|
Name |
Accession |
Description |
Interval |
E-value |
| HypF |
COG0068 |
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ... |
9-753 |
0e+00 |
|
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 439838 [Multi-domain] Cd Length: 757 Bit Score: 1070.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 9 ITKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNIGGLVEIILQSSEEKYNEFLQDLKANAPVGSEITNIETEDIKERE 88
Cdd:COG0068 2 KRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEEALEAFLEALRAEAPPLARIDSIEVEELPPEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 89 FDGFRIIESKDDEEI-SIIPPDLPVCESCERELFTGTDRRFLNPFISCMSCGARYTIIEELPYDRHNTTMRDFDMCPACR 167
Cdd:COG0068 82 FDGFRILESEAGGGGrTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPDCA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 168 EEYTSPRNRRFHAQTISCNDCGPYLIFNDLTGGSELTEKDAFHAAANIIESGGIIAVKGIGGYHFACSPFLEDTVLRLRE 247
Cdd:COG0068 162 AEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEGDDAIAAAAELLRAGKIVAIKGLGGFHLACDATNEEAVARLRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 248 LKGREAKPFAIMFESVDSIRKYCVVSEKEEELLKSKARPIVLLYLKNNS-MAPSACQGSIYCGAFLPYTPLHMLLVKRCG 326
Cdd:COG0068 242 RKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARPIVLLPKRPDSpLAPSVAPGLDTLGVMLPYTPLHHLLLDELG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 327 -PLIMTSANISDKPIIKDDSEMLSLKSPLLNGVLYNKRRIVRSVDDSVAKVVANSPQLIRRSRGYVPYPVFLKNRKKdlQ 405
Cdd:COG0068 322 rPLVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVVRVIDGKPRFLRRARGYAPLPIPLPFELP--P 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 406 IFAAGSDLKAAFCLYKNGNAVMSQYFGDLEEKTVLERYKASFRDLCHLLKITPDIAVCDMHPNYHSSRFAENL---GIPL 482
Cdd:COG0068 400 VLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLSTRLAEELaerGLPL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 483 TYVQHHHAHVASVMAEHHLKEQVIGVAFDGTGYGTDGKIWGGEFLICEGAEFKRVAHLRYIPVLGGDSSMRDAAKTAACF 562
Cdd:COG0068 480 IEVQHHHAHIAAVMAEHGLDGPVLGIALDGTGYGDDGTIWGGEFLLGDYAGFERVGHLRPFPLPGGDKAAREPWRMALAL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 563 LLNLGLD-------QYVKDERKDIIKAALKNNINTVPTSSMGRLFDAVSSLLEIQYENRYEGECAAMLEKeavLALRHKi 635
Cdd:COG0068 560 LYEAGGEellepllKRFSEKELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDEISYEGQAAMELEA---LADRAE- 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 636 EPKKLAFEIKRKSDLIEIDPKPMLKSMCH-LQNKDDTGSLALGFHYAVADMILEVCEIIRAEQKINTVALSGGVFQNTLL 714
Cdd:COG0068 636 EAEPYPFPLREIDGLLVLDWAPLLRALLEdLQAGVPPAEIAARFHNTLAEAIAELALRLAERTGIDTVALSGGVFQNRLL 715
|
730 740 750
....*....|....*....|....*....|....*....
gi 316939615 715 MERTLKILRDRHFNVYYNMSVPPNDGSIGLGQTFIGLVR 753
Cdd:COG0068 716 LELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAAR 754
|
|
| hypF |
TIGR00143 |
[NiFe] hydrogenase maturation protein HypF; A previously described regulatory effect of HypF ... |
45-746 |
0e+00 |
|
[NiFe] hydrogenase maturation protein HypF; A previously described regulatory effect of HypF mutatation is attributable to loss of activity of a regulatory hydrogenase. A zinc finger-like region CXXCX(18)CXXCX(24)CXXCX(18)CXXC region further supported the regulatory hypothesis. However, more recent work (PUBMED:11375153) shows the direct effect is on the activity of expressed hydrogenases with nickel/iron centers, rather than on expression. [Protein fate, Protein modification and repair]
