NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|501194192|ref|WP_012237210|]
View 

carbamoyltransferase HypF [Sorangium cellulosum]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 1-764 0e+00

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


:

Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1047.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGGVEIEVQGPERSLHAFVAGLTREPSAPARVERIEIERRAEQ 80
Cdd:COG0068    1 MKRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEEALEAFLEALRAEAPPLARIDSIEVEELPPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  81 DAGPFQILGSEAGNGARPSVPADLAVCEECAREVDSETGRRRRYPFTSCARCGPRYTILSGLPYDRARTTMDRFPMCPAC 160
Cdd:COG0068   81 GFDGFRILESEAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPDC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 161 AAEYADPSDRRFHAEPIACPACGPRVQLVAAARDPMDPGirssgspDGALREAAAAVLAGKVVAVKGLGGFHLLVDATSP 240
Cdd:COG0068  161 AAEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEG-------DDAIAAAAELLRAGKIVAIKGLGGFHLACDATNE 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 241 DAVALLRRRKRRDAKPFAVMFGSLDAVRGACRVSAAEADALRGPEAPIVLLRRLSPaaarVAIADAVAPGTPRLGALLPY 320
Cdd:COG0068  234 EAVARLRRRKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARPIVLLPKRPD----SPLAPSVAPGLDTLGVMLPY 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 321 TPLHRLVLELVGRPVVCTSGNLSDEPICTDASDALERLGGIADLFLVHDRPIVRPLDDSVARVGHAGVELLRRARGFTPL 400
Cdd:COG0068  310 TPLHHLLLDELGRPLVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVVRVIDGKPRFLRRARGYAPL 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 401 PLPLRIDAPPILALGGHLKSTTALFFDGQVVVSQHLGDAHTAEGAALIERTALDLTRLFRVRPERIACDLHPDYAGSRIA 480
Cdd:COG0068  390 PIPLPFELPPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLSTRLA 469

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 481 EQLaAAFRAPLVRVQHHHAHVAACVAEHGLDGPVLGLAWDGAGYGLDGALWGGEALVVDGASFRRAAHLRSFPLPGGERA 560
Cdd:COG0068  470 EEL-AERGLPLIEVQHHHAHIAAVMAEHGLDGPVLGIALDGTGYGDDGTIWGGEFLLGDYAGFERVGHLRPFPLPGGDKA 548

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 561 MREPRRSALGLLWELLGEGARDHARAWFRDAELGPLFSMLARGTGSPRTTSVGRLFDGVAALAGLRGAASFEGQAAMELE 640
Cdd:COG0068  549 AREPWRMALALLYEAGGEELLEPLLKRFSEKELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDEISYEGQAAMELE 628

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 641 CLAEAAGERAGYPLPLRASAAgmPAVIDFGPLLDAVLGDRRDGVSPGVIAARFHA----ALADVAEALAAASGLGRVVLA 716
Cdd:COG0068  629 ALADRAEEAEPYPFPLREIDG--LLVLDWAPLLRALLEDLQAGVPPAEIAARFHNtlaeAIAELALRLAERTGIDTVALS 706

                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*...
gi 501194192 717 GGCFQNALLAASIRERLTARGVEVFTPRLYPPGDGGLSLGQVLVAARR 764
Cdd:COG0068  707 GGVFQNRLLLELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAAR 754
 
Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 1-764 0e+00

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


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1047.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGGVEIEVQGPERSLHAFVAGLTREPSAPARVERIEIERRAEQ 80
Cdd:COG0068    1 MKRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEEALEAFLEALRAEAPPLARIDSIEVEELPPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  81 DAGPFQILGSEAGNGARPSVPADLAVCEECAREVDSETGRRRRYPFTSCARCGPRYTILSGLPYDRARTTMDRFPMCPAC 160
Cdd:COG0068   81 GFDGFRILESEAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPDC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 161 AAEYADPSDRRFHAEPIACPACGPRVQLVAAARDPMDPGirssgspDGALREAAAAVLAGKVVAVKGLGGFHLLVDATSP 240
Cdd:COG0068  161 AAEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEG-------DDAIAAAAELLRAGKIVAIKGLGGFHLACDATNE 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 241 DAVALLRRRKRRDAKPFAVMFGSLDAVRGACRVSAAEADALRGPEAPIVLLRRLSPaaarVAIADAVAPGTPRLGALLPY 320
Cdd:COG0068  234 EAVARLRRRKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARPIVLLPKRPD----SPLAPSVAPGLDTLGVMLPY 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 321 TPLHRLVLELVGRPVVCTSGNLSDEPICTDASDALERLGGIADLFLVHDRPIVRPLDDSVARVGHAGVELLRRARGFTPL 400
Cdd:COG0068  310 TPLHHLLLDELGRPLVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVVRVIDGKPRFLRRARGYAPL 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 401 PLPLRIDAPPILALGGHLKSTTALFFDGQVVVSQHLGDAHTAEGAALIERTALDLTRLFRVRPERIACDLHPDYAGSRIA 480
Cdd:COG0068  390 PIPLPFELPPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLSTRLA 469

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 481 EQLaAAFRAPLVRVQHHHAHVAACVAEHGLDGPVLGLAWDGAGYGLDGALWGGEALVVDGASFRRAAHLRSFPLPGGERA 560
Cdd:COG0068  470 EEL-AERGLPLIEVQHHHAHIAAVMAEHGLDGPVLGIALDGTGYGDDGTIWGGEFLLGDYAGFERVGHLRPFPLPGGDKA 548

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 561 MREPRRSALGLLWELLGEGARDHARAWFRDAELGPLFSMLARGTGSPRTTSVGRLFDGVAALAGLRGAASFEGQAAMELE 640
Cdd:COG0068  549 AREPWRMALALLYEAGGEELLEPLLKRFSEKELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDEISYEGQAAMELE 628

