|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05279 |
PRK05279 |
N-acetylglutamate synthase; Validated |
4-440 |
0e+00 |
|
N-acetylglutamate synthase; Validated
Pssm-ID: 235386 [Multi-domain] Cd Length: 441 Bit Score: 765.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 4 METPTQFVQWLRSVAPYIHAFGGKTFVVAFPGELVASGALPVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRF 83
Cdd:PRK05279 3 KERSTEFVDWFRHSAPYINAHRGKTFVIMLGGEAIAHGNFSNIVHDIALLHSLGIRLVLVHGARPQIEEQLAARGIEPRY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 84 HDGVRITDTAALECAKEAAGELRLDIEAAFSQGLPNTPMSNAQISIVSGNFVVARPLGVIDGVDFELTGVTRKIAAEKIH 163
Cdd:PRK05279 83 HKGLRVTDAAALECVKQAAGELRLDIEARLSMGLPNTPMAGAHIRVVSGNFVTARPLGVDDGVDYQHTGEVRRIDAEAIR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 164 PILQtEDNLVLLSPLGFSPTGEIFNLTMEDVAASAAIALHADKLIFITESPMMKDAGGAELRELSSHMAEAVLQ---AGF 240
Cdd:PRK05279 163 RQLD-SGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTESQGVLDEDGELIRELSPNEAQALLEaleDGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 241 LSDSAAFYLQHAIKACNAGVDRAHIIPYEMDGSALLEVFTHDGVGTMISHENLESLRQATIEDVGGIIKLIEPLEADGTL 320
Cdd:PRK05279 242 YNSGTARFLRAAVKACRGGVRRSHLISYAEDGALLQELFTRDGIGTMIVMESLEQLRRATIDDVGGILELIRPLEEQGIL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 321 VYRGRELIEREIDQFSVIDHDGVIFGCAALYPFPESKMGEMACLTVSPDAQTQGDGERILKHMENRARAAGLTKLFVLTT 400
Cdd:PRK05279 322 VRRSREQLEREIDKFTVIERDGLIIGCAALYPFPEEKMGEMACLAVHPDYRGSGRGERLLKRIEQRARQLGLKRLFVLTT 401
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 425721803 401 RTSHWFKKRGFVPATVDDLPKDRQHMYNWQRRSQVLIKTL 440
Cdd:PRK05279 402 RTAHWFLERGFVPVDVDDLPEAKRQLYNYQRRSKVLVKDL 441
|
|
| N-Ac-Glu-synth |
TIGR01890 |
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ... |
10-440 |
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: 590.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 10 FVQWLRSVAPYIHAFGGKTFVVAFPGELVASGALPVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRFHDGVRI 89
Cdd:TIGR01890 1 FVAWFREAAPYINAHRGKTFVVGLGGELVEGGNLGNIVADIALLHSLGVRLVLVHGARPQIERILAARGRTPHYHRGLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 90 TDTAALECAKEAAGELRLDIEAAFSQGLPNTPMSNAQISIVSGNFVVARPLGVIDGVDFELTGVTRKIAAEKIHPILQtE 169
Cdd:TIGR01890 81 TDEASLEQAQQAAGTLRLAIEARLSMSLSNTPMAGSRLPVVSGNFVTARPIGVIEGVDYEHTGVIRKIDTEGIRRQLD-A 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 170 DNLVLLSPLGFSPTGEIFNLTMEDVAASAAIALHADKLIFITESPMMKDAGGAELRELSSHMAEAVLQAgFLSDSAAFYL 249
Cdd:TIGR01890 160 GSIVLLSPLGHSPTGETFNLDMEDVATSVAISLKADKLIYFTLSPGISDPDGTLAAELSPQEVESLAER-LGSETTRRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 250 QHAIKACNAGVDRAHIIPYEMDGSALLEVFTHDGVGTMISHENLESLRQATIEDVGGIIKLIEPLEADGTLVYRGRELIE 329
Cdd:TIGR01890 239 SAAVKACRGGVHRSHIVSYAEDGSLLQELFTRDGIGTSISKEAFESIRQATIDDIGGIAALIRPLEEQGILVRRSREYLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 330 REIDQFSVIDHDGVIFGCAALYPFPESKMGEMACLTVSPDAQTQGDGERILKHMENRARAAGLTKLFVLTTRTSHWFKKR 409
Cdd:TIGR01890 319 REISEFSIIEHDGNIIGCAALYPYAEEDCGEMACLAVSPEYQDGGRGERLLAHIEDRARQMGISRLFVLTTRTGHWFRER 398
|
410 420 430
....*....|....*....|....*....|.