Pssm-ID: 272929 [Multi-domain] Cd Length: 711 Bit Score: 653.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 45 GGLVEIILQSSEEKynEFLQDLKANAPVGSEITNIETEDIKERE-FDGFRIIESKDD--EEISIIPPDLPVCESCERELF 121
Cdd:TIGR00143 2 GDGVEIVLEADKEE--SFLNRLKKGLPPLARIEKIIIEPFDGAEhFTTFRIRESKNGglSLLSIIPADVATCSDCLEEML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 122 TGTDRRFLNPFISCMSCGARYTIIEELPYDRHNTTMRDFDMCPACREEYTSPRNRRFHAQTISCNDCGPYLIFndLTGGS 201
Cdd:TIGR00143 80 DKNDRRYLYPFISCTHCGPRFTIIEALPYDRENTSMADFPLCPDCAKEYKDPLDRRFHAQPIACPRCGPQLNF--VSRGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 202 ELTEKDAFHAAANIIESGGIIAVKGIGGYHFACSPFLEDTVLRLRELKGREAKPFAIMFESVDSIRKYCVVSEKEEELLK 281
Cdd:TIGR00143 158 HAEQDDALLEAAKLLKKGKIIAIKGIGGFHLACDARNDEVVERLRLRKNRPLKPFAVMSPDLESAEQHAELNNLECELLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 282 SKARPIVLLYLKNNS-MAPSACQGSIYCGAFLPYTPLHMLLVKRCG-PLIMTSANISDKPIIKDDSEMLSLKSPLLNGVL 359
Cdd:TIGR00143 238 SPAAPIVLLRKKPDIkLAPNIAPNLPTIGVMLPYTPLHHLLLQLLAfPLVMTSANLPGLPMAIDNAEILDKLQGIADGFL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 360 YNKRRIVRSVDDSVAKVVANSPQLIRRSRGYVPYPVFLKNRKKDLQIFAAGSDLKAAFCLYKNGNAVMSQYFGDLEEKTV 439
Cdd:TIGR00143 318 VHNRRIVNRVDDSVVQHVAGEILFLRRSRGFAPQPLTLPPNGNPKKILALGAELKNTFSLLKGGQAYLSQHIGDLSVYET 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 440 LERYKASFRDLCHLLKITPDIAVCDMHPNYHSSRFAENLGIPLTYVQHHHAHVASVMAEH-HLKEQVIGVAFDGTGYGTD 518
Cdd:TIGR00143 398 YKFFKEALNFFLRIYDFEPQDIVCDLHPQYNTTQYAEELSLPVLRVQHHHAHALAVMADAgVLEEAVIGITWDGVGYGED 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 519 GKIWGGEFLICEGAEFKRVAHLRYIPVLGGDSSMRDAAKTAACFL----LNLGLDQYVKDERKD----IIKAALKNNINT 590
Cdd:TIGR00143 478 GKIWGGECLLIDLGRIERLGRLEEFWLLGGDLATKYPLRILLSILlkhdLNDFLKRYQKYFKQEkelsVLQQALEKKINA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 591 VPTSSMGRLFDAVSSLLEIQYENRYEGECAAMLEKEAVLALRHKIEPkklaFEIKRKS-DLIEIDPKPMLKsmchLQNKD 669
Cdd:TIGR00143 558 PLTTSTGRLFDAVAAALGLCGERTYEGEAAIALEALALRSDGIANYP----FEIKNKVlDLKEFYQRFLED----LLVGE 629
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 316939615 670 DTGSLALGFHYAVADMILEVCEIIRAEQKINTVALSGGVFQNTLLMERTLKILRDRHFNVYYNMSVPPNDGSIGLGQ 746
Cdd:TIGR00143 630 DRSKIAHIAHKFVASGLVEIATAIAVPFGIHKIVISGGVFYNRLLLERLAKYLKGLGFQFLFHRHLPPGDGGISLGQ 706
|
|
| Sua5_yciO_yrdC |
pfam01300 |
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ... |
214-385 |
3.00e-45 |
|
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain is found in SUA5 as well as HypF and YrdC. It has also been shown to be required for telomere recombniation in yeast.
Pssm-ID: 460153 [Multi-domain] Cd Length: 176 Bit Score: 159.60 E-value: 3.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 214 NIIESGGIIAVKGIGGYHFACSPFLEDTVLRLRELKGREA-KPFAIMFESVDSIRKYCvvSEKEEELLKSKAR----PIV 288
Cdd:pfam01300 1 EALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRdKPLAVMVADLEDLKEYA--EEVEEAALRLAERfwpgPLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 289 LLYLKNNSMAPSA-CQGSIYCGAFLPYTPLHMLLVKRCG-PLIMTSANISDKPIIKDDSEMLSLKSPLLNGVLYNKrRIV 366
Cdd:pfam01300 79 LVLKASKKPLPKLlTPGLGTVGVRLPDHPLALLLLEALGePLVATSANLSGEPSPTDAEEILEELGGRVDLILDGG-RIA 157
|
170
....*....|....*....
gi 316939615 367 RSVDDSVAKVVANSPQLIR 385
Cdd:pfam01300 158 GGVPSTVVDLTGGPPRILR 176
|
|
| HypF_C |
pfam17788 |
HypF Kae1-like domain; This domain is found in the HypF protein. In the structure it is one of ... |
401-498 |
9.37e-44 |
|
HypF Kae1-like domain; This domain is found in the HypF protein. In the structure it is one of the two subdomains of the Kae1 domain.