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 641 CLAEAAGERAGYPLPLRASAAgmPAVIDFGPLLDAVLGDRRDGVSPGVIAARFHA----ALADVAEALAAASGLGRVVLA 716
Cdd:COG0068  629 ALADRAEEAEPYPFPLREIDG--LLVLDWAPLLRALLEDLQAGVPPAEIAARFHNtlaeAIAELALRLAERTGIDTVALS 706

                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*...
gi 501194192 717 GGCFQNALLAASIRERLTARGVEVFTPRLYPPGDGGLSLGQVLVAARR 764
Cdd:COG0068  707 GGVFQNRLLLELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAAR 754
hypF TIGR00143
[NiFe] hydrogenase maturation protein HypF; A previously described regulatory effect of HypF ...
 40-762 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: 624.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   40 GVEIEVQG-PERSlhaFVAGLTREPSAPARVERIEIER-RAEQDAGPFQILGSEAGNGARPS-VPADLAVCEECAREVDS 116
Cdd:TIGR00143   4 GVEIVLEAdKEES---FLNRLKKGLPPLARIEKIIIEPfDGAEHFTTFRIRESKNGGLSLLSiIPADVATCSDCLEEMLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  117 ETGRRRRYPFTSCARCGPRYTILSGLPYDRARTTMDRFPMCPACAAEYADPSDRRFHAEPIACPACGPrvQLVAAARDpm 196
Cdd:TIGR00143  81 KNDRRYLYPFISCTHCGPRFTIIEALPYDRENTSMADFPLCPDCAKEYKDPLDRRFHAQPIACPRCGP--QLNFVSRG-- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  197 dpgirSSGSPDGALREAAAAVLAGKVVAVKGLGGFHLLVDATSPDAVALLRRRKRRDAKPFAVMFGSLDAVRGACRVSAA 276
Cdd:TIGR00143 157 -----GHAEQDDALLEAAKLLKKGKIIAIKGIGGFHLACDARNDEVVERLRLRKNRPLKPFAVMSPDLESAEQHAELNNL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  277 EADALRGPEAPIVLLRRlspaAARVAIADAVAPGTPRLGALLPYTPLHRLVLELVGRPVVCTSGNLSDEPICTDASDALE 356
Cdd:TIGR00143 232 ECELLTSPAAPIVLLRK----KPDIKLAPNIAPNLPTIGVMLPYTPLHHLLLQLLAFPLVMTSANLPGLPMAIDNAEILD 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  357 RLGGIADLFLVHDRPIVRPLDDSVARVGHAGVELLRRARGFTPLPLPLRIDA--PPILALGGHLKSTTALFFDGQVVVSQ 434
Cdd:TIGR00143 308 KLQGIADGFLVHNRRIVNRVDDSVVQHVAGEILFLRRSRGFAPQPLTLPPNGnpKKILALGAELKNTFSLLKGGQAYLSQ 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  435 HLGDAHTAEGAALIERTALDLTRLFRVRPERIACDLHPDYAGSRIAEQLAaafrAPLVRVQHHHAHVAACVAEHG-LDGP 513
Cdd:TIGR00143 388 HIGDLSVYETYKFFKEALNFFLRIYDFEPQDIVCDLHPQYNTTQYAEELS----LPVLRVQHHHAHALAVMADAGvLEEA 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  514 VLGLAWDGAGYGLDGALWGGEALVVDGASFRRAAHLRSFPLPGGERAMREPRRSALGLLWELLGEGARDHARAWF-RDAE 592
Cdd:TIGR00143 464 VIGITWDGVGYGEDGKIWGGECLLIDLGRIERLGRLEEFWLLGGDLATKYPLRILLSILLKHDLNDFLKRYQKYFkQEKE 543

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  593 LGPLFSMLARGTGSPRTTSVGRLFDGVAALAGLRGAASFEGQAAMELECLAEAAGERAGYPLPLRASAAgMPAVIDFGPL 672
Cdd:TIGR00143 544 LSVLQQALEKKINAPLTTSTGRLFDAVAAALGLCGERTYEGEAAIALEALALRSDGIANYPFEIKNKVL-DLKEFYQRFL 622

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  673 LDAVLGDRRDGVSpgVIAARFHAAL-ADVAEALAAASGLGRVVLAGGCFQNALLAASIRERLTARGVEVFTPRLYPPGDG 751
Cdd:TIGR00143 623 EDLLVGEDRSKIA--HIAHKFVASGlVEIATAIAVPFGIHKIVISGGVFYNRLLLERLAKYLKGLGFQFLFHRHLPPGDG 700

                         730
                  ....*....|.
gi 501194192  752 GLSLGQVLVAA 762
Cdd:TIGR00143 701 GISLGQAVAAA 711
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
 215-392 4.75e-43

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: 153.82  E-value: 4.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  215 AAVLAGKVVAVKGLGGFHLLVDATSPDAVALLRRRKRRDA-KPFAVMFGSLDAVRGACRvsAAEADALRGPEA----PIV 289
Cdd:pfam01300   1 EALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRdKPLAVMVADLEDLKEYAE--EVEEAALRLAERfwpgPLT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  290 LLRRLSPAAARVAIAdavaPGTPRLGALLPYTPLHRLVLELVGRPVVCTSGNLSDEPICTDASDALERLGGIADLFLVHD 369
Cdd:pfam01300  79 LVLKASKKPLPKLLT----PGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDGG 154

