|
Name |
Accession |
Description |
Interval |
E-value |
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
577-718 |
1.31e-17 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 80.81 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 577 SFFIRPAEPEDCPDILRLIKE-----LASYEgmEEKVSLTER-DLFRDGfgDNPLFYCLVAEapseqtESGvKTIGFAmY 650
Cdd:COG1247 1 EMTIRPATPEDAPAIAAIYNEaiaegTATFE--TEPPSEEEReAWFAAI--LAPGRPVLVAE------EDG-EVVGFA-S 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254587975 651 YFTYDPRIG-KLLHLEDFYITEDYQGIGIGADMLKKLSQIAINTECCGMQFLVIIWNQDSVEYYTRLGA 718
Cdd:COG1247 69 LGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
612-717 |
1.23e-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: 56.37 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 612 ERDLFRDGFGDNPLFYCLVAEapseqtesGVKTIGFAMYYFTYDPriGKLLHLEDFYITEDYQGIGIGADMLKKLSQIAI 691
Cdd:pfam00583 20 PLDLLEDWDEDASEGFFVAEE--------DGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGTALLQALLEWAR 89
|
90 100
....*....|....*....|....*.
gi 254587975 692 NTECCGMQFLVIIWNQDSVEYYTRLG 717
Cdd:pfam00583 90 ERGCERIFLEVAADNLAAIALYEKLG 115
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
18-550 |
2.92e-06 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 50.85 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 18 QPAM-SPPGLSPhnmqQPGTSQPYMNQPSMNQPAMNEPGVTIPDSSQSDINQAGQSQPNMKQPWSSTNQP-GIYKTDMSQ 95
Cdd:PRK10263 338 EPVTqTPPVASV----DVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPqQPYYAPAAE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 96 LGMKQPSASQAGMSQAGMWQPGPPTSDMKTINPWQWDPEYSGREPSDTWQITQSNQGTGQSDTVQEDPSCAEQK-----Q 170
Cdd:PRK10263 414 QPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQpvvepE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 171 PDTWKQDPSFPGMKKTEPWQwESSPPSVRQIDAWKWDPDHPGSnqlnlwQPQLSDSSTRQFDLRQAGPIELGKKESDTWQ 250
Cdd:PRK10263 494 PVVEETKPARPPLYYFEEVE-EKRAREREQLAAWYQPIPEPVK------EPEPIKSSLKAPSVAAVPPVEAAAAVSPLAS 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 251 LVPSQQGKTPSSSGQQDPSQQIVRHAvtwqtGPSPLAKTLSGPwhiGLNQSGMEQLNTCQ--TGFGQRYSMCQSSGSQSS 328
Cdd:PRK10263 567 GVKKATLATGAAATVAAPVFSLANSG-----GPRPQVKEGIGP---QLPRPKRIRVPTRRelASYGIKLPSQRAAEEKAR 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 329 MKEFHMLQSGSNQPDmNDVDVWQSGTSQPGMHQMDPWQWGHNYSGNTQ--------------------------SGQWTP 382
Cdd:PRK10263 639 EAQRNQYDSGDQYND-DEIDAMQQDELARQFAQTQQQRYGEQYQHDVPvnaedadaaaeaelarqfaqtqqqrySGEQPA 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 383 GPNALVVGQFDswqpVQPGMKYSESGPWSPRHLDMRQPSPSQLATRQFDKWQQNPSMPGVRQLYTWQPTSSFSDTRQLEK 462
Cdd:PRK10263 718 GANPFSLDDFE----FSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 463 -FHPCPINLNMEQFWEAVSRQPGTTQLGTNQLDTNQPDGTQSSQGGKTQSDKLEP-----SPRKPEMKGSQPDTSqsdsd 536
Cdd:PRK10263 794 pQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTLLHPllmrnGDSRPLHKPTTPLPS----- 868
|
570
....*....|....
gi 254587975 537 hLDISQPGPSQLEP 550
Cdd:PRK10263 869 -LDLLTPPPSEVEP 881
|
|
| Glutenin_hmw |
pfam03157 |
High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
3-412 |
9.67e-05 |
|
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.
Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 45.71 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 3 QPGTYQSGMTQPSVSQPAMSPPGLSPHNMQQPGTSQPYMNQPSMNQPAMNEPGVTIPDSSQSDINQAGQSQPNMKQPwsS 82
Cdd:pfam03157 331 QPGQGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQP--G 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 83 TNQPGIYKTDMSQLGMKQPSASQAGMSQAGMWQPGPPTSDMKTINPWQWDPEYSGREPSDTWQITQSNQ-GTGQSDTVQE 161
Cdd:pfam03157 409 QGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQQpGQGQPGYYPT 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 162 DPSCAEQ-KQPDTWKQD-PSFPGMKKTEPWQwesspPSVRQIDAWKWDPDHPGSNQlNLWQPQLSDSSTRQFDLRQAGPI 239
Cdd:pfam03157 489 SPQQSGQgQQLGQWQQQgQGQPGYYPTSPLQ-----PGQGQPGYYPTSPQQPGQGQ-QLGQLQQPTQGQQGQQSGQGQQG 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 240 ELGKKESDTWQLVPSQQGKTPSSSGQQDPSQQIVRHAVTWQTGPSPLAKTLSGPwhiGLNQSGMEQLNTCQTGFGQR-YS 318
Cdd:pfam03157 563 QQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQQPGQWQQP---GQGQPGYYPTSSLQLGQGQQgYY 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 319 MCQSSGSQSSMKEFHMLQSGSNQPDMNDVDVWQSGTSQPGMHQMDPWQWGHnySGNTQSGQWTPGPNALVVGQfDSWQPV 398
Cdd:pfam03157 640 PTSPQQPGQGQQPGQWQQSGQGQQGYYPTSPQQSGQAQQPGQGQQPGQWLQ--PGQGQQGYYPTSPQQPGQGQ-QLGQGQ 716
|
410
....*....|....
gi 254587975 399 QPGMKYSESGPWSP 412
Cdd:pfam03157 717 QSGQGQQGYYPTSP 730
|
|
| NAT_SF |
cd04301 |
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ... |
645-698 |
4.08e-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: 39.18 E-value: 4.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 254587975 645 IGFAMYYFtyDPRIGKLLHLEDFYITEDYQGIGIGADMLKKLSQIAINTECCGM 698
Cdd:cd04301 11 VGFASLSP--DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
|
|
| PTZ00330 |
PTZ00330 |
acetyltransferase; Provisional |
663-717 |
8.91e-03 |
|
acetyltransferase; Provisional
Pssm-ID: 140351 [Multi-domain] Cd Length: 147 Bit Score: 37.51 E-value: 8.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 254587975 663 HLEDFYITEDYQGIGIGADMLKKLSQIAINTECcgmqFLVII-WNQDSVEYYTRLG 717
Cdd:PTZ00330 84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGC----YKVILdCTEDMVAFYKKLG 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
577-718 |
1.31e-17 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 80.81 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 577 SFFIRPAEPEDCPDILRLIKE-----LASYEgmEEKVSLTER-DLFRDGfgDNPLFYCLVAEapseqtESGvKTIGFAmY 650
Cdd:COG1247 1 EMTIRPATPEDAPAIAAIYNEaiaegTATFE--TEPPSEEEReAWFAAI--LAPGRPVLVAE------EDG-EVVGFA-S 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254587975 651 YFTYDPRIG-KLLHLEDFYITEDYQGIGIGADMLKKLSQIAINTECCGMQFLVIIWNQDSVEYYTRLGA 718
Cdd:COG1247 69 LGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
|
|
| yhbS |
COG3153 |
Predicted N-acetyltransferase YhbS [General function prediction only]; |
580-717 |
1.75e-11 |
|
Predicted N-acetyltransferase YhbS [General function prediction only];