Pssm-ID: 436045 [Multi-domain] Cd Length: 99 Bit Score: 152.63 E-value: 9.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 401 KKDLQIFAAGSDLKAAFCLYKNGNAVMSQYFGDLEEKTVLERYKASFRDLCHLLKITPDIAVCDMHPNYHSSRFAENL-G 479
Cdd:pfam17788 1 KAKPPVLALGAELKNTFALAKGGQAFLSQHIGDLDNLETLEAFEETLEHLLRLYGIKPEVIACDLHPDYLSTRLAEELnG 80
|
90
....*....|....*....
gi 316939615 480 IPLTYVQHHHAHVASVMAE 498
Cdd:pfam17788 81 LPLIEVQHHHAHIAAVMAE 99
|
|
| Acylphosphatase |
pfam00708 |
Acylphosphatase; |
11-94 |
1.48e-25 |
|
Acylphosphatase;
Pssm-ID: 425830 Cd Length: 85 Bit Score: 100.74 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 11 KRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNIG-GLVEIILQSSEEKYNEFLQDLKaNAPVGSEITNIETEDIKER-E 88
Cdd:pfam00708 1 KKVLVTGRVQGVGFRPFVYRLAKELGLKGWVRNLPdGSVEIVVQGPEEDVDKFLEWLK-SGPPPARVDKVEVTEIDEPgD 79
|
....*.
gi 316939615 89 FDGFRI 94
Cdd:pfam00708 80 FSGFEI 85
|
|
| AcyP |
COG1254 |
Acylphosphatase [Energy production and conversion]; |
9-95 |
2.01e-22 |
|
Acylphosphatase [Energy production and conversion];
Pssm-ID: 440866 Cd Length: 89 Bit Score: 91.75 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 9 ITKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKANaPVGSEITNIETEDIKER 87
Cdd:COG1254 2 KRVRIIVSGRVQGVGFRAFTRRQARRLGLTGWVRNLpDGSVEVVAEGEEEAVEAFLEWLRKG-PPAARVEDVEVEEEEPT 80
|
....*....
gi 316939615 88 -EFDGFRII 95
Cdd:COG1254 81 gEFEGFEIR 89
|
|
| PRK14431 |
PRK14431 |
acylphosphatase; Provisional |
11-95 |
3.84e-15 |
|
acylphosphatase; Provisional
Pssm-ID: 184677 Cd Length: 89 Bit Score: 71.37 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 11 KRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNIGGLVEIILQSSEEKYNEFLQDLKANAPVGSEITNIETEDIK-EREF 89
Cdd:PRK14431 4 IHLQVFGRVQGVGFRYFTQRIAMNYNIVGTVQNVDDYVEIYAQGDDADLERFIQGVIEGASPASNVTSYQLEELElNQKL 83
|
....*.
gi 316939615 90 DGFRII 95
Cdd:PRK14431 84 SDFRSI 89
|
|
| zf-HYPF |
pfam07503 |
HypF finger; The HypF family of proteins are involved in the maturation and regulation of ... |
163-192 |
8.29e-14 |
|
HypF finger; The HypF family of proteins are involved in the maturation and regulation of hydrogenase. In the N-terminus they appear to have two Zinc finger domains, as modelled by this family.
Pssm-ID: 462187 [Multi-domain] Cd Length: 33 Bit Score: 65.45 E-value: 8.29e-14
10 20 30
....*....|....*....|....*....|
gi 316939615 163 CPACREEYTSPRNRRFHAQTISCNDCGPYL 192
Cdd:pfam07503 1 CPDCLREYFDPLDRRFHAQFIACTNCGPRL 30
|
|
| PRK14420 |
PRK14420 |
acylphosphatase; Provisional |
12-97 |
9.82e-12 |
|
acylphosphatase; Provisional
Pssm-ID: 237710 Cd Length: 91 Bit Score: 61.74 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 12 RITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKANAPVgSEITNIETEDIKERE-F 89
Cdd:PRK14420 5 HIIVDGRVQGVGFRYFVQMEADKRKLTGWVKNRdDGTVEIEAEGPEEALQLFLDAIEKGSPF-SKVTDVHIEERDVLSgE 83
|
....*...
gi 316939615 90 DGFRIIES 97
Cdd:PRK14420 84 KQFRIMYG 91
|
|
| TIGR00057 |
TIGR00057 |
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ... |
202-339 |
2.82e-11 |
|
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has paralogs, but YrdC called a tRNA modification protein. Ref 2 authors say probably heteromultimeric complex. Paralogs may mean its does the final binding to the tRNA. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 272879 [Multi-domain] Cd Length: 201 Bit Score: 63.50 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 202 ELTEKDAFHAAANIIESGGIIAVKGIGGYHFACSPFLEDTVLRLRELKGREA-KPFAIMFESVDSIRKYCVVSEKEEELL 280
Cdd:TIGR00057 4 ENPSQRGIEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSnKPLTVLVSDLSEIEKYAYVPDDAKRLM 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 316939615 281 KSKAR-PIVLLYLKNNSMAPSACQGSIYCGAFLPYTPLHMLLVKRCG-PLIMTSANISDKP 339
Cdd:TIGR00057 84 KKFWPgPLTLVLKKTPEIPRRVSGKRKTIGIRVPDNPIALELLEELGkPIVATSANLSGKP 144
|
|
| PRK14435 |
PRK14435 |
acylphosphatase; Provisional |
12-94 |
4.72e-11 |
|
acylphosphatase; Provisional
Pssm-ID: 184681 Cd Length: 90 Bit Score: 59.54 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 12 RITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKANAPVGSeITNIETEDIKEREFD 90
Cdd:PRK14435 5 KIRVEGIVQGVGFRYFTRRVAKSLGVKGYVMNMdDGSVFIHAEGDENALRRFLNEVAKGPPAAV-VTNVSVEETTPEGYE 83
|
....
gi 316939615 91 GFRI 94
Cdd:PRK14435 84 DFTI 87
|
|
| zf-HYPF |
pfam07503 |
HypF finger; The HypF family of proteins are involved in the maturation and regulation of ... |
113-145 |
1.17e-10 |
|
HypF finger; The HypF family of proteins are involved in the maturation and regulation of hydrogenase. In the N-terminus they appear to have two Zinc finger domains, as modelled by this family.
