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Conserved domains on  [gi|1852263780|ref|WP_173891959|]
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carbamoyltransferase HypF [Legionella micdadei]

Protein Classification

carbamoyltransferase HypF( domain architecture ID 11414624)

carbamoyltransferase HypF is involved in the biosynthesis of the CN ligand of the NiFe(CN)(2)CO centre of [NiFe]-hydrogenase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 3-743 0e+00

Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1023.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   3 ERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGVLIEVQG--LSVSSFLAQLLASLPPLAKIKDIETSHIALiD 80
Cdd:COG0068     2 KRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGeeEALEAFLEALRAEAPPLARIDSIEVEELPP-E 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780  81 HESSFQIIDSHKSGVSGSVISPDTSPCSDCLKELFDPDSRYYQYPFLNCTQCGPRFSITRELPYDRCQTSMSEFPLCLAC 160
Cdd:COG0068    81 GFDGFRILESEAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPDC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 161 KQDYSSPTNRRYHAQPTACKNCGPELSV-------------PIQAIAEALRAGKIIALKGVGGYQLLCDARNKSAIQRLR 227
Cdd:COG0068   161 AAEYEDPADRRFHAQPNACPVCGPQLWLldadgkplaegddAIAAAAELLRAGKIVAIKGLGGFHLACDATNEEAVARLR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 228 QKKYREAKPLALMVLNCISAEELVLISTEEKEVLVSPARPIVLLKKKQE-VLPKLVAPHLSCLGIMlpsspllyllFHAL 306
Cdd:COG0068   241 RRKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARPIVLLPKRPDsPLAPSVAPGLDTLGVMlpytplhhllLDEL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 307 AGFpeglgwlesihpwaLIATSANIAGNPLLIADEKANDELVAIADLIVSYNRQILTRVDDSVLRIINHSPHFVRRARGF 386
Cdd:COG0068   321 GRP--------------LVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVVRVIDGKPRFLRRARGY 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 387 SPISIQLPASIPSTLALGGHLKNTFCITRGNEAFVSQHIGSMTNKETIDFFHESLTHWMRFLDVKIERVACDLHPDFYTT 466
Cdd:COG0068   387 APLPIPLPFELPPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLST 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 467 HFASQY---NLPVIAVQHHHAHLASVVAEHQIMEPALGLALDGYGYGWDGKAWGGElFLLKKGAQAQRLAHFYPIPQPGG 543
Cdd:COG0068   467 RLAEELaerGLPLIEVQHHHAHIAAVMAEHGLDGPVLGIALDGTGYGDDGTIWGGE-FLLGDYAGFERVGHLRPFPLPGG 545

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 544 ERAVHETWRMAAAVLHCLNRDE---EIIQRFAEQsQVFGVARLLKTNPSLPTTSSCGRLFDAASALLNVNTLSHYEGQAP 620
Cdd:COG0068   546 DKAAREPWRMALALLYEAGGEEllePLLKRFSEK-ELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDEISYEGQAA 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 621 MQLESLVTSPEVfASGWTFTQE------QFNFLPTMLQLLQMK-----PKEGANLFHGTLIAGLADWILFYAKKTSINLV 689
Cdd:COG0068   625 MELEALADRAEE-AEPYPFPLReidgllVLDWAPLLRALLEDLqagvpPAEIAARFHNTLAEAIAELALRLAERTGIDTV 703

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1852263780 690 LLSGGCFLNQVLTEGLTKQLENHGLKVYLPQQLPANDGGISLGQVWIGGNYPEA 743
Cdd:COG0068   704 ALSGGVFQNRLLLELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAARLEG 757
 
Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 3-743 0e+00

Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1023.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   3 ERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGVLIEVQG--LSVSSFLAQLLASLPPLAKIKDIETSHIALiD 80
Cdd:COG0068     2 KRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGeeEALEAFLEALRAEAPPLARIDSIEVEELPP-E 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780  81 HESSFQIIDSHKSGVSGSVISPDTSPCSDCLKELFDPDSRYYQYPFLNCTQCGPRFSITRELPYDRCQTSMSEFPLCLAC 160
Cdd:COG0068    81 GFDGFRILESEAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPDC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 161 KQDYSSPTNRRYHAQPTACKNCGPELSV-------------PIQAIAEALRAGKIIALKGVGGYQLLCDARNKSAIQRLR 227
Cdd:COG0068   161 AAEYEDPADRRFHAQPNACPVCGPQLWLldadgkplaegddAIAAAAELLRAGKIVAIKGLGGFHLACDATNEEAVARLR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 228 QKKYREAKPLALMVLNCISAEELVLISTEEKEVLVSPARPIVLLKKKQE-VLPKLVAPHLSCLGIMlpsspllyllFHAL 306
Cdd:COG0068   241 RRKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARPIVLLPKRPDsPLAPSVAPGLDTLGVMlpytplhhllLDEL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 307 AGFpeglgwlesihpwaLIATSANIAGNPLLIADEKANDELVAIADLIVSYNRQILTRVDDSVLRIINHSPHFVRRARGF 386
Cdd:COG0068   321 GRP--------------LVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVVRVIDGKPRFLRRARGY 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 387 SPISIQLPASIPSTLALGGHLKNTFCITRGNEAFVSQHIGSMTNKETIDFFHESLTHWMRFLDVKIERVACDLHPDFYTT 466
Cdd:COG0068   387 APLPIPLPFELPPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLST 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 467 HFASQY---NLPVIAVQHHHAHLASVVAEHQIMEPALGLALDGYGYGWDGKAWGGElFLLKKGAQAQRLAHFYPIPQPGG 543
Cdd:COG0068   467 RLAEELaerGLPLIEVQHHHAHIAAVMAEHGLDGPVLGIALDGTGYGDDGTIWGGE-FLLGDYAGFERVGHLRPFPLPGG 545

