKLGGSSLTDkERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFA---RLTDAETLEVATmDALGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 104 LQLDITARL-SMSLNNTPLQGAHINVVSGNFIiaqplgvddgvdychSGRIRRIDEDAIHRQLDSGAI-VLMGPVAVSVT 181
Cdd:pfam00696 78 LGERLNAALlAAGLPAVGLPAAQLLATEAGFI---------------DDVVTRIDTEALEELLEAGVVpVITGFIGIDPE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 182 GESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNDDGDIVS--ELFPNEAQARVEAQEEKGDYNSGTVRFLRGAVKACR 259
Cdd:pfam00696 143 GELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKVPdaKLIPEISYDELLELLASGLATGGMKVKLPAALEAAR 222
|
250
....*....|
gi 15832929 260 SGVRRCHLIS 269
Cdd:pfam00696 223 RGGIPVVIVN 232
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
296-442 |
7.38e-34 |
|
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440859 [Multi-domain] Cd Length: 132 Bit Score: 123.56 E-value: 7.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 296 EQIRRATINDIGGILELIRPLEqqgilvrrsreqLEMEIDKFTIIQRDNTTIACAALYPFPEEkIGEMACVAVHPDYRSS 375
Cdd:COG1246 1 MTIRPATPDDVPAILELIRPYA------------LEEEIGEFWVAEEDGEIVGCAALHPLDED-LAELRSLAVHPDYRGR 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832929 376 SRGEVLLERIAAQAKQSGLSKLFVLTTR-SIHWFQERGFTPVDIDLLPESKKqlynYQRKSKVLMADL 442
Cdd:COG1246 68 GIGRRLLEALLAEARELGLKRLFLLTTSaAIHFYEKLGFEEIDKEDLPYAKV----WQRDSVVMEKDL 131
|
|
| argB |
CHL00202 |
acetylglutamate kinase; Provisional |
6-292 |
3.80e-33 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 133644 [Multi-domain] Cd Length: 284 Bit Score: 126.45 E-value: 3.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 6 KTELVEGFRHSVPYINTHRGKTFVIMLGGEAIEHENFSS-IVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHK 84
Cdd:CHL00202 4 NDERVQVLSEALPYIQKFRGRIMVIKYGGAAMKNLILKAdIIKDILFLSCIGLKIVVVHGGGPEINFWLKQLNISPKFWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 85 NIRVTDAKTLELVKQA-AGTLQLDITArlsmSLNNTPLQGAHINVVSGNFIIAQPlgvDDGVDYCHSGRIRRIDEDAIHR 163
Cdd:CHL00202 84 GIRVTDKVTMEIVEMVlAGKVNKDLVG----SINANGGKAVGLCGKDANLIVARA---SDKKDLGLVGEIQQVDPQLIDM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 164 QLDSGAIVLMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGV---TNDDGDIVSELfpNEAQARVEAQeeK 240
Cdd:CHL00202 157 LLEKNYIPVIASVAADHDGQTYNINADVVAGEIAAKLNAEKLILLTDTPGIladINDPNSLISTL--NIKEARNLAS--T 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15832929 241 GDYNSGTVRFLRGAVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQIVM 292
Cdd:CHL00202 233 GIISGGMIPKVNCCIRALAQGVEAAHIIDGKEKHALLLEILTEKGIGSMLVV 284
|
|
| PLN02512 |
PLN02512 |
acetylglutamate kinase |
16-290 |
6.95e-31 |
|
acetylglutamate kinase
Pssm-ID: 178128 Cd Length: 309 Bit Score: 120.56 E-value: 6.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 16 SVPYINTHRGKTFVIMLGGEAIEHENF-SSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVTDAKTL 94
Cdd:PLN02512 38 ALPFIQRFRGKTVVVKYGGAAMKDPELkAGVIRDLVLLSCVGLRPVLVHGGGPEINSWLKKVGIEPQFKNGLRVTDAETM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 95 ELVKQaagTLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLgvDDGVDYCHSGRIRRIDEDAIHRQLDSGAIVLMG 174
Cdd:PLN02512 118 EVVEM---VLVGKVNKSLVSLINKAGGTAVGLSGKDGRLLRARPS--PNSADLGFVGEVTRVDPTVLRPLVDDGHIPVIA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 175 PVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGV---TNDDGDIVSELFPNEaqarVEAQEEKGDYNSGTVRFL 251
Cdd:PLN02512 193 TVAADEDGQAYNINADTAAGEIAAALGAEKLILLTDVAGVledKDDPGSLVKELDIKG----VRKLIADGKIAGGMIPKV 268
|
250 260 270
....*....|....*....|....*....|....*....