Pssm-ID: 462187 [Multi-domain] Cd Length: 33 Bit Score: 56.59 E-value: 1.17e-10
10 20 30
....*....|....*....|....*....|...
gi 316939615 113 CESCERELFTGTDRRFLNPFISCMSCGARYTII 145
Cdd:pfam07503 1 CPDCLREYFDPLDRRFHAQFIACTNCGPRLSLI 33
|
|
| PRK14426 |
PRK14426 |
acylphosphatase; Provisional |
15-94 |
1.68e-10 |
|
acylphosphatase; Provisional
Pssm-ID: 184675 Cd Length: 92 Bit Score: 58.11 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 15 VSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKANAPVGSEITNIETEDIK-EREFDGF 92
Cdd:PRK14426 10 VYGRVQGVGFRYHTQHEALKLGLTGYAKNLdDGSVEVVACGEEEQVEKLMEWLKEGGPRSARVDRVLTEPHSpRGELTGF 89
|
..
gi 316939615 93 RI 94
Cdd:PRK14426 90 SI 91
|
|
| TsaC |
COG0009 |
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ... |
206-339 |
1.73e-10 |
|
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439780 [Multi-domain] Cd Length: 204 Bit Score: 61.26 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 206 KDAFHAAANIIESGGIIA-----VKGIGgyhfaCSPFLEDTVLRLRELKGREA-KPFAIMFESVDSIRKYC-VVSEKEEE 278
Cdd:COG0009 9 PRLIEQAAEALRAGGVVAyptdtVYGLG-----CDALNKEAVERIFAIKGRPRdKPLIVLVADLSQLEEYAkEVPDAARR 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 316939615 279 LLKS----------KARPIVLLYL--KNNSMApsacqgsIYCgaflpytPLHML---LVKRCG-PLIMTSANISDKP 339
Cdd:COG0009 84 LAKAfwpgpltlilPATKEVPDLLtgGRDTVA-------VRV-------PDHPValaLLRALGpPLASTSANLSGEP 146
|
|
| PRK14445 |
PRK14445 |
acylphosphatase; Provisional |
12-95 |
1.96e-10 |
|
acylphosphatase; Provisional
Pssm-ID: 172921 Cd Length: 91 Bit Score: 57.93 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 12 RITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKAnAPVGSEITNIEtedIKEREFD 90
Cdd:PRK14445 7 HLIVSGLVQGVGFRMFIDRAASELNLSGWVRNLpDGTVEIEAQGSSGMIDELIKQAER-GPSRSSVTSIM---VEELEPD 82
|
....*....
gi 316939615 91 ----GFRII 95
Cdd:PRK14445 83 sslkGFSII 91
|
|
| PRK14448 |
PRK14448 |
acylphosphatase; Provisional |
9-94 |
2.39e-10 |
|
acylphosphatase; Provisional
Pssm-ID: 172924 Cd Length: 90 Bit Score: 57.46 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 9 ITKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNIG-GLVEIILQSSEEKYNEFlQDLKANAPVGSEITNIETED-IKE 86
Cdd:PRK14448 2 LKKQFIVYGHVQGVGFRYFTWQEATKIGIKGYVKNRPdGSVEVVAVGSDAQIAAF-RDWLQHGPPTAVVCNVIEQDyQGS 80
|
....*...
gi 316939615 87 REFDGFRI 94
Cdd:PRK14448 81 RQFTHFSV 88
|
|
| PRK14434 |
PRK14434 |
acylphosphatase; Provisional |
12-94 |
1.05e-07 |
|
acylphosphatase; Provisional
Pssm-ID: 184680 Cd Length: 92 Bit Score: 50.14 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 12 RITVSGIVQGVGFRPFVHNIAKKHG-IPGTV-RNIGGLVEIILQS-SEEKYNEFLQDLKANAPVGSEITNIETEDIKERE 88
Cdd:PRK14434 5 RMIVSGRVQGVGFRYSVYSLALEIGdIYGRVwNNDDGTVEILAQSdDSAKLAKFIQEIRKGPSKWAKVTYVDVTMANFED 84
|
....*.