gi 425721803 410 GFVPATVDDLPKDRQHMYNWQRRSQVLIKTL 440
Cdd:TIGR01890 399 GFQTASVDELPEARRKLYNYQRNSKILMKRL 429
|
|
| AAK_NAGS-ABP |
cd04237 |
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ... |
9-288 |
2.17e-139 |
|
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: 400.39 E-value: 2.17e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 9 QFVQWLRSVAPYIHAFGGKTFVVAFPGELVASGALPVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRFHDGVR 88
Cdd:cd04237 1 QFVDWFREAAPYINAHRGKTFVIAFGGEAVAHPNFDNIVHDIALLHSLGIRLVLVHGARPQIDQRLAERGLEPRYHRGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 89 ITDTAALECAKEAAGELRLDIEAAFSQGLPNTPMSNAQISIVSGNFVVARPLGVIDGVDFELTGVTRKIAAEKIHPILQt 168
Cdd:cd04237 81 ITDAAALECVKEAAGAVRLEIEALLSMGLPNSPMAGARIRVVSGNFVTARPLGVVDGVDFGHTGEVRRIDADAIRRQLD- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 169 EDNLVLLSPLGFSPTGEIFNLTMEDVAASAAIALHADKLIFITESPMMKDAGGAELRELSSHMAEAVLQ-AGFLSDSAAF 247
Cdd:cd04237 160 QGSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADKLIFLTDGPGLLDDDGELIRELTAQEAEALLEtGALLTNDTAR 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 425721803 248 YLQHAIKACNAGVDRAHIIPYEMDGSALLEVFTHDGVGTMI 288
Cdd:cd04237 240 LLQAAIEACRGGVPRVHLISYAEDGALLLELFTRDGVGTLI 280
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
4-289 |
2.82e-113 |
|
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: 333.92 E-value: 2.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 4 METPTQFVQWLRSVAPYIHAFGGKTFVVAFPGELVASGAL-PVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGR 82
Cdd:COG0548 1 MESAIEKAEWLREALPYIQAFRGKTFVIKYGGEAMEDEELkAALAQDIALLKSLGIRPVLVHGGGPQINELLKRLGIESE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 83 FHDGVRITDTAALECAKEA-AGELRLDIEAAFSQGLPNtpmsNAQISIVSGNFVVARPLGVIDGVDFELTGVTRKIAAEK 161
Cdd:COG0548 81 FVNGLRVTDEETLEVVEMVlAGKVNKEIVALLSQGGGN----AVGLSGKDGNLITARPLGVGDGVDLGHVGEVRRVDPEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 162 IHPILQtEDNLVLLSPLGFSPTGEIFNLTMEDVAASAAIALHADKLIFITESPMMKDAGGAELRELSSHMAEAVLQAGFL 241
Cdd:COG0548 157 IRALLD-AGYIPVISPIGYSPTGEVYNINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTAAEAEELIADGVI 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 425721803 242 SDSAAFYLQHAIKACNAGVDRAHIIPYEMDGSALLEVFTHDGVGTMIS 289
Cdd:COG0548 236 SGGMIPKLEAALDAVRGGVKRVHIIDGRVPHALLLELFTDDGIGTMIV 283
|
|
| PLN02825 |
PLN02825 |
amino-acid N-acetyltransferase |
10-440 |
5.29e-110 |
|
amino-acid N-acetyltransferase
Pssm-ID: 215441 [Multi-domain] Cd Length: 515 Bit Score: 334.05 E-value: 5.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 10 FVQWLRSVAPYIHAFGGKTFVVAFPGELVASGALPVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRFHDGVRI 89
Cdd:PLN02825 1 FVRWFREAWPYIQGHRGSTFVVVISGEVVAGPHLDNILQDISLLHGLGIKFVLVPGTHVQIDKLLAERGREPKYVGAYRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 90 TDTAALECAKEAAGELRLDIEAAFSQGLP---------NTPMSNAQISIVSGNFVVARPLGVIDGVDFELTGVTRKIAAE 160