gi 15832929 252 RGAVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQI 290
Cdd:PLN02512 269 ECCVRSLAQGVKTAHIIDGRVPHSLLLEILTDEGAGTMI 307
|
|
| argB |
TIGR00761 |
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ... |
27-266 |
8.58e-27 |
|
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 273256 [Multi-domain] Cd Length: 231 Bit Score: 107.37 E-value: 8.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 27 TFVIMLGGEAI--EHENFssiVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVTDAKTLELVKQA-AGT 103
Cdd:TIGR00761 1 TIVIKIGGAAIsdLLEAF---ASDIAFLRAVGIKPVIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVVEMVlIGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 104 LQLDITArlsmSLNNTPLQGAHINVVSGNFIIAQPLGVDdgvDYCHSGRIRRIDEDAIHRQLDSGAIVLMGPVAVSVTGE 183
Cdd:TIGR00761 78 VNKELVA----LLNKHGINAIGLTGGDGQLFTARYLDKE---DLGYVGEIKKVNKALIEALLKAGYIPVISSLALTAEGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 184 SFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNDDGD-IVSELFPNEAqarvEAQEEKGDYNSGTVRFLRGAVKACRSGV 262
Cdd:TIGR00761 151 ALNVNADTAAGALAAALGAEKLVLLTDVPGILNGDGQsLISEIPLDEI----EQLIKQGIIKGGMIPKVNAALEALRGGV 226
|
....
gi 15832929 263 RRCH 266
Cdd:TIGR00761 227 RSVH 230
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
29-290 |
2.07e-25 |
|
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.
Pssm-ID: 239033 [Multi-domain] Cd Length: 248 Bit Score: 104.06 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 29 VIMLGGEAIEH-ENFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVTDAKTLELVKQAAGTLQLD 107
Cdd:cd02115 1 VIKFGGSSVSSeERLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDRETDALAAMGEGMSNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 108 ITARLSMS-LNNTPLQGAHINVVSGNfiiaqplgvddgvdYCHSGRIRRIDEDAIHRQLDSGAIVLMGPVAVSV---TGE 183
Cdd:cd02115 81 IAAALEQHgIKAVPLDLTQAGFASPN--------------QGHVGKITKVSTDRLKSLLENGILPILSGFGGTDekeTGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 184 SFNLTSEEIATQLAIKLKAEKMI------GFCSSQGVTNDDGDIVSELFPNEAqarveaqEEKgdYNSGTVRFLRGAVKA 257
Cdd:cd02115 147 LGRGGSDSTAALLAAALKADRLViltdvdGVYTADPRKVPDAKLLSELTYEEA-------AEL--AYAGAMVLKPKAADP 217
|
250 260 270
....*....|....*....|....*....|...