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 544 ERAVHETWRMAAAVLHCLNRDE---EIIQRFAEQsQVFGVARLLKTNPSLPTTSSCGRLFDAASALLNVNTLSHYEGQAP 620
Cdd:COG0068   546 DKAAREPWRMALALLYEAGGEEllePLLKRFSEK-ELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDEISYEGQAA 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 621 MQLESLVTSPEVfASGWTFTQE------QFNFLPTMLQLLQMK-----PKEGANLFHGTLIAGLADWILFYAKKTSINLV 689
Cdd:COG0068   625 MELEALADRAEE-AEPYPFPLReidgllVLDWAPLLRALLEDLqagvpPAEIAARFHNTLAEAIAELALRLAERTGIDTV 703

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1852263780 690 LLSGGCFLNQVLTEGLTKQLENHGLKVYLPQQLPANDGGISLGQVWIGGNYPEA 743
Cdd:COG0068   704 ALSGGVFQNRLLLELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAARLEG 757
hypF TIGR00143
[NiFe] hydrogenase maturation protein HypF; A previously described regulatory effect of HypF ...
 41-733 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: 631.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780  41 GVLIEVQGLSVSSFLAQLLASLPPLAKIKDIETSHIALIDHESSFQIIDSHKSGVSG-SVISPDTSPCSDCLKELFDPDS 119
Cdd:TIGR00143   4 GVEIVLEADKEESFLNRLKKGLPPLARIEKIIIEPFDGAEHFTTFRIRESKNGGLSLlSIIPADVATCSDCLEEMLDKND 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 120 RYYQYPFLNCTQCGPRFSITRELPYDRCQTSMSEFPLCLACKQDYSSPTNRRYHAQPTACKNCGPELSV----------- 188
Cdd:TIGR00143  84 RRYLYPFISCTHCGPRFTIIEALPYDRENTSMADFPLCPDCAKEYKDPLDRRFHAQPIACPRCGPQLNFvsrgghaeqdd 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 189 PIQAIAEALRAGKIIALKGVGGYQLLCDARNKSAIQRLRQKKYREAKPLALMVLNCISAEELVLISTEEKEVLVSPARPI 268
Cdd:TIGR00143 164 ALLEAAKLLKKGKIIAIKGIGGFHLACDARNDEVVERLRLRKNRPLKPFAVMSPDLESAEQHAELNNLECELLTSPAAPI 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 269 VLLKKKQEVLP-KLVAPHLSCLGIMlpsspLLYLLFHALagfpegLGWLESIhpwALIATSANIAGNPLLIADEKANDEL 347
Cdd:TIGR00143 244 VLLRKKPDIKLaPNIAPNLPTIGVM-----LPYTPLHHL------LLQLLAF---PLVMTSANLPGLPMAIDNAEILDKL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 348 VAIADLIVSYNRQILTRVDDSVLRIINHSPHFVRRARGFSPISIQLP--ASIPSTLALGGHLKNTFCITRGNEAFVSQHI 425
Cdd:TIGR00143 310 QGIADGFLVHNRRIVNRVDDSVVQHVAGEILFLRRSRGFAPQPLTLPpnGNPKKILALGAELKNTFSLLKGGQAYLSQHI 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 426 GSMTNKETIDFFHESLTHWMRFLDVKIERVACDLHPDFYTTHFASQYNLPVIAVQHHHAHLASVVAEHQIME-PALGLAL 504
Cdd:TIGR00143 390 GDLSVYETYKFFKEALNFFLRIYDFEPQDIVCDLHPQYNTTQYAEELSLPVLRVQHHHAHALAVMADAGVLEeAVIGITW 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 505 DGYGYGWDGKAWGGELFLLKKGaQAQRLAHFYPIPQPGGERAVHETWRMAAAVL--HCLNRDEEIIQRFAEQSQVFGV-A 581
Cdd:TIGR00143 470 DGVGYGEDGKIWGGECLLIDLG-RIERLGRLEEFWLLGGDLATKYPLRILLSILlkHDLNDFLKRYQKYFKQEKELSVlQ 548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 582 RLLKTNPSLPTTSSCGRLFDAASALLNV-NTLShYEGQAPMQLESLV-TSPEVFASGWTFTQEQFN----FLPTMLQLLQ 655
Cdd:TIGR00143 549 QALEKKINAPLTTSTGRLFDAVAAALGLcGERT-YEGEAAIALEALAlRSDGIANYPFEIKNKVLDlkefYQRFLEDLLV 627