gi 316939615 89 FDGFRI 94
Cdd:PRK14434 85 FSDFKI 90
|
|
| PRK14433 |
PRK14433 |
acylphosphatase; Provisional |
11-94 |
1.33e-07 |
|
acylphosphatase; Provisional
Pssm-ID: 184679 Cd Length: 87 Bit Score: 49.81 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 11 KRIT--VSGIVQGVGFRPFVHNIAKKHGIPGTVRNIG-GLVEIILQSSEEKYNEFLQDLKaNAPVGSEITNIETEDIKER 87
Cdd:PRK14433 1 MRLTalVSGRVQGVGYRAFVQKKARELGLSGYAENLSdGRVEVVAEGPKEALERLLHWLR-RGPRHARVEAVDVQWSEAT 79
|
....*..
gi 316939615 88 EFDGFRI 94
Cdd:PRK14433 80 GLKGFHV 86
|
|
| PRK14428 |
PRK14428 |
acylphosphatase; Provisional |
9-84 |
1.68e-07 |
|
acylphosphatase; Provisional
Pssm-ID: 172904 Cd Length: 97 Bit Score: 49.74 E-value: 1.68e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 316939615 9 ITKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLkANAPVGSEITNIETEDI 84
Cdd:PRK14428 8 VRKHIVVTGLVQGVGFRYFTVTQARRLGVQGWVRNCrDGSVELEAQGSSDAVQALVEQL-AIGPRWSEVSHVAVHDM 83
|
|
| PRK14450 |
PRK14450 |
acylphosphatase; Provisional |
12-82 |
2.93e-07 |
|
acylphosphatase; Provisional
Pssm-ID: 184683 Cd Length: 91 Bit Score: 49.07 E-value: 2.93e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 316939615 12 RITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI--GGLVEIILQSSEEKYNEFLqDLKANAPVGSEITNIETE 82
Cdd:PRK14450 5 KAIVKGKVQGVYFRDFTRTQATRLGLCGYAKNLanGNEVEVVAEGDKDSLLEFL-DLLRSGPPRAEVKEVETS 76
|
|
| PRK14432 |
PRK14432 |
acylphosphatase; Provisional |
15-94 |
4.00e-07 |
|
acylphosphatase; Provisional
Pssm-ID: 184678 Cd Length: 93 Bit Score: 48.75 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 15 VSGIVQGVGFRPFVHNIAKKHGIPGTVRNIG-GLVEIILQSSEEKYNEFLQDLKANAPVGSEITNIETEDIKER---EFD 90
Cdd:PRK14432 8 ISGKVQGVGFRFFTEQIANNMKLKGFVKNLNdGRVEIVAFFNTKEQMKKFEKLLKNGNKYSNIENIEKKVLDENypfQFN 87
|
....
gi 316939615 91 GFRI 94
Cdd:PRK14432 88 DFKI 91
|
|
| PRK14440 |
PRK14440 |
acylphosphatase; Provisional |
15-80 |
4.35e-07 |
|
acylphosphatase; Provisional
Pssm-ID: 172916 Cd Length: 90 Bit Score: 48.27 E-value: 4.35e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 316939615 15 VSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKANAPVgSEITNIE 80
Cdd:PRK14440 9 VYGLVQGVGFRKFVQIHAIRLGIKGYAKNLpDGSVEVVAEGYEEALSKLLERIKQGPPA-AEVEKVD 74
|
|
| PRK14443 |
PRK14443 |
acylphosphatase; Provisional |
10-79 |
5.04e-07 |
|
acylphosphatase; Provisional
Pssm-ID: 172919 Cd Length: 93 Bit Score: 48.13 E-value: 5.04e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 316939615 10 TKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKANAPVGSEITNI 79
Cdd:PRK14443 5 TAILRVTGFVQGVGFRYTTKHVAYKYDISGTVKNLdDGSVEIHAIAEEENLNKFIDAIKKGPSPGCRIEHV 75
|
|
| PRK14427 |
PRK14427 |
acylphosphatase; Provisional |
2-95 |
2.07e-06 |
|
acylphosphatase; Provisional
Pssm-ID: 172903 Cd Length: 94 Bit Score: 46.41 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 2 DKGKSKSITKRITvsGIVQGVGFRPFVHNIAKKHGIPGTVRNIG-GLVEIILQSSEEKYNEFLQDLKAN-APVGSEITNI 79
Cdd:PRK14427 1 PAAHQVRLSARVF--GVVQGVGFRYWTMRKAEELGLTGTVRNLDdGSVALVAEGTGEQVEKLLDWLNSDrAPGRVERVDH 78
|
90
....*....|....*.
gi 316939615 80 ETEDIkEREFDGFRII 95
Cdd:PRK14427 79 TVSEA-TGEFREFRAR 93
|
|
| PRK14436 |
PRK14436 |
acylphosphatase; Provisional |
13-95 |
2.09e-06 |
|
acylphosphatase; Provisional
Pssm-ID: 172912 Cd Length: 91 Bit Score: 46.50 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 13 ITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYnEFLQDLKANAPVGSEITNIETEDIKEREFDG 91
Cdd:PRK14436 8 LRIYGRVQGVGFRWSMQREARKLGVNGWVRNLpDGSVEAVLEGDEERV-EALIGWAHQGPPLARVTRVEVKWEEPKGEKG 86
|
....