                         170       180
                  ....*....|....*....|...
gi 501194192  370 RpIVRPLDDSVARVGHAGVELLR 392
Cdd:pfam01300 155 R-IAGGVPSTVVDLTGGPPRILR 176
PRK14445 PRK14445
acylphosphatase; Provisional
 3-75 2.13e-15

acylphosphatase; Provisional


Pssm-ID: 172921  Cd Length: 91  Bit Score: 72.18  E-value: 2.13e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501194192   3 RLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSApARVERIEIE 75
Cdd:PRK14445   5 RVHLIVSGLVQGVGFRMFIDRAASELNLSGWVRNLPDGtVEIEAQGSSGMIDELIKQAERGPSR-SSVTSIMVE 77
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 712-763 5.05e-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: 5.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501194192 712 RVVLAGGCFQNALLAASIRERLtaRGVEVFTPrlyP-PGDGGLSLGQVLVAAR 763
Cdd:cd24033  220 NLCLSGGCALNCVANSKLAEEG--LFKNVFVP---PaPGDSGLSLGAALYVYH 267
 
Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 1-764 0e+00

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


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1047.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGGVEIEVQGPERSLHAFVAGLTREPSAPARVERIEIERRAEQ 80
Cdd:COG0068    1 MKRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEEALEAFLEALRAEAPPLARIDSIEVEELPPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  81 DAGPFQILGSEAGNGARPSVPADLAVCEECAREVDSETGRRRRYPFTSCARCGPRYTILSGLPYDRARTTMDRFPMCPAC 160
Cdd:COG0068   81 GFDGFRILESEAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPDC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 161 AAEYADPSDRRFHAEPIACPACGPRVQLVAAARDPMDPGirssgspDGALREAAAAVLAGKVVAVKGLGGFHLLVDATSP 240
Cdd:COG0068  161 AAEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEG-------DDAIAAAAELLRAGKIVAIKGLGGFHLACDATNE 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 241 DAVALLRRRKRRDAKPFAVMFGSLDAVRGACRVSAAEADALRGPEAPIVLLRRLSPaaarVAIADAVAPGTPRLGALLPY 320
Cdd:COG0068  234 EAVARLRRRKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARPIVLLPKRPD----SPLAPSVAPGLDTLGVMLPY 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 321 TPLHRLVLELVGRPVVCTSGNLSDEPICTDASDALERLGGIADLFLVHDRPIVRPLDDSVARVGHAGVELLRRARGFTPL 400
Cdd:COG0068  310 TPLHHLLLDELGRPLVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVVRVIDGKPRFLRRARGYAPL 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 401 PLPLRIDAPPILALGGHLKSTTALFFDGQVVVSQHLGDAHTAEGAALIERTALDLTRLFRVRPERIACDLHPDYAGSRIA 480
Cdd:COG0068  390 PIPLPFELPPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLSTRLA 469

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 481 EQLaAAFRAPLVRVQHHHAHVAACVAEHGLDGPVLGLAWDGAGYGLDGALWGGEALVVDGASFRRAAHLRSFPLPGGERA 560
Cdd:COG0068  470 EEL-AERGLPLIEVQHHHAHIAAVMAEHGLDGPVLGIALDGTGYGDDGTIWGGEFLLGDYAGFERVGHLRPFPLPGGDKA 548

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 561 MREPRRSALGLLWELLGEGARDHARAWFRDAELGPLFSMLARGTGSPRTTSVGRLFDGVAALAGLRGAASFEGQAAMELE 640
Cdd:COG0068  549 AREPWRMALALLYEAGGEELLEPLLKRFSEKELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDEISYEGQAAMELE 628

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 641 CLAEAAGERAGYPLPLRASAAgmPAVIDFGPLLDAVLGDRRDGVSPGVIAARFHA----ALADVAEALAAASGLGRVVLA 716
Cdd:COG0068  629 ALADRAEEAEPYPFPLREIDG--LLVLDWAPLLRALLEDLQAGVPPAEIAARFHNtlaeAIAELALRLAERTGIDTVALS 706

                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*...
gi 501194192 717 GGCFQNALLAASIRERLTARGVEVFTPRLYPPGDGGLSLGQVLVAARR 764
Cdd:COG0068  707 GGVFQNRLLLELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAAR 754
hypF TIGR00143
[NiFe] hydrogenase maturation protein HypF; A previously described regulatory effect of HypF ...
 40-762 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: 624.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   40 GVEIEVQG-PERSlhaFVAGLTREPSAPARVERIEIER-RAEQDAGPFQILGSEAGNGARPS-VPADLAVCEECAREVDS 116
Cdd:TIGR00143   4 GVEIVLEAdKEES---FLNRLKKGLPPLARIEKIIIEPfDGAEHFTTFRIRESKNGGLSLLSiIPADVATCSDCLEEMLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  117 ETGRRRRYPFTSCARCGPRYTILSGLPYDRARTTMDRFPMCPACAAEYADPSDRRFHAEPIACPACGPrvQLVAAARDpm 196
Cdd:TIGR00143  81 KNDRRYLYPFISCTHCGPRFTIIEALPYDRENTSMADFPLCPDCAKEYKDPLDRRFHAQPIACPRCGP--QLNFVSRG-- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  197 dpgirSSGSPDGALREAAAAVLAGKVVAVKGLGGFHLLVDATSPDAVALLRRRKRRDAKPFAVMFGSLDAVRGACRVSAA 276
Cdd:TIGR00143 157 -----GHAEQDDALLEAAKLLKKGKIIAIKGIGGFHLACDARNDEVVERLRLRKNRPLKPFAVMSPDLESAEQHAELNNL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  277 EADALRGPEAPIVLLRRlspaAARVAIADAVAPGTPRLGALLPYTPLHRLVLELVGRPVVCTSGNLSDEPICTDASDALE 356
Cdd:TIGR00143 232 ECELLTSPAAPIVLLRK----KPDIKLAPNIAPNLPTIGVMLPYTPLHHLLLQLLAFPLVMTSANLPGLPMAIDNAEILD 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  357 RLGGIADLFLVHDRPIVRPLDDSVARVGHAGVELLRRARGFTPLPLPLRIDA--PPILALGGHLKSTTALFFDGQVVVSQ 434
Cdd:TIGR00143 308 KLQGIADGFLVHNRRIVNRVDDSVVQHVAGEILFLRRSRGFAPQPLTLPPNGnpKKILALGAELKNTFSLLKGGQAYLSQ 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  435 HLGDAHTAEGAALIERTALDLTRLFRVRPERIACDLHPDYAGSRIAEQLAaafrAPLVRVQHHHAHVAACVAEHG-LDGP 513
Cdd:TIGR00143 388 HIGDLSVYETYKFFKEALNFFLRIYDFEPQDIVCDLHPQYNTTQYAEELS----LPVLRVQHHHAHALAVMADAGvLEEA 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  514 VLGLAWDGAGYGLDGALWGGEALVVDGASFRRAAHLRSFPLPGGERAMREPRRSALGLLWELLGEGARDHARAWF-RDAE 592
Cdd:TIGR00143 464 VIGITWDGVGYGEDGKIWGGECLLIDLGRIERLGRLEEFWLLGGDLATKYPLRILLSILLKHDLNDFLKRYQKYFkQEKE 543