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852263780 656 MKPKEGANL-FHGTLIAGLADWILFYAKKTSINLVLLSGGCFLNQVLTEGLTKQLENHGLKVYLPQQLPANDGGISLGQ 733
Cdd:TIGR00143 628 GEDRSKIAHiAHKFVASGLVEIATAIAVPFGIHKIVISGGVFYNRLLLERLAKYLKGLGFQFLFHRHLPPGDGGISLGQ 706
HypF_C pfam17788
HypF Kae1-like domain; This domain is found in the HypF protein. In the structure it is one of ...
 398-492 2.60e-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: 154.17  E-value: 2.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 398 PSTLALGGHLKNTFCITRGNEAFVSQHIGSMTNKETIDFFHESLTHWMRFLDVKIERVACDLHPDFYTTHFASQY-NLPV 476
Cdd:pfam17788   4 PPVLALGAELKNTFALAKGGQAFLSQHIGDLDNLETLEAFEETLEHLLRLYGIKPEVIACDLHPDYLSTRLAEELnGLPL 83

                          90
                  ....*....|....*.
gi 1852263780 477 IAVQHHHAHLASVVAE 492
Cdd:pfam17788  84 IEVQHHHAHIAAVMAE 99
PRK14420 PRK14420
acylphosphatase; Provisional
 4-88 1.28e-11

acylphosphatase; Provisional


Pssm-ID: 237710  Cd Length: 91  Bit Score: 61.36  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   4 RLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQGL--SVSSFLAQLLASlPPLAKIKDIETSHIALID 80
Cdd:PRK14420    3 QYHIIVDGRVQGVGFRYFVQMEADKRKLTGWVKNRDDGtVEIEAEGPeeALQLFLDAIEKG-SPFSKVTDVHIEERDVLS 81


                  ....*...
gi 1852263780  81 HESSFQII 88
Cdd:PRK14420   82 GEKQFRIM 89
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 675-735 4.53e-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: 39.59  E-value: 4.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852263780 675 DWILFYAKKT-SINLVLlSGGCFLNQVLTEGLTKqlENHGLKVYLPqqlPA-NDGGISLGQVW 735
Cdd:cd24033   207 ELIKKLLERTgSDNLCL-SGGCALNCVANSKLAE--EGLFKNVFVP---PApGDSGLSLGAAL 263
 
Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 3-743 0e+00

Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1023.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   3 ERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGVLIEVQG--LSVSSFLAQLLASLPPLAKIKDIETSHIALiD 80
Cdd:COG0068     2 KRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGeeEALEAFLEALRAEAPPLARIDSIEVEELPP-E 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780  81 HESSFQIIDSHKSGVSGSVISPDTSPCSDCLKELFDPDSRYYQYPFLNCTQCGPRFSITRELPYDRCQTSMSEFPLCLAC 160
Cdd:COG0068    81 GFDGFRILESEAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPDC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 161 KQDYSSPTNRRYHAQPTACKNCGPELSV-------------PIQAIAEALRAGKIIALKGVGGYQLLCDARNKSAIQRLR 227
Cdd:COG0068   161 AAEYEDPADRRFHAQPNACPVCGPQLWLldadgkplaegddAIAAAAELLRAGKIVAIKGLGGFHLACDATNEEAVARLR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 228 QKKYREAKPLALMVLNCISAEELVLISTEEKEVLVSPARPIVLLKKKQE-VLPKLVAPHLSCLGIMlpsspllyllFHAL 306
Cdd:COG0068   241 RRKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARPIVLLPKRPDsPLAPSVAPGLDTLGVMlpytplhhllLDEL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 307 AGFpeglgwlesihpwaLIATSANIAGNPLLIADEKANDELVAIADLIVSYNRQILTRVDDSVLRIINHSPHFVRRARGF 386
Cdd:COG0068   321 GRP--------------LVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVVRVIDGKPRFLRRARGY 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 387 SPISIQLPASIPSTLALGGHLKNTFCITRGNEAFVSQHIGSMTNKETIDFFHESLTHWMRFLDVKIERVACDLHPDFYTT 466
Cdd:COG0068   387 APLPIPLPFELPPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLST 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 467 HFASQY---NLPVIAVQHHHAHLASVVAEHQIMEPALGLALDGYGYGWDGKAWGGElFLLKKGAQAQRLAHFYPIPQPGG 543
Cdd:COG0068   467 RLAEELaerGLPLIEVQHHHAHIAAVMAEHGLDGPVLGIALDGTGYGDDGTIWGGE-FLLGDYAGFERVGHLRPFPLPGG 545

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 544 ERAVHETWRMAAAVLHCLNRDE---EIIQRFAEQsQVFGVARLLKTNPSLPTTSSCGRLFDAASALLNVNTLSHYEGQAP 620
Cdd:COG0068   546 DKAAREPWRMALALLYEAGGEEllePLLKRFSEK-ELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDEISYEGQAA 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 621 MQLESLVTSPEVfASGWTFTQE------QFNFLPTMLQLLQMK-----PKEGANLFHGTLIAGLADWILFYAKKTSINLV 689
Cdd:COG0068   625 MELEALADRAEE-AEPYPFPLReidgllVLDWAPLLRALLEDLqagvpPAEIAARFHNTLAEAIAELALRLAERTGIDTV 703