Cdd:PLN02825 81 TDSAALQASMEAAGKIRVMIEAKLSPGPSipnlrrhgdNSRWHEVGVSVASGNFLAAKRRGVVNGVDFGATGEVKKIDVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 161 KIHPILQTeDNLVLLSPLGFSPTGEIFNLTMEDVAASAAIALHADKLIFITESPMMKDAGG-----------------AE 223
Cdd:PLN02825 161 RIKERLDS-NCIVLLSNLGYSSSGEVLNCNTYEVATACALAIGADKLICIVDGPILDENGRlirfmtleeadmlirkrAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 224 LRELSSHMAEAVLQAGF----------------------LSDSAAFYLQH------------------------------ 251
Cdd:PLN02825 240 QSEIAANYVKAVGGEDYsyslgldsvnttpfnnngrgfwGSGSATDSFQNgvgfdngnglsgeqgfaiggeerlsrlngy 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 252 ------AIKACNAGVDRAHIIPYEMDGSALLEVFTHDGVGTMISHENLESLRQATIEDVGGIIKLIEPLEADGTLVYRGR 325
Cdd:PLN02825 320 lselaaAAFVCRGGVQRVHLLDGTIEGVLLLELFTRDGMGTMIASDMYEGTRMARVEDLAGIRQIIRPLEESGILVRRTD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 326 ELIEREIDQFSVIDHDGVIFGCAALYPFPESKMGEMACLTVSPDAQTQGDGERILKHMENRARAAGLTKLFVLTTRTSHW 405
Cdd:PLN02825 400 EELLRALDSFVVVEREGSIIACAALFPFFEEKCGEVAAIAVSPECRGQGQGDKLLDYIEKKAASLGLEKLFLLTTRTADW 479
|
490 500 510
....*....|....*....|....*....|....*
gi 425721803 406 FKKRGFVPATVDDLPKDRQHMYNWQRRSQVLIKTL 440
Cdd:PLN02825 480 FVRRGFSECSIESLPEARRKRINLSRGSKYYMKKL 514
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
294-440 |
3.95e-36 |
|
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: 129.34 E-value: 3.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 294 ESLRQATIEDVGGIIKLIEPLeadgtlvyrgreLIEREIDQFSVIDHDGVIFGCAALYPFPEsKMGEMACLTVSPDAQTQ 373
Cdd:COG1246 1 MTIRPATPDDVPAILELIRPY------------ALEEEIGEFWVAEEDGEIVGCAALHPLDE-DLAELRSLAVHPDYRGR 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 425721803 374 GDGERILKHMENRARAAGLTKLFVLTTRTS-HWFKKRGFVPATVDDLPKDRQhmynWQRRSQVLIKTL 440
Cdd:COG1246 68 GIGRRLLEALLAEARELGLKRLFLLTTSAAiHFYEKLGFEEIDKEDLPYAKV----WQRDSVVMEKDL 131
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
4-291 |
1.96e-31 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 121.37 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 4 METPTQFVQWLRSVAPYIHAFGGKTFVVAFPGELVASGAL-PVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGR 82
Cdd:PRK00942 1 MIDALEKAEVLSEALPYIQRFMGKTIVIKYGGNAMTDEELkEAFARDIVLLKQVGINPVVVHGGGPQIDELLKKLGIESE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 83 FHDGVRITDTAALECAKEA-AGELRLDIEAAFSQ-GLpntpmsNA-QISIVSGNFVVARPLGviDGVDFELTGVTRKIAA 159
Cdd:PRK00942 81 FVNGLRVTDAETMEVVEMVlAGKVNKELVSLINKhGG------KAvGLSGKDGGLITAKKLE--EDEDLGFVGEVTPVNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 160 EKIHPILqtEDNLV-LLSPLGFSPTGEIFNLTMEDVAASAAIALHADKLIFITESPMMKDAGGAELRELSSHMAEAVLQA 238
Cdd:PRK00942 153 ALLEALL--EAGYIpVISPIGVGEDGETYNINADTAAGAIAAALGAEKLILLTDVPGVLDDKGQLISELTASEAEELIED 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 425721803 239 GFLSDSAAFYLQHAIKACNAGVDRAHIIpyemDG----SALLEVFTHDGVGTMISHE 291