gi 15832929 258 CRSGVRRCHLISYQEDGALlqELFSRDGIGTQI 290
Cdd:cd02115 218 AARAGIPVRIANTENPGAL--ALFTPDGGGTLI 248
|
|
| AAK_NAGK-fArgBP |
cd04252 |
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ... |
29-290 |
1.15e-16 |
|
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (fArgBP). The nuclear-encoded, mitochondrial polyprotein precursor with an N-terminal NAGK (ArgB) domain (this CD), a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved in the mitochondria into two distinct enzymes (NAGK-DUF619 and NAGPR). Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. This CD also includes some gamma-proteobacteria (Xanthomonas and Xylella) NAG kinases with an N-terminal NAGK (ArgB) domain (this CD) and a C-terminal DUF619 domain. The DUF619 domain is described as a putative distant homolog of the acetyltransferase, ArgA, predicted to function in NAG synthase association in fungi. Eukaryotic sequences have an N-terminal mitochondrial transit peptide. Members of this NAG kinase domain CD belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239785 [Multi-domain] Cd Length: 248 Bit Score: 79.34 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 29 VIMLGGEAIEHEnFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVTDAKTLELvkqaAGTLQLDI 108
Cdd:cd04252 2 VIKVGGAIIEDD-LDELAASLSFLQHVGLYPIVVHGAGPQLNEELEAAGVEPEYVDGLRVTDPETLAV----ARKVFLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 109 TARLSMSLNNTplqGAHINVVSGNFIIAQPLgvdDGVDYCHSGRIRRIDEDAIHRQLDSGAIVLMGPVAVSVTGESFNLT 188
Cdd:cd04252 77 NLKLVEALERN---GARARPITSGVFEAEYL---DKDKYGLVGKITGVNKAPIEAAIRAGYLPILTSLAETPSGQLLNVN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 189 SEEIATQLAIKLKAEKMIGFCSSQGVTNDDGDIVSELFPNEAQARVEAQEEkgdYNSGTVRFLRgAVKACRSGVRRCHLI 268
Cdd:cd04252 151 ADVAAGELARVLEPLKIVFLNETGGLLDGTGKKISAINLDEEYDDLMKQPW---VKYGTKLKIK-EIKELLDTLPRSSSV 226
|
250 260
....*....|....*....|..
gi 15832929 269 SYQEDGALLQELFSRDGIGTQI 290
Cdd:cd04252 227 SITSPDDLQKELFTHSGAGTLI 248
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
29-264 |
9.84e-16 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 76.86 E-value: 9.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 29 VIMLGGEAIEheNFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEP--LYHKN---IRVTDAKTLELVKQAAGT 103
Cdd:PRK14058 3 VVKIGGSVGI--DPEDALIDVASLWADGERVVLVHGGSDEVNELLERLGIEPrfVTSPSgvtSRYTDRETLEVFIMAMAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 104 LQLDITARL-SMSLNNTPLQGAHINVVSG---NFIIAqplgVDDG----VDYCHSGRIRRIDEDAIHRQLDSGAIVLMGP 175
Cdd:PRK14058 81 INKQLVERLqSLGVNAVGLSGLDGGLLEGkrkKAVRV----VEEGkkkiIRGDYTGKIEEVNTDLLKLLLKAGYLPVVAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 176 VAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGV---TNDDGDIVSELFPNEAQARVEAQEekgdynSGTVRFLR 252
Cdd:PRK14058 157 PALSEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLlrdPPDEGSLIERITPEEAEELSKAAG------GGMKKKVL 230
|
250
....*....|..