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  593 LGPLFSMLARGTGSPRTTSVGRLFDGVAALAGLRGAASFEGQAAMELECLAEAAGERAGYPLPLRASAAgMPAVIDFGPL 672
Cdd:TIGR00143 544 LSVLQQALEKKINAPLTTSTGRLFDAVAAALGLCGERTYEGEAAIALEALALRSDGIANYPFEIKNKVL-DLKEFYQRFL 622

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  673 LDAVLGDRRDGVSpgVIAARFHAAL-ADVAEALAAASGLGRVVLAGGCFQNALLAASIRERLTARGVEVFTPRLYPPGDG 751
Cdd:TIGR00143 623 EDLLVGEDRSKIA--HIAHKFVASGlVEIATAIAVPFGIHKIVISGGVFYNRLLLERLAKYLKGLGFQFLFHRHLPPGDG 700

                         730
                  ....*....|.
gi 501194192  752 GLSLGQVLVAA 762
Cdd:TIGR00143 701 GISLGQAVAAA 711
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
 215-392 4.75e-43

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: 153.82  E-value: 4.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  215 AAVLAGKVVAVKGLGGFHLLVDATSPDAVALLRRRKRRDA-KPFAVMFGSLDAVRGACRvsAAEADALRGPEA----PIV 289
Cdd:pfam01300   1 EALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPRdKPLAVMVADLEDLKEYAE--EVEEAALRLAERfwpgPLT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  290 LLRRLSPAAARVAIAdavaPGTPRLGALLPYTPLHRLVLELVGRPVVCTSGNLSDEPICTDASDALERLGGIADLFLVHD 369
Cdd:pfam01300  79 LVLKASKKPLPKLLT----PGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDGG 154

                         170       180
                  ....*....|....*....|...
gi 501194192  370 RpIVRPLDDSVARVGHAGVELLR 392
Cdd:pfam01300 155 R-IAGGVPSTVVDLTGGPPRILR 176
HypF_C pfam17788
HypF Kae1-like domain; This domain is found in the HypF protein. In the structure it is one of ...
 407-507 9.17e-40

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: 141.84  E-value: 9.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  407 DAPPILALGGHLKSTTALFFDGQVVVSQHLGDAHTAEGAALIERTALDLTRLFRVRPERIACDLHPDYAGSRIAEQLaaa 486
Cdd:pfam17788   2 AKPPVLALGAELKNTFALAKGGQAFLSQHIGDLDNLETLEAFEETLEHLLRLYGIKPEVIACDLHPDYLSTRLAEEL--- 78

                          90       100
                  ....*....|....*....|.
gi 501194192  487 FRAPLVRVQHHHAHVAACVAE 507
Cdd:pfam17788  79 NGLPLIEVQHHHAHIAAVMAE 99
Acylphosphatase pfam00708
Acylphosphatase;
6-87 5.14e-26

Acylphosphatase;


Pssm-ID: 425830  Cd Length: 85  Bit Score: 101.89  E-value: 5.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192    6 LRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSaPARVERIEIERRAEQ-DAG 83
Cdd:pfam00708   3 VLVTGRVQGVGFRPFVYRLAKELGLKGWVRNLPDGsVEIVVQGPEEDVDKFLEWLKSGPP-PARVDKVEVTEIDEPgDFS 81


                  ....
gi 501194192   84 PFQI 87
Cdd:pfam00708  82 GFEI 85
AcyP COG1254
Acylphosphatase [Energy production and conversion];
1-88 1.88e-24

Acylphosphatase [Energy production and conversion];


Pssm-ID: 440866  Cd Length: 89  Bit Score: 97.92  E-value: 1.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSApARVERIEIERRAE 79
Cdd:COG1254    1 MKRVRIIVSGRVQGVGFRAFTRRQARRLGLTGWVRNLPDGsVEVVAEGEEEAVEAFLEWLRKGPPA-ARVEDVEVEEEEP 79

                         90
                 ....*....|
gi 501194192  80 QDAGP-FQIL 88
Cdd:COG1254   80 TGEFEgFEIR 89
zf-HYPF pfam07503
HypF finger; The HypF family of proteins are involved in the maturation and regulation of ...
 157-189 2.60e-16