Cdd:PRK00942 231 GVITGGMIPKVEAALDAARGGVRSVHII----DGrvphALLLELFTDEGIGTMIVPD 283
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
19-288 |
1.08e-28 |
|
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: 113.75 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 19 PYIHAFGGKTFVVAFPGELVASGAL-PVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRFHDGVRITDTAALEC 97
Cdd:cd04250 7 PYIQKFRGKTVVIKYGGNAMKDEELkESFARDIVLLKYVGINPVVVHGGGPEINEMLKKLGIESEFVNGLRVTDEETMEI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 98 AKEA-AGELRLDIEAAFSQGLPNTpmsnAQISIVSGNFVVARPL---GVIDGVDFELTGVTRKIAAEKIHPILqtEDNLV 173
Cdd:cd04250 87 VEMVlVGKVNKEIVSLINRAGGKA----VGLSGKDGNLIKAKKKdatVIEEIIDLGFVGEVTEVNPELLETLL--EAGYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 174 -LLSPLGFSPTGEIFNLTMEDVAASAAIALHADKLIFITESP-MMKDAGGAE--LRELSSHMAEAVLQAGFLSDSAAFYL 249
Cdd:cd04250 161 pVIAPVGVGEDGETYNINADTAAGAIAAALKAEKLILLTDVAgVLDDPNDPGslISEISLKEAEELIADGIISGGMIPKV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 425721803 250 QHAIKACNAGVDRAHIIpyemDG----SALLEVFTHDGVGTMI 288
Cdd:cd04250 241 EACIEALEGGVKAAHII----DGrvphSLLLEIFTDEGIGTMI 279
|
|
| argB |
CHL00202 |
acetylglutamate kinase; Provisional |
4-288 |
8.30e-26 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 133644 [Multi-domain] Cd Length: 284 Bit Score: 106.03 E-value: 8.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 4 METPTQFVQWLRSVAPYIHAFGGKTFVVAFPGELVASGALPV-LAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGR 82
Cdd:CHL00202 1 MLNNDERVQVLSEALPYIQKFRGRIMVIKYGGAAMKNLILKAdIIKDILFLSCIGLKIVVVHGGGPEINFWLKQLNISPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 83 FHDGVRITDTAALECAKEA-AGELRLDIEAAfsqgLPNTPMSNAQISIVSGNFVVARPLGVIDgvdfelTGVTRKIaaEK 161
Cdd:CHL00202 81 FWNGIRVTDKVTMEIVEMVlAGKVNKDLVGS----INANGGKAVGLCGKDANLIVARASDKKD------LGLVGEI--QQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 162 IHP----ILQTEDNLVLLSPLGFSPTGEIFNLTMEDVAASAAIALHADKLIFITESP-MMKDAGGAE--LRELSSHMAEA 234
Cdd:CHL00202 149 VDPqlidMLLEKNYIPVIASVAADHDGQTYNINADVVAGEIAAKLNAEKLILLTDTPgILADINDPNslISTLNIKEARN 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 425721803 235 VLQAGFLSDSAAFYLQHAIKACNAGVDRAHIIPYEMDGSALLEVFTHDGVGTMI 288
Cdd:CHL00202 229 LASTGIISGGMIPKVNCCIRALAQGVEAAHIIDGKEKHALLLEILTEKGIGSML 282
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
37-288 |
2.19e-24 |
|
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: 101.43 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 37 LVASGALPVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRFHDGVRITDTAALECAKEA-AGELRLDIEAAFSQ 115
Cdd:cd04238 10 MKDEELKEAFADDIVLLKQVGINPVIVHGGGPEINELLKRLGIESEFVNGLRVTDKETMEIVEMVlAGKVNKELVSLLNR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 116 ------GLpntpmsnaqiSIVSGNFVVARPLGViDGVDFELTGVTRKIAAEKIHPILqtEDNLV-LLSPLGFSPTGEIFN 188