gi 15832929 253 GAVKACRSGVRR 264
Cdd:PRK14058 231 MAAEAVEGGVGR 242
|
|
| PRK07757 |
PRK07757 |
N-acetyltransferase; |
297-423 |
7.83e-15 |
|
N-acetyltransferase;
Pssm-ID: 236088 [Multi-domain] Cd Length: 152 Bit Score: 71.38 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 297 QIRRATINDIGGILELIRPLEQQGILVRRSREQLEMEIDKFTIIQRDNTTIACAALYpFPEEKIGEMACVAVHPDYRSSS 376
Cdd:PRK07757 3 EIRKARLSDVKAIHALINVYAKKGLMLPRSLDELYENIRDFYVAEEEGEIVGCCALH-ILWEDLAEIRSLAVSEDYRGQG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15832929 377 RGEVLLERIAAQAKQSGLSKLFVLTTrSIHWFQERGFTPVDIDLLPE 423
Cdd:PRK07757 82 IGRMLVEACLEEARELGVKRVFALTY-QPEFFEKLGFREVDKEALPQ 127
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
29-290 |
1.08e-14 |
|
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239784 [Multi-domain] Cd Length: 257 Bit Score: 73.56 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 29 VIMLGGE-AIEHENFSSIVNDIGLlhslgiRLVVVYGARPQIDANLAAHHHEPLY------HKNiRVTDAKTLELVKQAA 101
Cdd:cd04251 2 VVKIGGSvVSDLDKVIDDIANFGE------RLIVVHGGGNYVNEYLKRLGVEPKFvtspsgIRS-RYTDKETLEVFVMVM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 102 GTLQLDITARLSM---------SLNNTPLQGAHINVVSGNfIIAQPLGVDDGvdycHSGRIRRIDEDAIHRQLDSGAIVL 172
Cdd:cd04251 75 GLINKKIVARLHSlgvkavgltGLDGRLLEAKRKEIVRVN-ERGRKMIIRGG----YTGKVEKVNSDLIEALLDAGYLPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 173 MGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNdDGDIVSELFPNEAQARVEAQEekgdynSGTVRFLR 252
Cdd:cd04251 150 VSPVAYSEEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLYL-DGRVIERITVSDAESLLEKAG------GGMKRKLL 222
|
250 260 270
....*....|....*....|....*....|....*...
gi 15832929 253 GAVKACRSGVRRCHLISYQEDGALLQELfsrDGIGTQI 290
Cdd:cd04251 223 AAAEAVEGGVREVVIGDARADSPISSAL---NGGGTVI 257
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
294-423 |
4.05e-14 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 74.43 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 294 SAEQIRRATINDIGGILELIRPLEQQGILVRRSREQLEMEIDKFTIIQRDNTTIACAALYPFpEEKIGEMACVAVHPDYR 373
Cdd:PRK12308 462 SGVKVRPARLTDIDAIEGMVAYWAGLGENLPRSRNELVRDIGSFAVAEHHGEVTGCASLYIY-DSGLAEIRSLGVEAGWQ 540
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15832929 374 SSSRGEVLLERIAAQAKQSGLSKLFVLtTRSIHWFQERGFTPVDIDLLPE 423
Cdd:PRK12308 541 VQGQGSALVQYLVEKARQMAIKKVFVL-TRVPEFFMKQGFSPTSKSLLPE 589
|
|
| PRK07922 |
PRK07922 |
amino-acid N-acetyltransferase; |
291-417 |
6.11e-13 |
|
amino-acid N-acetyltransferase;
Pssm-ID: 236132 [Multi-domain] Cd Length: 169 Bit Score: 66.48 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 291 VMESAEQIRRATINDIGGILELIRPLEQQGILVRRSREQLEMEIDKFTIIQRDN-TTIACAALYPFPEEkIGEMACVAVH 369
Cdd:PRK07922 1 TAAGAITVRRARTSDVPAIKRLVDPYAQGRILLEKNLVTLYEAVQEFWVAEHLDgEVVGCGALHVMWED-LAEIRTVAVD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15832929 370 PDYRSSSRGEVLLERIAAQAKQSGLSKLFVLT------TRsiHWFQERGFTPVD 417
Cdd:PRK07922 80 PAARGRGVGHAIVERLLDVARELGLSRVFVLTfeveffAR--HGFVEIDGTPVT 131