Pssm-ID: 442387 [Multi-domain] Cd Length: 142 Bit Score: 62.41 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 580 IRPAEPEDCPDILRLIKElaSYEGMEEkvslteRDLFRDGFGDNPLFYCLVAEapseqtESGvKTIGFAMYYFTYDPRIG 659
Cdd:COG3153 1 IRPATPEDAEAIAALLRA--AFGPGRE------AELVDRLREDPAAGLSLVAE------DDG-EIVGHVALSPVDIDGEG 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 254587975 660 KLLHLEDFYITEDYQGIGIGADMLKKLSQIAINTeccGMQFLVIIWNQDSVEYYTRLG 717
Cdd:COG3153 66 PALLLGPLAVDPEYRGQGIGRALMRAALEAARER---GARAVVLLGDPSLLPFYERFG 120
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
612-717 |
1.23e-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: 56.37 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 612 ERDLFRDGFGDNPLFYCLVAEapseqtesGVKTIGFAMYYFTYDPriGKLLHLEDFYITEDYQGIGIGADMLKKLSQIAI 691
Cdd:pfam00583 20 PLDLLEDWDEDASEGFFVAEE--------DGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGTALLQALLEWAR 89
|
90 100
....*....|....*....|....*.
gi 254587975 692 NTECCGMQFLVIIWNQDSVEYYTRLG 717
Cdd:pfam00583 90 ERGCERIFLEVAADNLAAIALYEKLG 115
|
|
| RimI |
COG0456 |
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ... |
646-717 |
2.50e-09 |
|
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440224 [Multi-domain] Cd Length: 92 Bit Score: 54.66 E-value: 2.50e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254587975 646 GFAMYYFTYDPRIGkllHLEDFYITEDYQGIGIGADMLKKLSQIAINTECCGMQFLVIIWNQDSVEYYTRLG 717
Cdd:COG0456 1 GFALLGLVDGGDEA---EIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLG 69
|
|
| PhnO |
COG0454 |
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ... |
580-717 |
2.26e-08 |
|
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];
Pssm-ID: 440222 [Multi-domain] Cd Length: 136 Bit Score: 53.52 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 580 IRPAEPEDcpdilrlIKELASYEGMEEkvSLTERDlfrdgfGDNPLFYCLVAEAPSeqtesgvKTIGFAMYYFTYDPRig 659
Cdd:COG0454 3 IRKATPED-------INFILLIEALDA--ELKAME------GSLAGAEFIAVDDKG-------EPIGFAGLRRLDDKV-- 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 254587975 660 klLHLEDFYITEDYQGIGIGADMLKKLSQIAINTECCGMQFLVIIWNQDSVEYYTRLG 717
Cdd:COG0454 59 --LELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLG 114
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
580-717 |
1.34e-07 |
|
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: 51.15 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 580 IRPAEPEDCPDILRLIKELASYEgmeekvslterdlfrdgfgdnPLFYCLVAEapseqtESGvKTIGFAMYYftydPRIG 659
Cdd:COG1246 3 IRPATPDDVPAILELIRPYALEE---------------------EIGEFWVAE------EDG-EIVGCAALH----PLDE 50
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 254587975 660 KLLHLEDFYITEDYQGIGIGADMLKKLSQIAINTeccGMQFLVIIWNQDSVEYYTRLG 717
Cdd:COG1246 51 DLAELRSLAVHPDYRGRGIGRRLLEALLAEAREL---GLKRLFLLTTSAAIHFYEKLG 105
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
18-550 |
2.92e-06 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 50.85 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 18 QPAM-SPPGLSPhnmqQPGTSQPYMNQPSMNQPAMNEPGVTIPDSSQSDINQAGQSQPNMKQPWSSTNQP-GIYKTDMSQ 95