Cdd:cd04238 90 aggkavGL----------SGKDGGLIKAEKKEE-KDIDLGFVGEVTEVNPELLETLL--EAGYIpVIAPIAVDEDGETYN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 189 LTMEDVAASAAIALHADKLIFITESPMMKDAGGAELRELSSHMAEAVLQAGFLSDSAAFYLQHAIKACNAGVDRAHIIPY 268
Cdd:cd04238 157 VNADTAAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTPKEAEELIEDGVISGGMIPKVEAALEALEGGVRKVHIIDG 236
|
250 260
....*....|....*....|
gi 425721803 269 EMDGSALLEVFTHDGVGTMI 288
Cdd:cd04238 237 RVPHSLLLELFTDEGIGTMI 256
|
|
| PLN02512 |
PLN02512 |
acetylglutamate kinase |
6-288 |
1.23e-22 |
|
acetylglutamate kinase
Pssm-ID: 178128 Cd Length: 309 Bit Score: 97.45 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 6 TPTQFVQWLRSVAPYIHAFGGKTFVVAFPGELVASGALPV-LAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRFH 84
Cdd:PLN02512 27 TNLSRVDILSEALPFIQRFRGKTVVVKYGGAAMKDPELKAgVIRDLVLLSCVGLRPVLVHGGGPEINSWLKKVGIEPQFK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 85 DGVRITDTAALECAKEA-AGELRLDIeaafsQGLPNTPMSNA-QISIVSGNFVVARPLgvIDGVDFELTGVTRKIAAEKI 162
Cdd:PLN02512 107 NGLRVTDAETMEVVEMVlVGKVNKSL-----VSLINKAGGTAvGLSGKDGRLLRARPS--PNSADLGFVGEVTRVDPTVL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 163 HPILQTEdNLVLLSPLGFSPTGEIFNLTMEDVAASAAIALHADKLIFITESP---MMKDAGGAELRELSSHMAEAVLQAG 239
Cdd:PLN02512 180 RPLVDDG-HIPVIATVAADEDGQAYNINADTAAGEIAAALGAEKLILLTDVAgvlEDKDDPGSLVKELDIKGVRKLIADG 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 425721803 240 FLSDSAAFYLQHAIKACNAGVDRAHIIPYEMDGSALLEVFTHDGVGTMI 288
Cdd:PLN02512 259 KIAGGMIPKVECCVRSLAQGVKTAHIIDGRVPHSLLLEILTDEGAGTMI 307
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
295-425 |
6.27e-18 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 85.99 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 295 SLRQATIEDVGGIIKLIEPLEADGTLVYRGRELIEREIDQFSVIDHDGVIFGCAALYPFpESKMGEMACLTVSPDAQTQG 374
Cdd:PRK12308 465 KVRPARLTDIDAIEGMVAYWAGLGENLPRSRNELVRDIGSFAVAEHHGEVTGCASLYIY-DSGLAEIRSLGVEAGWQVQG 543
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 375 DGERILKHMENRARAAGLTKLFVLtTRTSHWFKKRGFVPATVDDLP----KD-----RQH 425
Cdd:PRK12308 544 QGSALVQYLVEKARQMAIKKVFVL-TRVPEFFMKQGFSPTSKSLLPekvlKDcdqcpRQH 602
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
27-266 |
3.64e-17 |
|
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: 80.49 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 27 KTFVVAFPGELVASG-ALPVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRFHdgvRITDTAALECAKE-AAGE 104
Cdd:pfam00696 1 KRVVIKLGGSSLTDKeRLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFA---RLTDAETLEVATMdALGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 105 LRLDIEAA-FSQGLPNTPMSNAQISIVSGNFVvarplgvidgvdfelTGVTRKIAAEKIHPILQtEDNLVLLSPL-GFSP 182