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
303-413 |
1.37e-09 |
|
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
Pssm-ID: 395465 [Multi-domain] Cd Length: 116 Bit Score: 55.60 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 303 INDIGGILELIRPLEQQGILVRRSREQLEMEIDKFTIIQRDNTTIACAALYPFPEE-KIGEMACVAVHPDYRSSSRGEVL 381
Cdd:pfam00583 1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEpPVGEIEGLAVAPEYRGKGIGTAL 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 15832929 382 LERIAAQAKQSGLSKLFVLT----TRSIHWFQERGF 413
Cdd:pfam00583 81 LQALLEWARERGCERIFLEVaadnLAAIALYEKLGF 116
|
|
| PhnO |
COG0454 |
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ... |
298-417 |
6.62e-09 |
|
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];
Pssm-ID: 440222 [Multi-domain] Cd Length: 136 Bit Score: 54.29 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 298 IRRATINDIGGILeLIRPLEQQgilvRRSREQLEMEiDKFTIIQRDNTTIACAALYPFPEeKIGEMACVAVHPDYRSSSR 377
Cdd:COG0454 3 IRKATPEDINFIL-LIEALDAE----LKAMEGSLAG-AEFIAVDDKGEPIGFAGLRRLDD-KVLELKRLYVLPEYRGKGI 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15832929 378 GEVLLERIAAQAKQSGLSKLFVLT----TRSIHWFQERGFTPVD 417
Cdd:COG0454 76 GKALLEALLEWARERGCTALELDTldgnPAAIRFYERLGFKEIE 119
|
|
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
297-417 |
1.77e-08 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 53.46 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 297 QIRRATINDIGGILELIRPLEQQGI----LVRRSREQLEMEIDKFT-------IIQRDNTTIACAALYPFPEEK----IG 361
Cdd:COG1247 3 TIRPATPEDAPAIAAIYNEAIAEGTatfeTEPPSEEEREAWFAAILapgrpvlVAEEDGEVVGFASLGPFRPRPayrgTA 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 362 EMAcVAVHPDYRSSSRGEVLLERIAAQAKQSGLSKLFVLT----TRSIHWFQERGFTPVD 417
Cdd:COG1247 83 EES-IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVladnEASIALYEKLGFEEVG 141
|
|
| yhbS |
COG3153 |
Predicted N-acetyltransferase YhbS [General function prediction only]; |
298-417 |
2.75e-08 |
|
Predicted N-acetyltransferase YhbS [General function prediction only];
Pssm-ID: 442387 [Multi-domain] Cd Length: 142 Bit Score: 52.40 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 298 IRRATINDIGGILELIR---PLEQQGILVRRSREQLEmeIDKFTIIQRDNTTIACAALYPFP---EEKIGEMACVAVHPD 371
Cdd:COG3153 1 IRPATPEDAEAIAALLRaafGPGREAELVDRLREDPA--AGLSLVAEDDGEIVGHVALSPVDidgEGPALLLGPLAVDPE 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15832929 372 YRSSSRGEVLLERIAAQAKQSGLSKLFVLTTRSIHWFQER-GFTPVD 417
Cdd:COG3153 79 YRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERfGFRPAG 125
|
|
| Acetyltransf_7 |
pfam13508 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
333-415 |
3.61e-08 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 463905 [Multi-domain] Cd Length: 84 Bit Score: 50.53 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 333 EIDKFTIIQRDNTTIACAALYPFPEEKIGEMACVAVHPDYRSSSRGEVLLERIAAQAKQSGLSKLFVLTT-RSIHWFQER 411
Cdd:pfam13508 1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTnRAAAFYEKL 80
|
....