Cdd:PRK10263 338 EPVTqTPPVASV----DVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPqQPYYAPAAE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 96 LGMKQPSASQAGMSQAGMWQPGPPTSDMKTINPWQWDPEYSGREPSDTWQITQSNQGTGQSDTVQEDPSCAEQK-----Q 170
Cdd:PRK10263 414 QPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQpvvepE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 171 PDTWKQDPSFPGMKKTEPWQwESSPPSVRQIDAWKWDPDHPGSnqlnlwQPQLSDSSTRQFDLRQAGPIELGKKESDTWQ 250
Cdd:PRK10263 494 PVVEETKPARPPLYYFEEVE-EKRAREREQLAAWYQPIPEPVK------EPEPIKSSLKAPSVAAVPPVEAAAAVSPLAS 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 251 LVPSQQGKTPSSSGQQDPSQQIVRHAvtwqtGPSPLAKTLSGPwhiGLNQSGMEQLNTCQ--TGFGQRYSMCQSSGSQSS 328
Cdd:PRK10263 567 GVKKATLATGAAATVAAPVFSLANSG-----GPRPQVKEGIGP---QLPRPKRIRVPTRRelASYGIKLPSQRAAEEKAR 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 329 MKEFHMLQSGSNQPDmNDVDVWQSGTSQPGMHQMDPWQWGHNYSGNTQ--------------------------SGQWTP 382
Cdd:PRK10263 639 EAQRNQYDSGDQYND-DEIDAMQQDELARQFAQTQQQRYGEQYQHDVPvnaedadaaaeaelarqfaqtqqqrySGEQPA 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 383 GPNALVVGQFDswqpVQPGMKYSESGPWSPRHLDMRQPSPSQLATRQFDKWQQNPSMPGVRQLYTWQPTSSFSDTRQLEK 462
Cdd:PRK10263 718 GANPFSLDDFE----FSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 463 -FHPCPINLNMEQFWEAVSRQPGTTQLGTNQLDTNQPDGTQSSQGGKTQSDKLEP-----SPRKPEMKGSQPDTSqsdsd 536
Cdd:PRK10263 794 pQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTLLHPllmrnGDSRPLHKPTTPLPS----- 868
|
570
....*....|....
gi 254587975 537 hLDISQPGPSQLEP 550
Cdd:PRK10263 869 -LDLLTPPPSEVEP 881
|
|
| PTZ00395 |
PTZ00395 |
Sec24-related protein; Provisional |
14-111 |
7.78e-06 |
|
Sec24-related protein; Provisional
Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 49.69 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 14 PSVSQPAMSPPGLSPHNMQQPGTSQPYMNQPSMNQPAMNEPGVTIPDSSQSDINQAGQSQPnmkqPWSSTNQPGIYKTDM 93
Cdd:PTZ00395 413 GYSNPGNSNPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNTPYSNAPLSNAP----PSSAKDHHSAYHAAY 488
|
90
....*....|....*...
gi 254587975 94 SQLGMKQPSASQAGMSQA 111
Cdd:PTZ00395 489 QHRAANQPAANLPTANQP 506
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1-198 |
9.32e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 1 MDQPGTYQSGMTQPsvsQPAMSPPGLSPHNMQQPGTSQPYMNQPSMNQPAMNEPGVT-IPDSSQSDINQAGQSQPNMKQP 79
Cdd:PHA03247 2886 LARPAVSRSTESFA---LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPqPPLAPTTDPAGAGEPSGAVPQP 2962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 80 WSSTNQPGIYKTDMSQLGMKQPSA----------SQAGMSQAGMWQPG---------PPTSDMKTInpwqWDPeySGREP 140
Cdd:PHA03247 2963 WLGALVPGRVAVPRFRVPQPAPSReapasstpplTGHSLSRVSSWASSlalheetdpPPVSLKQTL----WPP--DDTED 3036
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254587975 141 SDTWQITQSNqgTGQSDTVQEDPSCAEQKQPDTWKQDPSFPGMKKTEPWQWESSPPSV 198
Cdd:PHA03247 3037 SDADSLFDSD--SERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGPPPL 3092
|
|
| Glutenin_hmw |
pfam03157 |
High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
3-412 |
9.67e-05 |
|
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.
Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 45.71 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 3 QPGTYQSGMTQPSVSQPAMSPPGLSPHNMQQPGTSQPYMNQPSMNQPAMNEPGVTIPDSSQSDINQAGQSQPNMKQPwsS 82
Cdd:pfam03157 331 QPGQGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQP--G 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 83 TNQPGIYKTDMSQLGMKQPSASQAGMSQAGMWQPGPPTSDMKTINPWQWDPEYSGREPSDTWQITQSNQ-GTGQSDTVQE 161
Cdd:pfam03157 409 QGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQQpGQGQPGYYPT 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 162 DPSCAEQ-KQPDTWKQD-PSFPGMKKTEPWQwesspPSVRQIDAWKWDPDHPGSNQlNLWQPQLSDSSTRQFDLRQAGPI 239
Cdd:pfam03157 489 SPQQSGQgQQLGQWQQQgQGQPGYYPTSPLQ-----PGQGQPGYYPTSPQQPGQGQ-QLGQLQQPTQGQQGQQSGQGQQG 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 240 ELGKKESDTWQLVPSQQGKTPSSSGQQDPSQQIVRHAVTWQTGPSPLAKTLSGPwhiGLNQSGMEQLNTCQTGFGQR-YS 318
Cdd:pfam03157 563 QQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQQPGQWQQP---GQGQPGYYPTSSLQLGQGQQgYY 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 319 MCQSSGSQSSMKEFHMLQSGSNQPDMNDVDVWQSGTSQPGMHQMDPWQWGHnySGNTQSGQWTPGPNALVVGQfDSWQPV 398
Cdd:pfam03157 640 PTSPQQPGQGQQPGQWQQSGQGQQGYYPTSPQQSGQAQQPGQGQQPGQWLQ--PGQGQQGYYPTSPQQPGQGQ-QLGQGQ 716
|
410
....*....|....
gi 254587975 399 QPGMKYSESGPWSP 412
Cdd:pfam03157 717 QSGQGQQGYYPTSP 730
|
|
| Acetyltransf_7 |
pfam13508 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
624-717 |
2.58e-04 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 463905 [Multi-domain] Cd Length: 84 Bit Score: 40.13 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587975 624 PLFYCLVAEApseqtesGVKTIGFAMYYFTYDPRIGKLLHLedfYITEDYQGIGIGADMLKKLSQIAINTECCGMQFLVi 703
Cdd:pfam13508 1 PGGRFFVAED-------DGKIVGFAALLPLDDEGALAELRL---AVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET- 69
|
90
....*....|....
gi 254587975 704 iwNQDSVEYYTRLG 717
Cdd:pfam13508 70 --TNRAAAFYEKLG 81
|
|
| NAT_SF |
cd04301 |
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ... |
645-698 |
4.08e-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: 39.18 E-value: 4.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 254587975 645 IGFAMYYFtyDPRIGKLLHLEDFYITEDYQGIGIGADMLKKLSQIAINTECCGM 698
Cdd:cd04301 11 VGFASLSP--DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
|
|
| PTZ00330 |
PTZ00330 |
acetyltransferase; Provisional |
663-717 |
8.91e-03 |
|
acetyltransferase; Provisional
Pssm-ID: 140351 [Multi-domain] Cd Length: 147 Bit Score: 37.51 E-value: 8.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 254587975 663 HLEDFYITEDYQGIGIGADMLKKLSQIAINTECcgmqFLVII-WNQDSVEYYTRLG 717
Cdd:PTZ00330 84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGC----YKVILdCTEDMVAFYKKLG 135
|
|
| |