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1852263780 690 LLSGGCFLNQVLTEGLTKQLENHGLKVYLPQQLPANDGGISLGQVWIGGNYPEA 743
Cdd:COG0068   704 ALSGGVFQNRLLLELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAARLEG 757
hypF TIGR00143
[NiFe] hydrogenase maturation protein HypF; A previously described regulatory effect of HypF ...
 41-733 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: 631.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780  41 GVLIEVQGLSVSSFLAQLLASLPPLAKIKDIETSHIALIDHESSFQIIDSHKSGVSG-SVISPDTSPCSDCLKELFDPDS 119
Cdd:TIGR00143   4 GVEIVLEADKEESFLNRLKKGLPPLARIEKIIIEPFDGAEHFTTFRIRESKNGGLSLlSIIPADVATCSDCLEEMLDKND 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 120 RYYQYPFLNCTQCGPRFSITRELPYDRCQTSMSEFPLCLACKQDYSSPTNRRYHAQPTACKNCGPELSV----------- 188
Cdd:TIGR00143  84 RRYLYPFISCTHCGPRFTIIEALPYDRENTSMADFPLCPDCAKEYKDPLDRRFHAQPIACPRCGPQLNFvsrgghaeqdd 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 189 PIQAIAEALRAGKIIALKGVGGYQLLCDARNKSAIQRLRQKKYREAKPLALMVLNCISAEELVLISTEEKEVLVSPARPI 268
Cdd:TIGR00143 164 ALLEAAKLLKKGKIIAIKGIGGFHLACDARNDEVVERLRLRKNRPLKPFAVMSPDLESAEQHAELNNLECELLTSPAAPI 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 269 VLLKKKQEVLP-KLVAPHLSCLGIMlpsspLLYLLFHALagfpegLGWLESIhpwALIATSANIAGNPLLIADEKANDEL 347
Cdd:TIGR00143 244 VLLRKKPDIKLaPNIAPNLPTIGVM-----LPYTPLHHL------LLQLLAF---PLVMTSANLPGLPMAIDNAEILDKL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 348 VAIADLIVSYNRQILTRVDDSVLRIINHSPHFVRRARGFSPISIQLP--ASIPSTLALGGHLKNTFCITRGNEAFVSQHI 425
Cdd:TIGR00143 310 QGIADGFLVHNRRIVNRVDDSVVQHVAGEILFLRRSRGFAPQPLTLPpnGNPKKILALGAELKNTFSLLKGGQAYLSQHI 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 426 GSMTNKETIDFFHESLTHWMRFLDVKIERVACDLHPDFYTTHFASQYNLPVIAVQHHHAHLASVVAEHQIME-PALGLAL 504
Cdd:TIGR00143 390 GDLSVYETYKFFKEALNFFLRIYDFEPQDIVCDLHPQYNTTQYAEELSLPVLRVQHHHAHALAVMADAGVLEeAVIGITW 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 505 DGYGYGWDGKAWGGELFLLKKGaQAQRLAHFYPIPQPGGERAVHETWRMAAAVL--HCLNRDEEIIQRFAEQSQVFGV-A 581
Cdd:TIGR00143 470 DGVGYGEDGKIWGGECLLIDLG-RIERLGRLEEFWLLGGDLATKYPLRILLSILlkHDLNDFLKRYQKYFKQEKELSVlQ 548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 582 RLLKTNPSLPTTSSCGRLFDAASALLNV-NTLShYEGQAPMQLESLV-TSPEVFASGWTFTQEQFN----FLPTMLQLLQ 655
Cdd:TIGR00143 549 QALEKKINAPLTTSTGRLFDAVAAALGLcGERT-YEGEAAIALEALAlRSDGIANYPFEIKNKVLDlkefYQRFLEDLLV 627

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852263780 656 MKPKEGANL-FHGTLIAGLADWILFYAKKTSINLVLLSGGCFLNQVLTEGLTKQLENHGLKVYLPQQLPANDGGISLGQ 733
Cdd:TIGR00143 628 GEDRSKIAHiAHKFVASGLVEIATAIAVPFGIHKIVISGGVFYNRLLLERLAKYLKGLGFQFLFHRHLPPGDGGISLGQ 706
HypF_C pfam17788
HypF Kae1-like domain; This domain is found in the HypF protein. In the structure it is one of ...
 398-492 2.60e-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: 154.17  E-value: 2.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 398 PSTLALGGHLKNTFCITRGNEAFVSQHIGSMTNKETIDFFHESLTHWMRFLDVKIERVACDLHPDFYTTHFASQY-NLPV 476
Cdd:pfam17788   4 PPVLALGAELKNTFALAKGGQAFLSQHIGDLDNLETLEAFEETLEHLLRLYGIKPEVIACDLHPDYLSTRLAEELnGLPL 83

                          90
                  ....*....|....*.
gi 1852263780 477 IAVQHHHAHLASVVAE 492
Cdd:pfam17788  84 IEVQHHHAHIAAVMAE 99
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
 195-381 1.63e-34

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: 129.55  E-value: 1.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 195 EALRAGKIIALKGVGGYQLLCDARNKSAIQRLRQKKYREA-KPLALMVLNCISAEELVliSTEEKEVLVSPAR----PIV 269
Cdd:pfam01300   1 EALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRdKPLAVMVADLEDLKEYA--EEVEEAALRLAERfwpgPLT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 270 L-LKKKQEVLPKLVAPHLSCLGIMLPSSPLLYLLFHALaGFPeglgwlesihpwaLIATSANIAGNPLLIADEKANDELV 348
Cdd:pfam01300  79 LvLKASKKPLPKLLTPGLGTVGVRLPDHPLALLLLEAL-GEP-------------LVATSANLSGEPSPTDAEEILEELG 144