gi 316939615 92 FRII 95
Cdd:PRK14436 87 FRVV 90
|
|
| PRK14442 |
PRK14442 |
acylphosphatase; Provisional |
9-94 |
2.38e-06 |
|
acylphosphatase; Provisional
Pssm-ID: 172918 Cd Length: 91 Bit Score: 46.41 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 9 ITKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNIG-GLVEIILQSSEEKYNEfLQDLKANAPVGSEITNIETEDIKER 87
Cdd:PRK14442 4 ICLHAYVGGRVQGVGFRQATREEADRLELDGWVRNLDdGRVEVVWEGEEDRAKA-LERWLGRGPRHAEVSAVEVEQMPLQ 82
|
....*..
gi 316939615 88 EFDGFRI 94
Cdd:PRK14442 83 GIAGFVV 89
|
|
| PRK14451 |
PRK14451 |
acylphosphatase; Provisional |
9-94 |
3.44e-06 |
|
acylphosphatase; Provisional
Pssm-ID: 237715 Cd Length: 89 Bit Score: 45.69 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 9 ITKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNIG-GLVEIILQSSEEKYNEFLQDLKaNAPVGSEITNIETEDIKER 87
Cdd:PRK14451 3 LCMRCYISGRVQGVWFRASAKKLAEQLMISGWARNLAdGRVEVFACGKEDKLEEFYTWLQ-KGPLNARVDVCTRENLPWQ 81
|
....*..
gi 316939615 88 EFDGFRI 94
Cdd:PRK14451 82 DYISFDV 88
|
|
| PRK14425 |
PRK14425 |
acylphosphatase; Provisional |
12-94 |
4.40e-06 |
|
acylphosphatase; Provisional
Pssm-ID: 172901 Cd Length: 94 Bit Score: 45.62 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 12 RITVSGIVQGVGFRPFVHNIAKKHGIPGTVRN-IGGLVEIILQSSEEKYNEFLQDLKaNAPVGSEITNIETEDIKEREF- 89
Cdd:PRK14425 9 RVRITGRVQGVGFRDWTRDEAERLGLTGWVRNeSDGSVTALIAGPDSAISAMIERFR-RGPPGASVSGVETEAAQLEEAp 87
|
....*
gi 316939615 90 DGFRI 94
Cdd:PRK14425 88 TDFRI 92
|
|
| PRK14421 |
PRK14421 |
acylphosphatase; Provisional |
9-83 |
1.18e-05 |
|
acylphosphatase; Provisional
Pssm-ID: 237711 [Multi-domain] Cd Length: 99 Bit Score: 44.41 E-value: 1.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 316939615 9 ITKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRN-IGGLVEIILQSSEEKYNEFLQDLKaNAPVGSEITNIETED 83
Cdd:PRK14421 4 IVRQVTIRGRVQGVGYRAWVARTAEALGLEGWVRNrRDGSVEALFAGPADAVAEMIARCR-RGPSAARVDAVEDEP 78
|
|
| PRK14449 |
PRK14449 |
acylphosphatase; Provisional |
10-94 |
3.53e-05 |
|
acylphosphatase; Provisional
Pssm-ID: 184682 Cd Length: 90 Bit Score: 42.89 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 10 TKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKaNAPVGSEITNIEtEDIKERE 88
Cdd:PRK14449 4 TVHLRITGHVQGVGLRYSVYQKAVSLGITGYAENLyDGSVEVVAEGDEENIKELINFIK-TGLRWARVDNVE-ERWSDYK 81
|
....*...
gi 316939615 89 --FDGFRI 94
Cdd:PRK14449 82 geYRDFRI 89
|
|
| PRK14423 |
PRK14423 |
acylphosphatase; Provisional |
15-94 |
4.85e-05 |
|
acylphosphatase; Provisional
Pssm-ID: 237713 Cd Length: 92 Bit Score: 42.74 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 15 VSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKANAPvGSEITNIETEDIKEREFDGFR 93
Cdd:PRK14423 11 VSGRVQGVYYRASTRDTARELGVDGWVRNLdDGRVEAVFEGPRDAVEAMVEWCHEGSP-AAVVEDVEVEYEEPEGLDGFE 89
|
.
gi 316939615 94 I 94
Cdd:PRK14423 90 I 90
|
|
| PRK14429 |
PRK14429 |
acylphosphatase; Provisional |
11-90 |
5.89e-05 |
|
acylphosphatase; Provisional
Pssm-ID: 184676 Cd Length: 90 Bit Score: 42.40 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 11 KR--ITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLqdlkANAPVGSEITNIETEDIKER 87
Cdd:PRK14429 2 KRvlIKLTGKVQGVGCRRATLTKARALGVTGYVTNCeDGSVEILAQGSDPAVDNLI----AWCEVGVPCTEVLRVTVEED 77
|
...