gi 15832929 412 GFTP 415
Cdd:pfam13508 81 GFEE 84
|
|
| RimI |
COG0456 |
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ... |
348-418 |
6.74e-08 |
|
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440224 [Multi-domain] Cd Length: 92 Bit Score: 50.04 E-value: 6.74e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832929 348 ACAALYPFPEEKIGEMACVAVHPDYRSSSRGEVLLERIAAQAKQSGLSKLFVLT----TRSIHWFQERGFTPVDI 418
Cdd:COG0456 1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVrednEAAIALYEKLGFEEVGE 75
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| AAK_NAGS-Urea |
cd04236 |
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ... |
39-288 |
1.84e-05 |
|
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the urea cycle found in animals. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate; NAG is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Ureogenic NAGS activity is dependent on the concentration of glutamate (substrate) and arginine (activator). Domain architecture of ureogenic NAGS consists of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal DUF619 domain. Members of this CD belong to the protein superfamily, the Amino Acid Kinase Family (AAKF).
Pssm-ID: 239769 [Multi-domain] Cd Length: 271 Bit Score: 45.99 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 39 HENFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLaaHHHEPLYHKNIRVTDAKTLELVKQAAGTlqlditarlsmslNN 118
Cdd:cd04236 50 LEMVQSLSFGLAFLQRMDMKLLVVMGLSAPDGTNM--SDLELQAARSRLVKDCKTLVEALQANSA-------------AA 114
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 119 TPLQGAhinvvsGNFIIAQPlgVDDGVDYchsGRIRRIDEDAIHRQLDSGAIVLMGPVAVSVTGESFNLTSEEIATQLAI 198
Cdd:cd04236 115 HPLFSG------ESVLQAEE--PEPGASK---GPSVSVDTELLQWCLGSGHIPLVCPIGETSSGRSVSLDSSEVTTAIAK 183
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 199 KLKAEKMIGFCSSQGVTNDDGDIVSE-LFPNEAQARVEAQ--EEKGDYNSGTVRFLRGAVKACRSGVrrchlISYQEdgA 275
Cdd:cd04236 184 ALQPIKVIFLNRSGGLRDQKHKVLPQvHLPADLPSLSDAEwlSETEQNRIQDIATLLNALPSMSSAV-----ITSAE--T 256
|
250
....*....|...
gi 15832929 276 LLQELFSRDGIGT 288
Cdd:cd04236 257 LLTELFSHKGSGT 269
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| PRK04531 |
PRK04531 |
acetylglutamate kinase; Provisional |
25-302 |
2.88e-05 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 235306 [Multi-domain] Cd Length: 398 Bit Score: 46.20 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 25 GKTFVIMLGGEAIEHENFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVTDAKTLELVKqaaGTL 104
Cdd:PRK04531 35 AERFAVIKVGGAVLRDDLEALASSLSFLQEVGLTPIVVHGAGPQLDAELDAAGIEKETVNGLRVTSPEALAIVR---KVF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 105 QLDitarlsmslnNTPLQgahinvvsgnfiiaqplgvddgvdychsgrirrideDAIHRQLDSGAIVLMGPVAVSVTGES 184
Cdd:PRK04531 112 QRS----------NLDLV------------------------------------EAVESSLRAGSIPVIASLGETPSGQI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832929 185 FNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNDDGDIVSEL-FPNEAQARVeaqeeKGDYNSGTVRFLRGAVKACRSGVR 263
Cdd:PRK04531 146 LNINADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSInLSTEYDHLM-----QQPWINGGMKLKLEQIKELLDRLP 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 15832929 264 RCHLISYQEDGALLQELFSRDGIGTQIvmESAEQIRRAT 302
Cdd:PRK04531 221 LESSVSITSPSDLAKELFTHKGSGTLV--RRGERILRAT 257
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|
| NAT_SF |
cd04301 |
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ... |
337-399 |
1.78e-04 |
|
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.
Pssm-ID: 173926 [Multi-domain] Cd Length: 65 Bit Score: 39.57 E-value: 1.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832929 337 FTIIQRDNTTIACAALYPFP-EEKIGEMACVAVHPDYRSSSRGEVLLERIAAQAKQSGLSKLFV 399
Cdd:cd04301 1 FLVAEDDGEIVGFASLSPDGsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
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