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1852263780 349 AIADLIVSYNRqILTRVDDSVLRIINHSPHFVR 381
Cdd:pfam01300 145 GRVDLILDGGR-IAGGVPSTVVDLTGGPPRILR 176
Acylphosphatase pfam00708
Acylphosphatase;
5-87 1.10e-23

Acylphosphatase;


Pssm-ID: 425830  Cd Length: 85  Bit Score: 95.35  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   5 LQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQG--LSVSSFLAQLLASlPPLAKIKDIETSHIALIDH 81
Cdd:pfam00708   1 KKVLVTGRVQGVGFRPFVYRLAKELGLKGWVRNLPDGsVEIVVQGpeEDVDKFLEWLKSG-PPPARVDKVEVTEIDEPGD 79


                  ....*.
gi 1852263780  82 ESSFQI 87
Cdd:pfam00708  80 FSGFEI 85
AcyP COG1254
Acylphosphatase [Energy production and conversion];
3-88 6.50e-21

Acylphosphatase [Energy production and conversion];


Pssm-ID: 440866  Cd Length: 89  Bit Score: 87.52  E-value: 6.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   3 ERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQG--LSVSSFLAqLLASLPPLAKIKDIETSHIALI 79
Cdd:COG1254     2 KRVRIIVSGRVQGVGFRAFTRRQARRLGLTGWVRNLPDGsVEVVAEGeeEAVEAFLE-WLRKGPPAARVEDVEVEEEEPT 80


                  ....*....
gi 1852263780  80 DHESSFQII 88
Cdd:COG1254    81 GEFEGFEIR 89
zf-HYPF pfam07503
HypF finger; The HypF family of proteins are involved in the maturation and regulation of ...
 107-139 3.53e-15

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: 69.69  E-value: 3.53e-15
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1852263780 107 CSDCLKELFDPDSRYYQYPFLNCTQCGPRFSIT 139
Cdd:pfam07503   1 CPDCLREYFDPLDRRFHAQFIACTNCGPRLSLI 33
zf-HYPF pfam07503
HypF finger; The HypF family of proteins are involved in the maturation and regulation of ...
 157-188 2.16e-13

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: 64.29  E-value: 2.16e-13
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1852263780 157 CLACKQDYSSPTNRRYHAQPTACKNCGPELSV 188
Cdd:pfam07503   1 CPDCLREYFDPLDRRFHAQFIACTNCGPRLSL 32
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
 190-389 2.71e-12

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: 66.20  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 190 IQAIAEALRAGKIIALKGVGGYQLLCDARNKSAIQRLRQKKYREA-KPLALMVLNCISAEELVLISTEEKEVL--VSPAR 266
Cdd:TIGR00057  11 IEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPSnKPLTVLVSDLSEIEKYAYVPDDAKRLMkkFWPGP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 267 PIVLLKKKqEVLPKLVAPHLSCLGIMLPSSPLLYLLFHALaGFPeglgwlesihpwaLIATSANIAGNPLLIADEKANDE 346
Cdd:TIGR00057  91 LTLVLKKT-PEIPRRVSGKRKTIGIRVPDNPIALELLEEL-GKP-------------IVATSANLSGKPSATDVEEAVDE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1852263780 347 LVAIADLIV---SYNRQILTrvddSVLRIINHSPHFVRRARGFSPI 389
Cdd:TIGR00057 156 LGKLVDLIIdagPCLGGEPS----TIIDLTDDTPKVLREGVGSEPI 197
PRK14420 PRK14420
acylphosphatase; Provisional
 4-88 1.28e-11

acylphosphatase; Provisional


Pssm-ID: 237710  Cd Length: 91  Bit Score: 61.36  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   4 RLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQGL--SVSSFLAQLLASlPPLAKIKDIETSHIALID 80
Cdd:PRK14420    3 QYHIIVDGRVQGVGFRYFVQMEADKRKLTGWVKNRDDGtVEIEAEGPeeALQLFLDAIEKG-SPFSKVTDVHIEERDVLS 81


                  ....*...
gi 1852263780  81 HESSFQII 88
Cdd:PRK14420   82 GEKQFRIM 89
PRK14450 PRK14450
acylphosphatase; Provisional
 5-87 9.28e-11

acylphosphatase; Provisional


Pssm-ID: 184683  Cd Length: 91  Bit Score: 58.70  E-value: 9.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   5 LQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGVLIEV----QGLSVSSFLaQLLASLPPLAKIKDIETSHIALID 80
Cdd:PRK14450    4 LKAIVKGKVQGVYFRDFTRTQATRLGLCGYAKNLANGNEVEVvaegDKDSLLEFL-DLLRSGPPRAEVKEVETSWETATA 82


                  ....*..
gi 1852263780  81 HESSFQI 87
Cdd:PRK14450   83 NYSDFRI 89
PRK14452 PRK14452
acylphosphatase; Provisional
 1-78 4.00e-10

acylphosphatase; Provisional


Pssm-ID: 237716  Cd Length: 107  Bit Score: 57.55  E-value: 4.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   1 MAERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGVlIEVQGLSVSSFLAQLLASL---PPLAKIKDIETSHIA 77
Cdd:PRK14452   18 FAERWRFLIEGRVQGVGFRASCCRRALDLGLSGWVRNLSDGS-VEVQAEGPPLALSELRAWCergPPGARVKRVDPSQLP 96