Cdd:pfam00696 78 LGERLNAAlLAAGLPAVGLPAAQLLATEAGFI---------------DDVVTRIDTEALEELLE-AGVVPVITGFiGIDP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 183 TGEIFNLTMEDVAASAAIALHADKLIFITESP--MMKDAGGAE----LRELSSHMAEAVLQAGFLSDSAAFYLQHAIKAC 256
Cdd:pfam00696 142 EGELGRGSSDTLAALLAEALGADKLIILTDVDgvYTADPRKVPdaklIPEISYDELLELLASGLATGGMKVKLPAALEAA 221
|
250
....*....|
gi 425721803 257 NAGVDRAHII 266
Cdd:pfam00696 222 RRGGIPVVIV 231
|
|
| PRK07757 |
PRK07757 |
N-acetyltransferase; |
296-420 |
2.73e-14 |
|
N-acetyltransferase;
Pssm-ID: 236088 [Multi-domain] Cd Length: 152 Bit Score: 69.84 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 296 LRQATIEDVGGIIKLIEPLEADGTLVYRGRELIEREIDQFSVIDHDGVIFGCAALYPFPEsKMGEMACLTVSPDAQTQGD 375
Cdd:PRK07757 4 IRKARLSDVKAIHALINVYAKKGLMLPRSLDELYENIRDFYVAEEEGEIVGCCALHILWE-DLAEIRSLAVSEDYRGQGI 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 425721803 376 GERILKHMENRARAAGLTKLFVLTTRTsHWFKKRGFVPATVDDLP 420
Cdd:PRK07757 83 GRMLVEACLEEARELGVKRVFALTYQP-EFFEKLGFREVDKEALP 126
|
|
| argB |
TIGR00761 |
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ... |
43-265 |
1.21e-13 |
|
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: 70.00 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 43 LPVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRFHDGVRITDTAALECAKEA-AGELRLDIEAAFSQ-GLPNT 120
Cdd:TIGR00761 15 LEAFASDIAFLRAVGIKPVIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVVEMVlIGQVNKELVALLNKhGINAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 121 PMSNAqisivSGNFVVARplgVIDGVDFELTGVTRKIAAEKIHPILQtEDNLVLLSPLGFSPTGEIFNLTMEDVAASAAI 200
Cdd:TIGR00761 95 GLTGG-----DGQLFTAR---YLDKEDLGYVGEIKKVNKALIEALLK-AGYIPVISSLALTAEGQALNVNADTAAGALAA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 425721803 201 ALHADKLIFITESP-MMKDAGGAELRELSSHMAEAVLQAGFLSDSAAFYLQHAIKACNAGVDRAHI 265
Cdd:TIGR00761 166 ALGAEKLVLLTDVPgILNGDGQSLISEIPLDEIEQLIKQGIIKGGMIPKVNAALEALRGGVRSVHI 231
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
30-288 |
4.05e-13 |
|
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: 69.01 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 30 VVAFPGELVASGA-LPVLAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRFHDGVRITDTAALECAKEAAGELRLD 108
Cdd:cd02115 1 VIKFGGSSVSSEErLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDRETDALAAMGEGMSNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 109 IEAAFSQglpntpmsnaqiSIVSGNFVVARPLGVIDGvDFELTGVTRKIAAEKIHPILQtEDNLVLLSPLGFSP---TGE 185
Cdd:cd02115 81 IAAALEQ------------HGIKAVPLDLTQAGFASP-NQGHVGKITKVSTDRLKSLLE-NGILPILSGFGGTDekeTGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 186 IFNLTMEDVAASAAIALHADKLIFITESPMMKDAGGAE------LRELSSHMAEAVLQAGF--LSDSAAFYL-QHAIkac 256
Cdd:cd02115 147 LGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPRKvpdaklLSELTYEEAAELAYAGAmvLKPKAADPAaRAGI--- 223
|
250 260 270
....*....|....*....|....*....|..