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: 72.77  E-value: 2.60e-16
                          10        20        30
                  ....*....|....*....|....*....|...
gi 501194192  157 CPACAAEYADPSDRRFHAEPIACPACGPRVQLV 189
Cdd:pfam07503   1 CPDCLREYFDPLDRRFHAQFIACTNCGPRLSLI 33
PRK14445 PRK14445
acylphosphatase; Provisional
 3-75 2.13e-15

acylphosphatase; Provisional


Pssm-ID: 172921  Cd Length: 91  Bit Score: 72.18  E-value: 2.13e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501194192   3 RLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSApARVERIEIE 75
Cdd:PRK14445   5 RVHLIVSGLVQGVGFRMFIDRAASELNLSGWVRNLPDGtVEIEAQGSSGMIDELIKQAERGPSR-SSVTSIMVE 77
PRK14420 PRK14420
acylphosphatase; Provisional
 1-81 2.25e-14

acylphosphatase; Provisional


Pssm-ID: 237710  Cd Length: 91  Bit Score: 69.06  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLtREPSAPARVERIEIERRAE 79
Cdd:PRK14420   1 MLQYHIIVDGRVQGVGFRYFVQMEADKRKLTGWVKNRDDGtVEIEAEGPEEALQLFLDAI-EKGSPFSKVTDVHIEERDV 79


                 ..
gi 501194192  80 QD 81
Cdd:PRK14420  80 LS 81
PRK14448 PRK14448
acylphosphatase; Provisional
 8-88 1.09e-13

acylphosphatase; Provisional


Pssm-ID: 172924  Cd Length: 90  Bit Score: 67.09  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   8 VYGIVQGVGFRPFVYRRASALGLGGWVRNRP-GGVEIEVQGPERSLHAFVAGLTREPSApARVER-IEIERRAEQDAGPF 85
Cdd:PRK14448   8 VYGHVQGVGFRYFTWQEATKIGIKGYVKNRPdGSVEVVAVGSDAQIAAFRDWLQHGPPT-AVVCNvIEQDYQGSRQFTHF 86


                 ...
gi 501194192  86 QIL 88
Cdd:PRK14448  87 SVR 89
PRK14436 PRK14436
acylphosphatase; Provisional
 3-89 4.60e-13

acylphosphatase; Provisional


Pssm-ID: 172912  Cd Length: 91  Bit Score: 65.37  E-value: 4.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   3 RLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRP-GGVEIEVQGPERSLHAFVAGLTREPSApARVERIEIERRAEQD 81
Cdd:PRK14436   5 RAHLRIYGRVQGVGFRWSMQREARKLGVNGWVRNLPdGSVEAVLEGDEERVEALIGWAHQGPPL-ARVTRVEVKWEEPKG 83


                 ....*...
gi 501194192  82 AGPFQILG 89
Cdd:PRK14436  84 EKGFRVVG 91
PRK14424 PRK14424
acylphosphatase; Provisional
 6-79 6.36e-13

acylphosphatase; Provisional


Pssm-ID: 184674  Cd Length: 94  Bit Score: 65.25  E-value: 6.36e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501194192   6 LRVYGIVQGVGFRPFVYRRASALGLGGWVRNRP-GGVEIEVQGPERSLHAFVAGLTREPSApARVERIEIERRAE 79
Cdd:PRK14424  11 VRVRGVVQGVGFRHATVREAHALGLRGWVANLEdGTVEAMIQGPAAQIDRMLAWLRHGPPA-ARVTEVTFEERRT 84
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
 209-366 8.16e-13

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: 67.81  E-value: 8.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 209 ALREAAAAVLAGKVVA-----VKGLGGfhllvDATSPDAVALLRRRKRRDA-KPFAVMFGSLDAVRG-ACRVSAAEADAL 281
Cdd:COG0009   11 LIEQAAEALRAGGVVAyptdtVYGLGC-----DALNKEAVERIFAIKGRPRdKPLIVLVADLSQLEEyAKEVPDAARRLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192 282 R----GP-----EAPIVLLRRLspaaarvaiadavapgTPRLGallpyT-----PLHRLVLELV---GRPVVCTSGNLSD 344
Cdd:COG0009   86 KafwpGPltlilPATKEVPDLL----------------TGGRD-----TvavrvPDHPVALALLralGPPLASTSANLSG 144

                        170       180
                 ....*....|....*....|..
gi 501194192 345 EPICTDASDALERLGGIADLFL 366
Cdd:COG0009  145 EPPPTTAEEVREQLGDRVDLIL 166
PRK14440 PRK14440
acylphosphatase; Provisional
 1-73 2.48e-12

acylphosphatase; Provisional


Pssm-ID: 172916  Cd Length: 90  Bit Score: 63.29  E-value: 2.48e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRP-GGVEIEVQGPERSLHAFVAGLTREPSApARVERIE 73
Cdd:PRK14440   2 LKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPdGSVEVVAEGYEEALSKLLERIKQGPPA-AEVEKVD 74
zf-HYPF pfam07503
HypF finger; The HypF family of proteins are involved in the maturation and regulation of ...
 107-139 6.01e-12

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: 60.44  E-value: 6.01e-12
                          10        20        30
                  ....*....|....*....|....*....|...
gi 501194192  107 CEECAREVDSETGRRRRYPFTSCARCGPRYTIL 139
Cdd:pfam07503   1 CPDCLREYFDPLDRRFHAQFIACTNCGPRLSLI 33
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
 209-366 1.18e-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: 64.66  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  209 ALREAAAAVLAGKVVAVKGLGGFHLLVDATSPDAVALLRR-RKRRDAKPFAVMFGSLDAVRGACRVSAaeaDALR----- 282
Cdd:TIGR00057  10 GIEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRiKGRPSNKPLTVLVSDLSEIEKYAYVPD---DAKRlmkkf 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192  283 --GP-----EAPIVLLRRLSPAAArvaiadavapgtpRLGALLPYTPLHRLVLELVGRPVVCTSGNLSDEPICTDASDAL 355
Cdd:TIGR00057  87 wpGPltlvlKKTPEIPRRVSGKRK-------------TIGIRVPDNPIALELLEELGKPIVATSANLSGKPSATDVEEAV 153