                  .
gi 1852263780  78 L 78
Cdd:PRK14452   97 V 97
PRK14445 PRK14445
acylphosphatase; Provisional
 1-48 2.58e-09

acylphosphatase; Provisional


Pssm-ID: 172921  Cd Length: 91  Bit Score: 54.85  E-value: 2.58e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1852263780   1 MAERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQG 48
Cdd:PRK14445    2 MEKRVHLIVSGLVQGVGFRMFIDRAASELNLSGWVRNLPDGtVEIEAQG 50
PRK14425 PRK14425
acylphosphatase; Provisional
 3-87 3.71e-09

acylphosphatase; Provisional


Pssm-ID: 172901  Cd Length: 94  Bit Score: 54.48  E-value: 3.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   3 ERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG---VLIEVQGLSVSSFLAQLLASlPPLAKIKDIETSHIALI 79
Cdd:PRK14425    6 EAVRVRITGRVQGVGFRDWTRDEAERLGLTGWVRNESDGsvtALIAGPDSAISAMIERFRRG-PPGASVSGVETEAAQLE 84


                  ....*...
gi 1852263780  80 DHESSFQI 87
Cdd:PRK14425   85 EAPTDFRI 92
PRK14433 PRK14433
acylphosphatase; Provisional
 4-73 7.35e-08

acylphosphatase; Provisional


Pssm-ID: 184679  Cd Length: 87  Bit Score: 50.58  E-value: 7.35e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852263780   4 RLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGvLIEVQGLSVSSFLAQLLASL---PPLAKIKDIET 73
Cdd:PRK14433    2 RLTALVSGRVQGVGYRAFVQKKARELGLSGYAENLSDG-RVEVVAEGPKEALERLLHWLrrgPRHARVEAVDV 73
PRK14441 PRK14441
acylphosphatase; Provisional
 1-87 2.78e-07

acylphosphatase; Provisional


Pssm-ID: 172917  Cd Length: 93  Bit Score: 49.21  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   1 MAERLQ--ILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQGLSVS-SFLAQLLASLPPLAKIKDIETSHI 76
Cdd:PRK14441    1 MADRVRarIVVSGRVQGVAFRQSAADEARRLGVEGWVRNLPDGrVEAEAEGERAAvGALVRWCHAGPPAARVDRVEVEWV 80

                          90
                  ....*....|.
gi 1852263780  77 ALIDHESSFQI 87
Cdd:PRK14441   81 EPAGDLGAFEI 91
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
 190-355 3.71e-07

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: 51.25  E-value: 3.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 190 IQAIAEALRAGKIIAL--KGVggYQLLCDARNKSAIQRLRQKKYREA-KPLALMVLNcIS-AEELVLISTEEKEVLVS-- 263
Cdd:COG0009    12 IEQAAEALRAGGVVAYptDTV--YGLGCDALNKEAVERIFAIKGRPRdKPLIVLVAD-LSqLEEYAKEVPDAARRLAKaf 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780 264 -PaRPI-VLLKKKQEVlPKLVAPHLSCLGImlpsspllyllfhalaGFPEglgwlesiHPWA----------LIATSANI 331
Cdd:COG0009    89 wP-GPLtLILPATKEV-PDLLTGGRDTVAV----------------RVPD--------HPVAlallralgppLASTSANL 142

                         170       180
                  ....*....|....*....|....*
gi 1852263780 332 AGNP-LLIADEkANDELVAIADLIV 355
Cdd:COG0009   143 SGEPpPTTAEE-VREQLGDRVDLIL 166
PRK14424 PRK14424
acylphosphatase; Provisional
 3-73 3.79e-07

acylphosphatase; Provisional


Pssm-ID: 184674  Cd Length: 94  Bit Score: 48.68  E-value: 3.79e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852263780   3 ERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQGLS--VSSFLAQLLASlPPLAKIKDIET 73
Cdd:PRK14424    7 ETYYVRVRGVVQGVGFRHATVREAHALGLRGWVANLEDGtVEAMIQGPAaqIDRMLAWLRHG-PPAARVTEVTF 79
PRK14435 PRK14435
acylphosphatase; Provisional
 5-87 6.28e-07

acylphosphatase; Provisional


Pssm-ID: 184681  Cd Length: 90  Bit Score: 47.98  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   5 LQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQG--LSVSSFLAQlLASLPPLAKIKDIETSHIALIDH 81
Cdd:PRK14435    4 LKIRVEGIVQGVGFRYFTRRVAKSLGVKGYVMNMDDGsVFIHAEGdeNALRRFLNE-VAKGPPAAVVTNVSVEETTPEGY 82