gi 316939615 88 EFD 90
Cdd:PRK14429 78 EAD 80
|
|
| PRK14430 |
PRK14430 |
acylphosphatase; Provisional |
10-92 |
1.94e-04 |
|
acylphosphatase; Provisional
Pssm-ID: 172906 Cd Length: 92 Bit Score: 41.06 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 10 TKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRN-IGGLVEIILQSSEEKYnEFLQDLKANAPVGSEITNIETEDiKERE 88
Cdd:PRK14430 5 TWRLVAHGRVQGVGYRAACADAADDLGLGGWVRNrADGTVEVMASGTVRQL-EALRAWMEAGPPAAQVTKVEVGP-GAGE 82
|
....
gi 316939615 89 FDGF 92
Cdd:PRK14430 83 FAGF 86
|
|
| PRK14447 |
PRK14447 |
acylphosphatase; Provisional |
13-95 |
2.45e-04 |
|
acylphosphatase; Provisional
Pssm-ID: 172923 Cd Length: 95 Bit Score: 40.69 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 13 ITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI--GGLVEIILQSSEEKYNEFLQDLKANAPvGSEITNIET--EDIKErE 88
Cdd:PRK14447 8 LFIRGKVQGVFFRQSMKEVANRNGVRGWVRNRsdGRTVEAVLEGPRDAVLKVIEWARVGPP-GARVEDVEVkwEEYKG-E 85
|
....*..
gi 316939615 89 FDGFRII 95
Cdd:PRK14447 86 FQDFRIL 92
|
|
| PRK14424 |
PRK14424 |
acylphosphatase; Provisional |
10-92 |
6.60e-04 |
|
acylphosphatase; Provisional
Pssm-ID: 184674 Cd Length: 94 Bit Score: 39.44 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 10 TKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKaNAPVGSEITNIETED-IKER 87
Cdd:PRK14424 8 TYYVRVRGVVQGVGFRHATVREAHALGLRGWVANLeDGTVEAMIQGPAAQIDRMLAWLR-HGPPAARVTEVTFEErRTEK 86
|
....*
gi 316939615 88 EFDGF 92
Cdd:PRK14424 87 RFERF 91
|
|
| PRK14439 |
PRK14439 |
acylphosphatase; Provisional |
15-94 |
9.17e-04 |
|
acylphosphatase; Provisional
Pssm-ID: 237714 Cd Length: 163 Bit Score: 40.84 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 15 VSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYNEFLQDLKANAPVGSEITNIETEDIKER-EFDGF 92
Cdd:PRK14439 81 VYGRVQGVGFRYTTQYEAKKLGLTGYAKNLdDGSVEVVACGEEGQVEKLMQWLKSGGPRSARVERVLSEPHHPSgELTDF 160
|
..
gi 316939615 93 RI 94
Cdd:PRK14439 161 RI 162
|
|
| ASKHA_NBD_MJ1051-like_N |
cd24100 |
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ... |
681-745 |
9.27e-04 |
|
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and similar proteins; The family includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ1051 and protein MJ1058. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.
Pssm-ID: 466950 [Multi-domain] Cd Length: 238 Bit Score: 41.69 E-value: 9.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 316939615 681 AVADMILE--VCEIIR---AEQKINTVALSGGVFQNTLLMertLKILRDRHFNvyyNMSVPPN--DGSIGLG 745
Cdd:cd24100 165 AAVQRVLEevVVEWVKnalKKTGIKNLALAGGVFANVKLN---QRIAELPEVE---NLFVFPSmgDGGLALG 230
|
|
| ASKHA_NBD_TsaD_bac |
cd24133 |
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ... |
666-737 |
1.17e-03 |
|
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase TsaD and similar proteins; TsaD (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD, or tRNA threonylcarbamoyladenosine biosynthesis protein TsaD, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Pssm-ID: 466983 Cd Length: 328 Bit Score: 41.70 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 316939615 666 QNKDDtgsLALGFHYAVADMILEVCEIIRAEQKINTVALSGGVFQNTLLMERTLKILRDRHFNVYYnmsvPP 737
Cdd:cd24133 230 QNKAD---IAASFQEAVVDVLVEKTLRAAKETGIKRLVVAGGVAANSRLREKLEEAAEKRGLEVYI----PP 294
|
|
| PRK14422 |
PRK14422 |
acylphosphatase; Provisional |
12-94 |
1.33e-03 |
|
acylphosphatase; Provisional
Pssm-ID: 237712 Cd Length: 93 Bit Score: 38.57 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 12 RIT--VSGIVQGVGFRPFVHNIAKKHGIPGTVRNIG-GLVEIILQSSEEKYNEFLQDLKANAPVGSEITNIETEDIKERE 88
Cdd:PRK14422 7 RLTawVHGHVQGVGFRWWTRSRALELGLTGYAANLAdGRVQVVAEGPRAACEKLLQLLRGDDTPGRVDKVVEDWSEPRGQ 86
|
....*.
gi 316939615 89 FDGFRI 94
Cdd:PRK14422 87 ITGFVE 92
|
|
| PRK14438 |
PRK14438 |
acylphosphatase; Provisional |
9-94 |
2.07e-03 |
|
acylphosphatase; Provisional
Pssm-ID: 172914 Cd Length: 91 Bit Score: 37.90 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 9 ITKRITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSEEKYnEFLQDLKANAPVGSEITNIETEDIKER 87
Cdd:PRK14438 3 IRAMVTVKGLVQGVAFRHHTQQTAQRLNVSGWVKNLpNGSVQGCFEGEETDV-AALIDWCHHGPSRARVSGVIVEREEFR 81
|
....*...