gi 425721803 257 nagvdRAHIIPYEMDGsaLLEVFTHDGVGTMI 288
Cdd:cd02115 224 -----PVRIANTENPG--ALALFTPDGGGTLI 248
|
|
| PRK07922 |
PRK07922 |
amino-acid N-acetyltransferase; |
295-413 |
2.49e-12 |
|
amino-acid N-acetyltransferase;
Pssm-ID: 236132 [Multi-domain] Cd Length: 169 Bit Score: 64.94 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 295 SLRQATIEDVGGIIKLIEPLEadgtlvyRGRELIERE-------IDQFSVIDH-DGVIFGCAALYPFPESkMGEMACLTV 366
Cdd:PRK07922 7 TVRRARTSDVPAIKRLVDPYA-------QGRILLEKNlvtlyeaVQEFWVAEHlDGEVVGCGALHVMWED-LAEIRTVAV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 425721803 367 SPDAQTQGDGERILKHMENRARAAGLTKLFVLTTRTShWFKKRGFVP 413
Cdd:PRK07922 79 DPAARGRGVGHAIVERLLDVARELGLSRVFVLTFEVE-FFARHGFVE 124
|
|
| yhbS |
COG3153 |
Predicted N-acetyltransferase YhbS [General function prediction only]; |
296-420 |
1.18e-11 |
|
Predicted N-acetyltransferase YhbS [General function prediction only];
Pssm-ID: 442387 [Multi-domain] Cd Length: 142 Bit Score: 62.03 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 296 LRQATIEDVGGIIKLIE---PLEADGTLVYRGREliEREIDQFSVIDHDGVIFGCAALYPFP---ESKMGEMACLTVSPD 369
Cdd:COG3153 1 IRPATPEDAEAIAALLRaafGPGREAELVDRLRE--DPAAGLSLVAEDDGEIVGHVALSPVDidgEGPALLLGPLAVDPE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 425721803 370 AQTQGDGERILKHMENRARAAGLTKLFVLTTRTSHWF-KKRGFVPATVDDLP 420
Cdd:COG3153 79 YRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFyERFGFRPAGELGLT 130
|
|
| AAK_NAGK-fArgBP |
cd04252 |
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ... |
46-288 |
3.25e-11 |
|
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: 63.17 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 46 LAQDLSLLVGLGIRIVLVHGSRPQVAEQLALRNVEGRFHDGVRITDTAALECAKEA--AGELRLdIEAAFSQGLPNTPms 123
Cdd:cd04252 17 LAASLSFLQHVGLYPIVVHGAGPQLNEELEAAGVEPEYVDGLRVTDPETLAVARKVflEENLKL-VEALERNGARARP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 124 naqisIVSGNFvvarPLGVIDGVDFELTGVTRKIAAEKIHPILQTeDNLVLLSPLGFSPTGEIFNLTMEDVAASAAIALH 203
Cdd:cd04252 94 -----ITSGVF----EAEYLDKDKYGLVGKITGVNKAPIEAAIRA-GYLPILTSLAETPSGQLLNVNADVAAGELARVLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 204 ADKLIFITESPMMKDAGGaelrELSSHMAEAVLQAGFLSDSAAFY-----LQHaIKACNAGVDR----AHIIPYEMdgsa 274
Cdd:cd04252 164 PLKIVFLNETGGLLDGTG----KKISAINLDEEYDDLMKQPWVKYgtklkIKE-IKELLDTLPRsssvSITSPDDL---- 234
|
250
....*....|....