                  ....*.
gi 1852263780  82 EsSFQI 87
Cdd:PRK14435   83 E-DFTI 87
PRK14421 PRK14421
acylphosphatase; Provisional
 6-37 7.27e-07

acylphosphatase; Provisional


Pssm-ID: 237711 [Multi-domain]  Cd Length: 99  Bit Score: 47.88  E-value: 7.27e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1852263780   6 QILIKGQVQGVGFRPHVYRVALRLNLTGWVQN 37
Cdd:PRK14421    7 QVTIRGRVQGVGYRAWVARTAEALGLEGWVRN 38
PRK14438 PRK14438
acylphosphatase; Provisional
 1-48 1.14e-06

acylphosphatase; Provisional


Pssm-ID: 172914  Cd Length: 91  Bit Score: 47.14  E-value: 1.14e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1852263780   1 MAERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGvliEVQG 48
Cdd:PRK14438    1 MKIRAMVTVKGLVQGVAFRHHTQQTAQRLNVSGWVKNLPNG---SVQG 45
PRK14431 PRK14431
acylphosphatase; Provisional
 3-88 2.13e-06

acylphosphatase; Provisional


Pssm-ID: 184677  Cd Length: 89  Bit Score: 46.33  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   3 ERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGVLIEVQG--LSVSSFLAQLLASLPPLAKIKDIETSHIALID 80
Cdd:PRK14431    2 RHIHLQVFGRVQGVGFRYFTQRIAMNYNIVGTVQNVDDYVEIYAQGddADLERFIQGVIEGASPASNVTSYQLEELELNQ 81


                  ....*...
gi 1852263780  81 HESSFQII 88
Cdd:PRK14431   82 KLSDFRSI 89
PRK14426 PRK14426
acylphosphatase; Provisional
 9-37 5.77e-06

acylphosphatase; Provisional


Pssm-ID: 184675  Cd Length: 92  Bit Score: 45.40  E-value: 5.77e-06
                          10        20
                  ....*....|....*....|....*....
gi 1852263780   9 IKGQVQGVGFRPHVYRVALRLNLTGWVQN 37
Cdd:PRK14426   10 VYGRVQGVGFRYHTQHEALKLGLTGYAKN 38
PRK14440 PRK14440
acylphosphatase; Provisional
 1-91 7.27e-06

acylphosphatase; Provisional


Pssm-ID: 172916  Cd Length: 90  Bit Score: 44.80  E-value: 7.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   1 MAERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGVlIEVQGLSVSSFLAQLLASL---PPLAKIKDIETShia 77
Cdd:PRK14440    1 MLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGS-VEVVAEGYEEALSKLLERIkqgPPAAEVEKVDFS--- 76

                          90
                  ....*....|....
gi 1852263780  78 LIDHESSFQIIDSH 91
Cdd:PRK14440   77 FSEYKGEFEDFETY 90
PRK14449 PRK14449
acylphosphatase; Provisional
 1-37 1.60e-05

acylphosphatase; Provisional


Pssm-ID: 184682  Cd Length: 90  Bit Score: 44.05  E-value: 1.60e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1852263780   1 MAERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQN 37
Cdd:PRK14449    1 MKKTVHLRITGHVQGVGLRYSVYQKAVSLGITGYAEN 37
PRK14447 PRK14447
acylphosphatase; Provisional
 4-72 2.21e-05

acylphosphatase; Provisional


Pssm-ID: 172923  Cd Length: 95  Bit Score: 43.77  E-value: 2.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852263780   4 RLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGVLIEVQGLSVSSFLAQLL--ASL-PPLAKIKDIE 72
Cdd:PRK14447    5 RAHLFIRGKVQGVFFRQSMKEVANRNGVRGWVRNRSDGRTVEAVLEGPRDAVLKVIewARVgPPGARVEDVE 76
PRK14429 PRK14429
acylphosphatase; Provisional
 4-56 3.13e-05

acylphosphatase; Provisional


Pssm-ID: 184676  Cd Length: 90  Bit Score: 43.17  E-value: 3.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1852263780   4 RLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQG--LSVSSFLA 56
Cdd:PRK14429    3 RVLIKLTGKVQGVGCRRATLTKARALGVTGYVTNCEDGsVEILAQGsdPAVDNLIA 58
PRK14423 PRK14423
acylphosphatase; Provisional
 4-37 5.01e-05

acylphosphatase; Provisional


Pssm-ID: 237713  Cd Length: 92  Bit Score: 42.74  E-value: 5.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1852263780   4 RLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQN 37
Cdd:PRK14423    6 RAHVFVSGRVQGVYYRASTRDTARELGVDGWVRN 39
PRK14428 PRK14428
acylphosphatase; Provisional
 4-83 8.08e-05

acylphosphatase; Provisional


Pssm-ID: 172904  Cd Length: 97  Bit Score: 42.04  E-value: 8.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   4 RLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQGLS-VSSFLAQLLASLPPLAKIKDIETSHIALIDH 81
Cdd:PRK14428    9 RKHIVVTGLVQGVGFRYFTVTQARRLGVQGWVRNCRDGsVELEAQGSSdAVQALVEQLAIGPRWSEVSHVAVHDMPIIDE 88