                         170
                  ....*....|.
gi 501194192  356 ERLGGIADLFL 366
Cdd:TIGR00057 154 DELGKLVDLII 164
PRK14435 PRK14435
acylphosphatase; Provisional
 1-87 2.96e-11

acylphosphatase; Provisional


Pssm-ID: 184681  Cd Length: 90  Bit Score: 60.31  E-value: 2.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRP-GGVEIEVQGPERSLHAFVAGLTREPSApARVERIEIERRAE 79
Cdd:PRK14435   1 MKALKIRVEGIVQGVGFRYFTRRVAKSLGVKGYVMNMDdGSVFIHAEGDENALRRFLNEVAKGPPA-AVVTNVSVEETTP 79


                 ....*...
gi 501194192  80 QDAGPFQI 87
Cdd:PRK14435  80 EGYEDFTI 87
PRK14421 PRK14421
acylphosphatase; Provisional
 8-84 3.07e-11

acylphosphatase; Provisional


Pssm-ID: 237711 [Multi-domain]  Cd Length: 99  Bit Score: 60.59  E-value: 3.07e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501194192   8 VYGIVQGVGFRPFVYRRASALGLGGWVRN-RPGGVEIEVQGPERSLHAFVAGLTREPSApARVERIEierraEQDAGP 84
Cdd:PRK14421  10 IRGRVQGVGYRAWVARTAEALGLEGWVRNrRDGSVEALFAGPADAVAEMIARCRRGPSA-ARVDAVE-----DEPAAP 81
PRK14431 PRK14431
acylphosphatase; Provisional
 1-75 3.67e-11

acylphosphatase; Provisional


Pssm-ID: 184677  Cd Length: 89  Bit Score: 59.81  E-value: 3.67e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGGVEIEVQGPERSLHAFVAGLTREPSAPARVERIEIE 75
Cdd:PRK14431   1 MRHIHLQVFGRVQGVGFRYFTQRIAMNYNIVGTVQNVDDYVEIYAQGDDADLERFIQGVIEGASPASNVTSYQLE 75
PRK14452 PRK14452
acylphosphatase; Provisional
 3-87 1.39e-10

acylphosphatase; Provisional


Pssm-ID: 237716  Cd Length: 107  Bit Score: 59.09  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   3 RLALRVYGIVQGVGFRPFVYRRASALGLGGWVRN-RPGGVEIEVQGPERSLHAFVAGLTREPSApARVERIEIERRAEQD 81
Cdd:PRK14452  21 RWRFLIEGRVQGVGFRASCCRRALDLGLSGWVRNlSDGSVEVQAEGPPLALSELRAWCERGPPG-ARVKRVDPSQLPVTG 99


                 ....*.
gi 501194192  82 AGPFQI 87
Cdd:PRK14452 100 DDWFEV 105
PRK14430 PRK14430
acylphosphatase; Provisional
 6-83 6.81e-10

acylphosphatase; Provisional


Pssm-ID: 172906  Cd Length: 92  Bit Score: 56.47  E-value: 6.81e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501194192   6 LRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSApARVERIEIERRAEQDAG 83
Cdd:PRK14430   8 LVAHGRVQGVGYRAACADAADDLGLGGWVRNRADGtVEVMASGTVRQLEALRAWMEAGPPA-AQVTKVEVGPGAGEFAG 85
PRK14427 PRK14427
acylphosphatase; Provisional
 3-73 2.08e-09

acylphosphatase; Provisional


Pssm-ID: 172903  Cd Length: 94  Bit Score: 55.27  E-value: 2.08e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501194192   3 RLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRP-GGVEIEVQGPERSLHAFVAGLTREpSAPARVERIE 73
Cdd:PRK14427   7 RLSARVFGVVQGVGFRYWTMRKAEELGLTGTVRNLDdGSVALVAEGTGEQVEKLLDWLNSD-RAPGRVERVD 77
PRK14426 PRK14426
acylphosphatase; Provisional
 8-75 2.17e-09

acylphosphatase; Provisional


Pssm-ID: 184675  Cd Length: 92  Bit Score: 55.03  E-value: 2.17e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501194192   8 VYGIVQGVGFRPFVYRRASALGLGGWVRNR-PGGVEIEVQGPERSLHAFVAGLTREPSAPARVERIEIE 75
Cdd:PRK14426  10 VYGRVQGVGFRYHTQHEALKLGLTGYAKNLdDGSVEVVACGEEEQVEKLMEWLKEGGPRSARVDRVLTE 78
PRK14449 PRK14449
acylphosphatase; Provisional
 6-73 2.18e-09

acylphosphatase; Provisional


Pssm-ID: 184682  Cd Length: 90  Bit Score: 54.83  E-value: 2.18e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501194192   6 LRVYGIVQGVGFRPFVYRRASALGLGGWVRNRP-GGVEIEVQGPERS----LHAFVAGLTRepsapARVERIE 73
Cdd:PRK14449   7 LRITGHVQGVGLRYSVYQKAVSLGITGYAENLYdGSVEVVAEGDEENikelINFIKTGLRW-----ARVDNVE 74
PRK14433 PRK14433
acylphosphatase; Provisional
 2-87 6.21e-09

acylphosphatase; Provisional


Pssm-ID: 184679  Cd Length: 87  Bit Score: 53.66  E-value: 6.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   2 PRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSApARVERIEIERRAEQ 80
Cdd:PRK14433   1 MRLTALVSGRVQGVGYRAFVQKKARELGLSGYAENLSDGrVEVVAEGPKEALERLLHWLRRGPRH-ARVEAVDVQWSEAT 79