gi 425721803 275 LLEVFTHDGVGTMI 288
Cdd:cd04252 235 QKELFTHSGAGTLI 248
|
|
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
296-429 |
1.17e-10 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 60.01 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 296 LRQATIEDVGGIIKLIEPLEADGTLVYRGRELIEREIDQFS-----------VIDHDGVIFGCAALYPFPESKMGEMACL 364
Cdd:COG1247 4 IRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFaailapgrpvlVAEEDGEVVGFASLGPFRPRPAYRGTAE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 425721803 365 T---VSPDAQTQGDGERILKHMENRARAAGLTKLFVLTTRTSH----WFKKRGFVPatVDDLPKDRQHMYNW 429
Cdd:COG1247 84 EsiyVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEasiaLYEKLGFEE--VGTLPEVGFKFGRW 153
|
|
| Acetyltransf_7 |
pfam13508 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
331-413 |
3.98e-09 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 463905 [Multi-domain] Cd Length: 84 Bit Score: 53.23 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 331 EIDQFSVIDHDGVIFGCAALYPFPESKMGEMACLTVSPDAQTQGDGERILKHMENRARAAGLTKLFVLTTRTS-HWFKKR 409
Cdd:pfam13508 1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAaAFYEKL 80
|
....
gi 425721803 410 GFVP 413
Cdd:pfam13508 81 GFEE 84
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
325-411 |
1.13e-07 |
|
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: 50.21 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 325 RELIEREIDQFSVIDHDGVIFGCAALYPFP-ESKMGEMACLTVSPDAQTQGDGERILKHMENRARAAGLTKLFVLTTRTS 403
Cdd:pfam00583 25 EDWDEDASEGFFVAEEDGELVGFASLSIIDdEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADN 104
|
90
....*....|..
gi 425721803 404 ----HWFKKRGF 411
Cdd:pfam00583 105 laaiALYEKLGF 116
|
|
| RimI |
COG0456 |
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ... |
346-413 |
1.13e-07 |
|
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440224 [Multi-domain] Cd Length: 92 Bit Score: 49.27 E-value: 1.13e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 425721803 346 GCAALYPFPESKMGEMACLTVSPDAQTQGDGERILKHMENRARAAGLTKLFvLTTRTS-----HWFKKRGFVP 413
Cdd:COG0456 1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLR-LEVREDneaaiALYEKLGFEE 72
|
|
| PRK04531 |
PRK04531 |
acetylglutamate kinase; Provisional |
1-288 |
2.87e-06 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 235306 [Multi-domain] Cd Length: 398 Bit Score: 49.28 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 1 MRQMETPTQFVQWLRSVAP------YIHAFG---GKTFVVAFPGELVASGALPVLAQDLSLLVGLGIRIVLVHGSRPQVA 71
Cdd:PRK04531 1 QANMKTRQIIVRLLSSMASakeisqYLKRFSqldAERFAVIKVGGAVLRDDLEALASSLSFLQEVGLTPIVVHGAGPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 72 EQLALRNVEGRFHDGVRITDTAALECAKeaagelRLDIEAafsqglpNTPMSNAQISIVSgnfvvarplgvidgvdfelt 151
Cdd:PRK04531 81 AELDAAGIEKETVNGLRVTSPEALAIVR------KVFQRS-------NLDLVEAVESSLR-------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425721803 152 gvtrkiaAEKIhPILqtednlvllSPLGFSPTGEIFNLTMEDVAASAAIALHADKLIFITESPMMKDAGGAELRELSSHM 231
Cdd:PRK04531 128 -------AGSI-PVI---------ASLGETPSGQILNINADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLST 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 425721803 232 AEAVLQAGFLSDSAAFYLQHAIKACNAGVDRAHIIPYEMDGSALLEVFTHDGVGTMI 288
Cdd:PRK04531 191 EYDHLMQQPWINGGMKLKLEQIKELLDRLPLESSVSITSPSDLAKELFTHKGSGTLV 247
|
|
| Citrate_lyase_ligase |
cd02169 |
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ... |
363-418 |
6.64e-03 |
|
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.
Pssm-ID: 173920 [Multi-domain] Cd Length: 297 Bit Score: 38.40 E-value: 6.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 425721803 363 CLTVSPDAQTQGDGERILKHMENRARAAGLTKLFVLT-TRTSHWFKKRGFVP-ATVDD 418
Cdd:cd02169 30 CVAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTkPKNAKFFRGLGFKElANASD 87
|
|
| |