                  ..
gi 1852263780  82 ES 83
Cdd:PRK14428   89 TA 90
PRK14436 PRK14436
acylphosphatase; Provisional
 4-72 8.18e-05

acylphosphatase; Provisional


Pssm-ID: 172912  Cd Length: 91  Bit Score: 41.87  E-value: 8.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852263780   4 RLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQN---NALGVLIEVQGLSVSSFLAQLLASlPPLAKIKDIE 72
Cdd:PRK14436    5 RAHLRIYGRVQGVGFRWSMQREARKLGVNGWVRNlpdGSVEAVLEGDEERVEALIGWAHQG-PPLARVTRVE 75
PRK14442 PRK14442
acylphosphatase; Provisional
 5-78 1.25e-04

acylphosphatase; Provisional


Pssm-ID: 172918  Cd Length: 91  Bit Score: 41.40  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852263780   5 LQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG---VLIEVQGLSVSSfLAQLLASLPPLAKIKDIETSHIAL 78
Cdd:PRK14442    6 LHAYVGGRVQGVGFRQATREEADRLELDGWVRNLDDGrveVVWEGEEDRAKA-LERWLGRGPRHAEVSAVEVEQMPL 81
PRK14434 PRK14434
acylphosphatase; Provisional
 4-87 1.93e-04

acylphosphatase; Provisional


Pssm-ID: 184680  Cd Length: 92  Bit Score: 40.90  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   4 RLQILIKGQVQGVGFRPHVYRVALRL-NLTGWVQNNALG-VLIEVQGLS---VSSFLAQLLASLPPLAKIKDIETShIAL 78
Cdd:PRK14434    3 KVRMIVSGRVQGVGFRYSVYSLALEIgDIYGRVWNNDDGtVEILAQSDDsakLAKFIQEIRKGPSKWAKVTYVDVT-MAN 81


                  ....*....
gi 1852263780  79 IDHESSFQI 87
Cdd:PRK14434   82 FEDFSDFKI 90
PRK14427 PRK14427
acylphosphatase; Provisional
 4-89 2.08e-04

acylphosphatase; Provisional


Pssm-ID: 172903  Cd Length: 94  Bit Score: 41.02  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   4 RLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG---VLIEVQGLSVSSFLAQLLASLPPlAKIKDIETSHIALID 80
Cdd:PRK14427    7 RLSARVFGVVQGVGFRYWTMRKAEELGLTGTVRNLDDGsvaLVAEGTGEQVEKLLDWLNSDRAP-GRVERVDHTVSEATG 85


                  ....*....
gi 1852263780  81 HESSFQIID 89
Cdd:PRK14427   86 EFREFRARD 94
PRK14437 PRK14437
acylphosphatase; Provisional
 5-87 2.09e-04

acylphosphatase; Provisional


Pssm-ID: 172913  Cd Length: 109  Bit Score: 41.25  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   5 LQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQGLSVS-SFLAQLLASLPPLAKIKDIETSHIALIDHe 82
Cdd:PRK14437   25 IHATVSGKVQGVFFRESVRKKAEELQLTGWVKNLSHGdVELVACGERDSiMILTEWLWEGPPQAAVSNVNWEEIVVEDY- 103


                  ....*
gi 1852263780  83 SSFQI 87
Cdd:PRK14437  104 SDFRV 108
PRK14448 PRK14448
acylphosphatase; Provisional
 6-72 6.69e-04

acylphosphatase; Provisional


Pssm-ID: 172924  Cd Length: 90  Bit Score: 39.36  E-value: 6.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852263780   6 QILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGVlIEVQGLSVSSFLAQLLASL---PPLAKIKDIE 72
Cdd:PRK14448    5 QFIVYGHVQGVGFRYFTWQEATKIGIKGYVKNRPDGS-VEVVAVGSDAQIAAFRDWLqhgPPTAVVCNVI 73
PRK14422 PRK14422
acylphosphatase; Provisional
 3-48 9.94e-04

acylphosphatase; Provisional


Pssm-ID: 237712  Cd Length: 93  Bit Score: 38.95  E-value: 9.94e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1852263780   3 ERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALG-VLIEVQG 48
Cdd:PRK14422    6 VRLTAWVHGHVQGVGFRWWTRSRALELGLTGYAANLADGrVQVVAEG 52
PRK14430 PRK14430
acylphosphatase; Provisional
 3-72 1.44e-03

acylphosphatase; Provisional


Pssm-ID: 172906  Cd Length: 92  Bit Score: 38.36  E-value: 1.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852263780   3 ERLQILIKGQVQGVGFRPHVYRVALRLNLTGWVQNNALGVlIEVQGLSVSSFLAQLLASL---PPLAKIKDIE 72
Cdd:PRK14430    4 ETWRLVAHGRVQGVGYRAACADAADDLGLGGWVRNRADGT-VEVMASGTVRQLEALRAWMeagPPAAQVTKVE 75
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 675-735 4.53e-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: 39.59  E-value: 4.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852263780 675 DWILFYAKKT-SINLVLlSGGCFLNQVLTEGLTKqlENHGLKVYLPqqlPA-NDGGISLGQVW 735
Cdd:cd24033   207 ELIKKLLERTgSDNLCL-SGGCALNCVANSKLAE--EGLFKNVFVP---PApGDSGLSLGAAL 263
ASKHA_NBD_MJ1051-like_N cd24100
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ...
 475-536 8.01e-03

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: 38.61  E-value: 8.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1852263780 475 PVIAVQHHHAHLASVVAEHQIMEPALGLALDGYGYGWDGKAW---GGELFLLKKGAQAQRLAHFY 536
Cdd:cd24100    71 KIIFVDHHLAHAASAYYTSPGFDDALVITLDGGGDGLSGTVSigeGGKLERLATSPALASLGLFY 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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