                 ....*..
gi 501194192  81 DAGPFQI 87
Cdd:PRK14433  80 GLKGFHV 86
PRK14429 PRK14429
acylphosphatase; Provisional
 1-75 9.00e-09

acylphosphatase; Provisional


Pssm-ID: 184676  Cd Length: 90  Bit Score: 53.19  E-value: 9.00e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRN-RPGGVEIEVQGPERSLHAFVAGLtrEPSAP-ARVERIEIE 75
Cdd:PRK14429   1 MKRVLIKLTGKVQGVGCRRATLTKARALGVTGYVTNcEDGSVEILAQGSDPAVDNLIAWC--EVGVPcTEVLRVTVE 75
PRK14450 PRK14450
acylphosphatase; Provisional
 1-75 1.03e-08

acylphosphatase; Provisional


Pssm-ID: 184683  Cd Length: 91  Bit Score: 52.93  E-value: 1.03e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGGVEIEV--QGPERSLHAFVAGLTrepSAPARVERIEIE 75
Cdd:PRK14450   1 MHCLKAIVKGKVQGVYFRDFTRTQATRLGLCGYAKNLANGNEVEVvaEGDKDSLLEFLDLLR---SGPPRAEVKEVE 74
PRK14428 PRK14428
acylphosphatase; Provisional
 3-63 1.05e-08

acylphosphatase; Provisional


Pssm-ID: 172904  Cd Length: 97  Bit Score: 53.21  E-value: 1.05e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501194192   3 RLALRVYGIVQGVGFRPFVYRRASALGLGGWVRN-RPGGVEIEVQGPERSLHAFVAGLTREP 63
Cdd:PRK14428   9 RKHIVVTGLVQGVGFRYFTVTQARRLGVQGWVRNcRDGSVELEAQGSSDAVQALVEQLAIGP 70
PRK14441 PRK14441
acylphosphatase; Provisional
 3-87 9.51e-08

acylphosphatase; Provisional


Pssm-ID: 172917  Cd Length: 93  Bit Score: 50.36  E-value: 9.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   3 RLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSApARVERIEIERRAEQ- 80
Cdd:PRK14441   6 RARIVVSGRVQGVAFRQSAADEARRLGVEGWVRNLPDGrVEAEAEGERAAVGALVRWCHAGPPA-ARVDRVEVEWVEPAg 84


                 ....*..
gi 501194192  81 DAGPFQI 87
Cdd:PRK14441  85 DLGAFEI 91
PRK14438 PRK14438
acylphosphatase; Provisional
 3-76 1.12e-07

acylphosphatase; Provisional


Pssm-ID: 172914  Cd Length: 91  Bit Score: 50.22  E-value: 1.12e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501194192   3 RLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSApARVERIEIER 76
Cdd:PRK14438   4 RAMVTVKGLVQGVAFRHHTQQTAQRLNVSGWVKNLPNGsVQGCFEGEETDVAALIDWCHHGPSR-ARVSGVIVER 77
PRK14423 PRK14423
acylphosphatase; Provisional
 8-87 3.15e-07

acylphosphatase; Provisional


Pssm-ID: 237713  Cd Length: 92  Bit Score: 48.91  E-value: 3.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   8 VYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVaGLTREPSAPARVERIEIERRAEQDAGPFQ 86
Cdd:PRK14423  11 VSGRVQGVYYRASTRDTARELGVDGWVRNLDDGrVEAVFEGPRDAVEAMV-EWCHEGSPAAVVEDVEVEYEEPEGLDGFE 89


                 .
gi 501194192  87 I 87
Cdd:PRK14423  90 I 90
PRK14442 PRK14442
acylphosphatase; Provisional
 1-87 3.77e-07

acylphosphatase; Provisional


Pssm-ID: 172918  Cd Length: 91  Bit Score: 48.72  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   1 MPRLALRVY--GIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSApARVERIEIERR 77
Cdd:PRK14442   1 MARICLHAYvgGRVQGVGFRQATREEADRLELDGWVRNLDDGrVEVVWEGEEDRAKALERWLGRGPRH-AEVSAVEVEQM 79

                         90
                 ....*....|
gi 501194192  78 AEQDAGPFQI 87
Cdd:PRK14442  80 PLQGIAGFVV 89
PRK14443 PRK14443
acylphosphatase; Provisional
 6-88 9.08e-07

acylphosphatase; Provisional


Pssm-ID: 172919  Cd Length: 93  Bit Score: 47.75  E-value: 9.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   6 LRVYGIVQGVGFRPFVYRRASALGLGGWVRN-RPGGVEIEVQGPERSLHAFVAGLTREPSAPARVERIEIERRAE-QDAG 83
Cdd:PRK14443   8 LRVTGFVQGVGFRYTTKHVAYKYDISGTVKNlDDGSVEIHAIAEEENLNKFIDAIKKGPSPGCRIEHVYIYKGAPvEERK 87


                 ....*
gi 501194192  84 PFQIL 88
Cdd:PRK14443  88 TFDIV 92
PRK14422 PRK14422
acylphosphatase; Provisional
 3-72 1.14e-06

acylphosphatase; Provisional


Pssm-ID: 237712  Cd Length: 93  Bit Score: 47.43  E-value: 1.14e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501194192   3 RLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSaPARVERI 72
Cdd:PRK14422   7 RLTAWVHGHVQGVGFRWWTRSRALELGLTGYAANLADGrVQVVAEGPRAACEKLLQLLRGDDT-PGRVDKV 76
PRK14451 PRK14451
acylphosphatase; Provisional
 8-88 3.09e-06

acylphosphatase; Provisional


Pssm-ID: 237715  Cd Length: 89  Bit Score: 46.07  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   8 VYGIVQGVGFRPFVYRRASALGLGGWVRN-RPGGVEIEVQGPERSLHAFVAGLTREPSApARVERIEIERRAEQDAGPFQ 86
Cdd:PRK14451   9 ISGRVQGVWFRASAKKLAEQLMISGWARNlADGRVEVFACGKEDKLEEFYTWLQKGPLN-ARVDVCTRENLPWQDYISFD 87