gi 316939615 88 -EFDGFRI 94
Cdd:PRK14438 82 gEFDDFDI 89
|
|
| ASKHA_NBD_Kae1_TsaD |
cd24031 |
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ... |
673-739 |
2.17e-03 |
|
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine threonylcarbamoyltransferase; tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein, or tRNA threonylcarbamoyladenosine biosynthesis protein, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The family includes different orthologous of tRNA N6-adenosine threonylcarbamoyltransferase, such as bacterial kinase-associated endopeptidase 1 (Kae1) and TsaD (also known as YgjD) protein, mammalian O-sialoglycoprotein endopeptidase (OSGEP) and yeast protein Kae1, as well as mammalian OSGEP-like protein 1 (OSGEPL1) and yeast protein Qri7, which are the mitochondrial versions of the universal Kae1/TsaD (also known as YgjD) protein and essential for mitochondrial genome maintenance.
Pssm-ID: 466881 Cd Length: 304 Bit Score: 40.93 E-value: 2.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 316939615 673 SLALGFHYAVADMILEVCEIIRAEQKINTVALSGGVFQNTLLMERTLKILRDRHFNVYYnmsvPPND 739
Cdd:cd24031 223 DIAYSFQETVFDMLVEKTERALAHTNKKEVVLVGGVSANNRLREMLATMCEKRGGEFFY----PPPE 285
|
|
| ASKHA_NBD_NodU_CmcH-like_N |
cd24033 |
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ... |
674-745 |
2.36e-03 |
|
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH family includes NodU from Rhizobium, CmcH from Amycolatopsis lactamdurans, the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius, NovN from Streptomyces niveus and NolNO from Sinorhizobium fredii. NodU is a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. 3'-hydroxymethylcephem-O-carbamoyltransferase CmcH (EC 2.1.3.7), also called 3'-hydroxymethylcephem-O-CASE (CCT), is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity. nebramycin 5' synthase TobZ (EC 6.1.2.2), also called kanamycin A carbamoyltransferase, or tobramycin carbamoyltransferase, functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. Novobiocin biosynthesis protein NovN (EC 2.1.3.12), also called decarbamoylnovobiocin carbamoyltransferase, acts as a carbamoyltransferase that mediates 3'-carbamoylation of the noviosyl ring to produce novobiocin, the final step in the novobiocin biosynthesis pathway. Nodulation protein NolNO (EC 2.1.3.-), also called NolO or Y4hD, is involved in the O-carbamoylation of nod factors. Members in this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.
Pssm-ID: 466883 [Multi-domain] Cd Length: 268 Bit Score: 40.36 E-value: 2.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 316939615 674 LALGFHYAVADMILEVCEIIRAEQKINTVALSGGVFQNTLLmerTLKILRDRHFnvyYNMSVPP--NDGSIGLG 745
Cdd:cd24033 193 LAATVQKVFEEALLELIKKLLERTGSDNLCLSGGCALNCVA---NSKLAEEGLF---KNVFVPPapGDSGLSLG 260
|
|
| PRK14441 |
PRK14441 |
acylphosphatase; Provisional |
12-49 |
2.93e-03 |
|
acylphosphatase; Provisional
Pssm-ID: 172917 Cd Length: 93 Bit Score: 37.65 E-value: 2.93e-03
10 20 30
....*....|....*....|....*....|....*....
gi 316939615 12 RITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNIG-GLVE 49
Cdd:PRK14441 8 RIVVSGRVQGVAFRQSAADEARRLGVEGWVRNLPdGRVE 46
|
|
| PRK14444 |
PRK14444 |
acylphosphatase; Provisional |
15-56 |
4.26e-03 |
|
acylphosphatase; Provisional
Pssm-ID: 172920 Cd Length: 92 Bit Score: 37.17 E-value: 4.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 316939615 15 VSGIVQGVGFRPFVHNIAKKHGIPGTVRNI-GGLVEIILQSSE 56
Cdd:PRK14444 10 ISGRVQGVNFRAYTRDRAREAGVKGWVRNLsDGRVEAVFEGSR 52
|
|
| PRK14437 |
PRK14437 |
acylphosphatase; Provisional |
13-94 |
4.83e-03 |
|
acylphosphatase; Provisional
Pssm-ID: 172913 Cd Length: 109 Bit Score: 37.40 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316939615 13 ITVSGIVQGVGFRPFVHNIAKKHGIPGTVRNIG-GLVEIILqSSEEKYNEFLQDLKANAPVGSEITNIETEDIKEREFDG 91
Cdd:PRK14437 27 ATVSGKVQGVFFRESVRKKAEELQLTGWVKNLShGDVELVA-CGERDSIMILTEWLWEGPPQAAVSNVNWEEIVVEDYSD 105
|
...
gi 316939615 92 FRI 94
Cdd:PRK14437 106 FRV 108
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