                 ..
gi 501194192  87 IL 88
Cdd:PRK14451  88 VL 89
PRK14425 PRK14425
acylphosphatase; Provisional
 6-75 3.49e-06

acylphosphatase; Provisional


Pssm-ID: 172901  Cd Length: 94  Bit Score: 46.00  E-value: 3.49e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501194192   6 LRVYGIVQGVGFRPFVYRRASALGLGGWVRNRP-GGVEIEVQGPERSLHAFVAGLTREPSApARVERIEIE 75
Cdd:PRK14425  10 VRITGRVQGVGFRDWTRDEAERLGLTGWVRNESdGSVTALIAGPDSAISAMIERFRRGPPG-ASVSGVETE 79
PRK14444 PRK14444
acylphosphatase; Provisional
 1-74 6.52e-06

acylphosphatase; Provisional


Pssm-ID: 172920  Cd Length: 92  Bit Score: 45.26  E-value: 6.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG-VEIEVQGPERSLHAFVAGLTREPSApARVERIEI 74
Cdd:PRK14444   3 MVRAHVFISGRVQGVNFRAYTRDRAREAGVKGWVRNLSDGrVEAVFEGSRPAVQKMISWCYSGPSH-ARVERVEV 76
PRK14434 PRK14434
acylphosphatase; Provisional
 1-87 1.22e-05

acylphosphatase; Provisional


Pssm-ID: 184680  Cd Length: 92  Bit Score: 44.36  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYrrASALGLGG-----WvRNRPGGVEIEVQGP-ERSLHAFVAGLTREPSAPARVERIEI 74
Cdd:PRK14434   1 MQKVRMIVSGRVQGVGFRYSVY--SLALEIGDiygrvW-NNDDGTVEILAQSDdSAKLAKFIQEIRKGPSKWAKVTYVDV 77

                         90
                 ....*....|...
gi 501194192  75 ERRAEQDAGPFQI 87
Cdd:PRK14434  78 TMANFEDFSDFKI 90
PRK14447 PRK14447
acylphosphatase; Provisional
 1-86 3.26e-05

acylphosphatase; Provisional


Pssm-ID: 172923  Cd Length: 95  Bit Score: 43.39  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   1 MPRLALRVYGIVQGVGFRPFVYRRASALGLGGWVRNRPGG--VEIEVQGPeRSLHAFVAGLTREPSAPARVERIEIerRA 78
Cdd:PRK14447   3 MVRAHLFIRGKVQGVFFRQSMKEVANRNGVRGWVRNRSDGrtVEAVLEGP-RDAVLKVIEWARVGPPGARVEDVEV--KW 79


                 ....*...
gi 501194192  79 EQDAGPFQ 86
Cdd:PRK14447  80 EEYKGEFQ 87
PRK14446 PRK14446
acylphosphatase; Provisional
 8-72 2.77e-04

acylphosphatase; Provisional


Pssm-ID: 172922  Cd Length: 88  Bit Score: 40.47  E-value: 2.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501194192   8 VYGIVQGVGFRPFVYRRASALGLGGWVRNRP-GGVEIEVQGPERSLHAFVAGLTREPSApARVERI 72
Cdd:PRK14446   8 VSGVVQGVWYRASTRERAVALGLVGHARNQAdGSVEVVAAGSAAALEALEAWLWQGPPA-ATVAAV 72
PRK14439 PRK14439
acylphosphatase; Provisional
 8-72 9.95e-04

acylphosphatase; Provisional


Pssm-ID: 237714  Cd Length: 163  Bit Score: 40.45  E-value: 9.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501194192   8 VYGIVQGVGFRPFVYRRASALGLGGWVRN-RPGGVEIEVQGPERSLHAFVAGLTREPSAPARVERI 72
Cdd:PRK14439  81 VYGRVQGVGFRYTTQYEAKKLGLTGYAKNlDDGSVEVVACGEEGQVEKLMQWLKSGGPRSARVERV 146
PRK14437 PRK14437
acylphosphatase; Provisional
 8-87 1.89e-03

acylphosphatase; Provisional


Pssm-ID: 172913  Cd Length: 109  Bit Score: 38.55  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501194192   8 VYGIVQGVGFRPFVYRRASALGLGGWVRN-RPGGVEIEVQGPERSLHAFVAGLTREPSAPArVERIEIERRAEQDAGPFQ 86
Cdd:PRK14437  29 VSGKVQGVFFRESVRKKAEELQLTGWVKNlSHGDVELVACGERDSIMILTEWLWEGPPQAA-VSNVNWEEIVVEDYSDFR 107


                 .
gi 501194192  87 I 87
Cdd:PRK14437 108 V 108
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 712-763 5.05e-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: 5.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501194192 712 RVVLAGGCFQNALLAASIRERLtaRGVEVFTPrlyP-PGDGGLSLGQVLVAAR 763
Cdd:cd24033  220 NLCLSGGCALNCVANSKLAEEG--LFKNVFVP---PaPGDSGLSLGAALYVYH 267
ASKHA_NBD_MJ1051-like_N cd24100
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ...
 709-764 6.69e-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: 38.99  E-value: 6.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501194192 709 GLGRVVLAGGCFQNALLAASIRERLTARGVEVFtPrlyPPGDGGLSLGQVLVAARR 764
Cdd:cd24100  187 GIKNLALAGGVFANVKLNQRIAELPEVENLFVF-P---SMGDGGLALGAALLALAE 238
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH