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Conserved domains on  [gi|2021001947|ref|WP_208854623|]
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carbamoyltransferase HypF [Corynebacterium amycolatum]

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, ...
 1-780 0e+00

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


:

Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1016.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQGVFIEVEGTSDALAAFCSQLFTELPALARIINHSAEPVAVL 80
Cdd:COG0068     1 MKRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEEALEAFLEALRAEAPPLARIDSIEVEELPPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947  81 GhEHEFTIVPSRHSYSGRALLPPDTALCPDCRREFFDPTNPRYLYPFISCTNCGPRLSIITELPYDRPRTTMAAFPMCTP 160
Cdd:COG0068    81 G-FDGFRILESEAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 161 CEREYTDPTDRRYHAQPISCFDCGPRLSWHDAGDTTTATSREEVlalfRRAHALLDDGALLAVKGIGGFHLVCDATNDAA 240
Cdd:COG0068   160 CAAEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEGDDAI----AAAAELLRAGKIVAIKGLGGFHLACDATNEEA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 241 CEKLRLRKRRPDKPLAVMAPTVDTAAQLVELTEQEKRFLDSPEAPIVIAPKQRSGPLSNLIAPGLDSFGIMLPYSGIHLL 320
Cdd:COG0068   236 VARLRRRKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARPIVLLPKRPDSPLAPSVAPGLDTLGVMLPYTPLHHL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 321 LCD---RPLVVTSGNLSGEPVCTDNADALKKLGHIADAFILHDREIHVPVEDSV--FIGTAPS--RRSRGFAPIPVSITa 393
Cdd:COG0068   316 LLDelgRPLVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVvrVIDGKPRflRRARGYAPLPIPLP- 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 394 tdsrshtstgpgsatgpgisvrcTSQPTIFATGGELKNTFAIAHGDLAHVSAHIGDMGSWASQKAYQRAVDQLLSMRDAT 473
Cdd:COG0068   395 -----------------------FELPPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVR 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 474 PELVVCDLHPGYATTAFAERFaAEHDIELLAVQHHFAHALSLLAEHRLlspnADRAVVATLDGTGYGTDGSIWGGEILTL 553
Cdd:COG0068   452 PEVIACDLHPDYLSTRLAEEL-AERGLPLIEVQHHHAHIAAVMAEHGL----DGPVLGIALDGTGYGDDGTIWGGEFLLG 526

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 554 SRssANWERTWHCPTFPLVGGDRAVTHPWRLALGLTHAWELDD--DHLLRNLSnEREVALVKSQLATGVGTVQTSSLGRI 631
Cdd:COG0068   527 DY--AGFERVGHLRPFPLPGGDKAAREPWRMALALLYEAGGEEllEPLLKRFS-EKELALLRQMLERGINSPLTSSAGRL 603

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 632 FDAAAALLLPRWRgggaISYEAQAAMELEAAATRYVRSHAEALGAVSSETKSEH-----LQEVIREAVASPDVEQAAFVF 706
Cdd:COG0068   604 FDAVAALLGICDE----ISYEGQAAMELEALADRAEEAEPYPFPLREIDGLLVLdwaplLRALLEDLQAGVPPAEIAARF 679

                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021001947 707 HSGVAGLVGKRLVQAAEKSGTDVVGVSGGCANNALLMELLRHEVATEGFTLLQHQIVPPGDGGLSLGQAVAGRL 780
Cdd:COG0068   680 HNTLAEAIAELALRLAERTGIDTVALSGGVFQNRLLLELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAA 753
 
Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 1-780 0e+00

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


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1016.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQGVFIEVEGTSDALAAFCSQLFTELPALARIINHSAEPVAVL 80
Cdd:COG0068     1 MKRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEEALEAFLEALRAEAPPLARIDSIEVEELPPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947  81 GhEHEFTIVPSRHSYSGRALLPPDTALCPDCRREFFDPTNPRYLYPFISCTNCGPRLSIITELPYDRPRTTMAAFPMCTP 160
Cdd:COG0068    81 G-FDGFRILESEAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 161 CEREYTDPTDRRYHAQPISCFDCGPRLSWHDAGDTTTATSREEVlalfRRAHALLDDGALLAVKGIGGFHLVCDATNDAA 240
Cdd:COG0068   160 CAAEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEGDDAI----AAAAELLRAGKIVAIKGLGGFHLACDATNEEA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 241 CEKLRLRKRRPDKPLAVMAPTVDTAAQLVELTEQEKRFLDSPEAPIVIAPKQRSGPLSNLIAPGLDSFGIMLPYSGIHLL 320
Cdd:COG0068   236 VARLRRRKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARPIVLLPKRPDSPLAPSVAPGLDTLGVMLPYTPLHHL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 321 LCD---RPLVVTSGNLSGEPVCTDNADALKKLGHIADAFILHDREIHVPVEDSV--FIGTAPS--RRSRGFAPIPVSITa 393
Cdd:COG0068   316 LLDelgRPLVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVvrVIDGKPRflRRARGYAPLPIPLP- 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 394 tdsrshtstgpgsatgpgisvrcTSQPTIFATGGELKNTFAIAHGDLAHVSAHIGDMGSWASQKAYQRAVDQLLSMRDAT 473
Cdd:COG0068   395 -----------------------FELPPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVR 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 474 PELVVCDLHPGYATTAFAERFaAEHDIELLAVQHHFAHALSLLAEHRLlspnADRAVVATLDGTGYGTDGSIWGGEILTL 553
Cdd:COG0068   452 PEVIACDLHPDYLSTRLAEEL-AERGLPLIEVQHHHAHIAAVMAEHGL----DGPVLGIALDGTGYGDDGTIWGGEFLLG 526

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 554 SRssANWERTWHCPTFPLVGGDRAVTHPWRLALGLTHAWELDD--DHLLRNLSnEREVALVKSQLATGVGTVQTSSLGRI 631
Cdd:COG0068   527 DY--AGFERVGHLRPFPLPGGDKAAREPWRMALALLYEAGGEEllEPLLKRFS-EKELALLRQMLERGINSPLTSSAGRL 603

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 632 FDAAAALLLPRWRgggaISYEAQAAMELEAAATRYVRSHAEALGAVSSETKSEH-----LQEVIREAVASPDVEQAAFVF 706
Cdd:COG0068   604 FDAVAALLGICDE----ISYEGQAAMELEALADRAEEAEPYPFPLREIDGLLVLdwaplLRALLEDLQAGVPPAEIAARF 679

                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021001947 707 HSGVAGLVGKRLVQAAEKSGTDVVGVSGGCANNALLMELLRHEVATEGFTLLQHQIVPPGDGGLSLGQAVAGRL 780
Cdd:COG0068   680 HNTLAEAIAELALRLAERTGIDTVALSGGVFQNRLLLELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAA 753
hypF TIGR00143
[NiFe] hydrogenase maturation protein HypF; A previously described regulatory effect of HypF ...
 37-777 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: 680.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947  37 DEQGVFIEVEGtsDALAAFCSQLFTELPALARIINHSAEPVAVLGHEHEFTIVPSR-HSYSGRALLPPDTALCPDCRREF 115
Cdd:TIGR00143   1 TGDGVEIVLEA--DKEESFLNRLKKGLPPLARIEKIIIEPFDGAEHFTTFRIRESKnGGLSLLSIIPADVATCSDCLEEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 116 FDPTNPRYLYPFISCTNCGPRLSIITELPYDRPRTTMAAFPMCTPCEREYTDPTDRRYHAQPISCFDCGPRLSWHDAGDT 195
Cdd:TIGR00143  79 LDKNDRRYLYPFISCTHCGPRFTIIEALPYDRENTSMADFPLCPDCAKEYKDPLDRRFHAQPIACPRCGPQLNFVSRGGH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 196 TTAtsrEEVLalfRRAHALLDDGALLAVKGIGGFHLVCDATNDAACEKLRLRKRRPDKPLAVMAPTVDTAAQLVELTEQE 275
Cdd:TIGR00143 159 AEQ---DDAL---LEAAKLLKKGKIIAIKGIGGFHLACDARNDEVVERLRLRKNRPLKPFAVMSPDLESAEQHAELNNLE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 276 KRFLDSPEAPIVIAPKQRSGPLSNLIAPGLDSFGIMLPYSGIHLLLCDR---PLVVTSGNLSGEPVCTDNADALKKLGHI 352
Cdd:TIGR00143 233 CELLTSPAAPIVLLRKKPDIKLAPNIAPNLPTIGVMLPYTPLHHLLLQLlafPLVMTSANLPGLPMAIDNAEILDKLQGI 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 353 ADAFILHDREIHVPVEDSV--FIGTAPS--RRSRGFAPIPVSITATDsrshtstgpgsatgpgisvrctSQPTIFATGGE 428
Cdd:TIGR00143 313 ADGFLVHNRRIVNRVDDSVvqHVAGEILflRRSRGFAPQPLTLPPNG----------------------NPKKILALGAE 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 429 LKNTFAIAHGDLAHVSAHIGDMGSWASQKAYQRAVDQLLSMRDATPELVVCDLHPGYATTAFAERFAAEHdielLAVQHH 508
Cdd:TIGR00143 371 LKNTFSLLKGGQAYLSQHIGDLSVYETYKFFKEALNFFLRIYDFEPQDIVCDLHPQYNTTQYAEELSLPV----LRVQHH 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 509 FAHALSLLAEHRLLspnaDRAVVA-TLDGTGYGTDGSIWGGEIL--TLSRssanWERTWHCPTFPLVGGDRAVTHPWRLA 585
Cdd:TIGR00143 447 HAHALAVMADAGVL----EEAVIGiTWDGVGYGEDGKIWGGECLliDLGR----IERLGRLEEFWLLGGDLATKYPLRIL 518

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 586 LGLthAWELDDDHLLRNLSN----EREVALVKSQLATGVGTVQTSSLGRIFDAAAALLlprwRGGGAISYEAQAAMELEA 661
Cdd:TIGR00143 519 LSI--LLKHDLNDFLKRYQKyfkqEKELSVLQQALEKKINAPLTTSTGRLFDAVAAAL----GLCGERTYEGEAAIALEA 592

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 662 AATRyvrshaeALGAVSSE--------TKSEHLQEVIREAVASPDVEQAAFVFHSGVAGLVGKRLVQAAEKSGTDVVGVS 733
Cdd:TIGR00143 593 LALR-------SDGIANYPfeiknkvlDLKEFYQRFLEDLLVGEDRSKIAHIAHKFVASGLVEIATAIAVPFGIHKIVIS 665

                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....
gi 2021001947 734 GGCANNALLMELLRHEVATEGFTLLQHQIVPPGDGGLSLGQAVA 777
Cdd:TIGR00143 666 GGVFYNRLLLERLAKYLKGLGFQFLFHRHLPPGDGGISLGQAVA 709
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
 213-371 1.79e-50

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: 174.62  E-value: 1.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 213 ALLDDGALLAVKGIGGFHLVCDATNDAACEKLRLRKRRP-DKPLAVMAPTVDTAAQLVEltEQEKRFLDSPEA----PIV 287
Cdd:pfam01300   1 EALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPrDKPLAVMVADLEDLKEYAE--EVEEAALRLAERfwpgPLT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 288 IAPKQRSGPLSNLIAPGLDSFGIMLPYSGIHLLLCDR---PLVVTSGNLSGEPVCTDNADALKKLGHIADAFILHDReIH 364
Cdd:pfam01300  79 LVLKASKKPLPKLLTPGLGTVGVRLPDHPLALLLLEAlgePLVATSANLSGEPSPTDAEEILEELGGRVDLILDGGR-IA 157


                  ....*..
gi 2021001947 365 VPVEDSV 371
Cdd:pfam01300 158 GGVPSTV 164
PRK14435 PRK14435
acylphosphatase; Provisional
 1-88 3.88e-11

acylphosphatase; Provisional


Pssm-ID: 184681  Cd Length: 90  Bit Score: 59.92  E-value: 3.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGN-DEQGVFIEVEGTSDALAAFCSQLfTELPALARIINHSAEPVAV 79
Cdd:PRK14435    1 MKALKIRVEGIVQGVGFRYFTRRVAKSLGVKGYVMNmDDGSVFIHAEGDENALRRFLNEV-AKGPPAAVVTNVSVEETTP 79


                  ....*....
gi 2021001947  80 LGHEhEFTI 88
Cdd:PRK14435   80 EGYE-DFTI 87
ASKHA_NBD_MJ1051-like_N cd24100
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ...
 461-559 1.34e-04

N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and similar proteins; The family includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ1051 and protein MJ1058. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.


Pssm-ID: 466950 [Multi-domain]  Cd Length: 238  Bit Score: 44.00  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 461 RAVDQLLSMRDATPE---LVVcdlhpgYATTAFAERFaaeHDIEllavqHHFAHALSLLAehrlLSPNADRAVVATLDGT 537
Cdd:cd24100    42 RAIEEVLKLAGISPSdidAVA------VAGLFSKAKI---IFVD-----HHLAHAASAYY----TSPGFDDALVITLDGG 103

                          90       100
                  ....*....|....*....|....*
gi 2021001947 538 GYGTDGSIW---GGEILTLSRSSAN 559
Cdd:cd24100   104 GDGLSGTVSigeGGKLERLATSPAL 128
 
Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 1-780 0e+00

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


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1016.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQGVFIEVEGTSDALAAFCSQLFTELPALARIINHSAEPVAVL 80
Cdd:COG0068     1 MKRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEEALEAFLEALRAEAPPLARIDSIEVEELPPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947  81 GhEHEFTIVPSRHSYSGRALLPPDTALCPDCRREFFDPTNPRYLYPFISCTNCGPRLSIITELPYDRPRTTMAAFPMCTP 160
Cdd:COG0068    81 G-FDGFRILESEAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 161 CEREYTDPTDRRYHAQPISCFDCGPRLSWHDAGDTTTATSREEVlalfRRAHALLDDGALLAVKGIGGFHLVCDATNDAA 240
Cdd:COG0068   160 CAAEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEGDDAI----AAAAELLRAGKIVAIKGLGGFHLACDATNEEA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 241 CEKLRLRKRRPDKPLAVMAPTVDTAAQLVELTEQEKRFLDSPEAPIVIAPKQRSGPLSNLIAPGLDSFGIMLPYSGIHLL 320
Cdd:COG0068   236 VARLRRRKRRPAKPFAVMARDLETARRLCEVSEAEEALLTSPARPIVLLPKRPDSPLAPSVAPGLDTLGVMLPYTPLHHL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 321 LCD---RPLVVTSGNLSGEPVCTDNADALKKLGHIADAFILHDREIHVPVEDSV--FIGTAPS--RRSRGFAPIPVSITa 393
Cdd:COG0068   316 LLDelgRPLVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVvrVIDGKPRflRRARGYAPLPIPLP- 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 394 tdsrshtstgpgsatgpgisvrcTSQPTIFATGGELKNTFAIAHGDLAHVSAHIGDMGSWASQKAYQRAVDQLLSMRDAT 473
Cdd:COG0068   395 -----------------------FELPPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVR 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 474 PELVVCDLHPGYATTAFAERFaAEHDIELLAVQHHFAHALSLLAEHRLlspnADRAVVATLDGTGYGTDGSIWGGEILTL 553
Cdd:COG0068   452 PEVIACDLHPDYLSTRLAEEL-AERGLPLIEVQHHHAHIAAVMAEHGL----DGPVLGIALDGTGYGDDGTIWGGEFLLG 526

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 554 SRssANWERTWHCPTFPLVGGDRAVTHPWRLALGLTHAWELDD--DHLLRNLSnEREVALVKSQLATGVGTVQTSSLGRI 631
Cdd:COG0068   527 DY--AGFERVGHLRPFPLPGGDKAAREPWRMALALLYEAGGEEllEPLLKRFS-EKELALLRQMLERGINSPLTSSAGRL 603

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 632 FDAAAALLLPRWRgggaISYEAQAAMELEAAATRYVRSHAEALGAVSSETKSEH-----LQEVIREAVASPDVEQAAFVF 706
Cdd:COG0068   604 FDAVAALLGICDE----ISYEGQAAMELEALADRAEEAEPYPFPLREIDGLLVLdwaplLRALLEDLQAGVPPAEIAARF 679

                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021001947 707 HSGVAGLVGKRLVQAAEKSGTDVVGVSGGCANNALLMELLRHEVATEGFTLLQHQIVPPGDGGLSLGQAVAGRL 780
Cdd:COG0068   680 HNTLAEAIAELALRLAERTGIDTVALSGGVFQNRLLLELLRARLEAAGFKVLLHRQVPPNDGGISLGQAAIAAA 753
hypF TIGR00143
[NiFe] hydrogenase maturation protein HypF; A previously described regulatory effect of HypF ...
 37-777 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: 680.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947  37 DEQGVFIEVEGtsDALAAFCSQLFTELPALARIINHSAEPVAVLGHEHEFTIVPSR-HSYSGRALLPPDTALCPDCRREF 115
Cdd:TIGR00143   1 TGDGVEIVLEA--DKEESFLNRLKKGLPPLARIEKIIIEPFDGAEHFTTFRIRESKnGGLSLLSIIPADVATCSDCLEEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 116 FDPTNPRYLYPFISCTNCGPRLSIITELPYDRPRTTMAAFPMCTPCEREYTDPTDRRYHAQPISCFDCGPRLSWHDAGDT 195
Cdd:TIGR00143  79 LDKNDRRYLYPFISCTHCGPRFTIIEALPYDRENTSMADFPLCPDCAKEYKDPLDRRFHAQPIACPRCGPQLNFVSRGGH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 196 TTAtsrEEVLalfRRAHALLDDGALLAVKGIGGFHLVCDATNDAACEKLRLRKRRPDKPLAVMAPTVDTAAQLVELTEQE 275
Cdd:TIGR00143 159 AEQ---DDAL---LEAAKLLKKGKIIAIKGIGGFHLACDARNDEVVERLRLRKNRPLKPFAVMSPDLESAEQHAELNNLE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 276 KRFLDSPEAPIVIAPKQRSGPLSNLIAPGLDSFGIMLPYSGIHLLLCDR---PLVVTSGNLSGEPVCTDNADALKKLGHI 352
Cdd:TIGR00143 233 CELLTSPAAPIVLLRKKPDIKLAPNIAPNLPTIGVMLPYTPLHHLLLQLlafPLVMTSANLPGLPMAIDNAEILDKLQGI 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 353 ADAFILHDREIHVPVEDSV--FIGTAPS--RRSRGFAPIPVSITATDsrshtstgpgsatgpgisvrctSQPTIFATGGE 428
Cdd:TIGR00143 313 ADGFLVHNRRIVNRVDDSVvqHVAGEILflRRSRGFAPQPLTLPPNG----------------------NPKKILALGAE 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 429 LKNTFAIAHGDLAHVSAHIGDMGSWASQKAYQRAVDQLLSMRDATPELVVCDLHPGYATTAFAERFAAEHdielLAVQHH 508
Cdd:TIGR00143 371 LKNTFSLLKGGQAYLSQHIGDLSVYETYKFFKEALNFFLRIYDFEPQDIVCDLHPQYNTTQYAEELSLPV----LRVQHH 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 509 FAHALSLLAEHRLLspnaDRAVVA-TLDGTGYGTDGSIWGGEIL--TLSRssanWERTWHCPTFPLVGGDRAVTHPWRLA 585
Cdd:TIGR00143 447 HAHALAVMADAGVL----EEAVIGiTWDGVGYGEDGKIWGGECLliDLGR----IERLGRLEEFWLLGGDLATKYPLRIL 518

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 586 LGLthAWELDDDHLLRNLSN----EREVALVKSQLATGVGTVQTSSLGRIFDAAAALLlprwRGGGAISYEAQAAMELEA 661
Cdd:TIGR00143 519 LSI--LLKHDLNDFLKRYQKyfkqEKELSVLQQALEKKINAPLTTSTGRLFDAVAAAL----GLCGERTYEGEAAIALEA 592

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 662 AATRyvrshaeALGAVSSE--------TKSEHLQEVIREAVASPDVEQAAFVFHSGVAGLVGKRLVQAAEKSGTDVVGVS 733
Cdd:TIGR00143 593 LALR-------SDGIANYPfeiknkvlDLKEFYQRFLEDLLVGEDRSKIAHIAHKFVASGLVEIATAIAVPFGIHKIVIS 665

                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....
gi 2021001947 734 GGCANNALLMELLRHEVATEGFTLLQHQIVPPGDGGLSLGQAVA 777
Cdd:TIGR00143 666 GGVFYNRLLLERLAKYLKGLGFQFLFHRHLPPGDGGISLGQAVA 709
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
 213-371 1.79e-50

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: 174.62  E-value: 1.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 213 ALLDDGALLAVKGIGGFHLVCDATNDAACEKLRLRKRRP-DKPLAVMAPTVDTAAQLVEltEQEKRFLDSPEA----PIV 287
Cdd:pfam01300   1 EALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPrDKPLAVMVADLEDLKEYAE--EVEEAALRLAERfwpgPLT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 288 IAPKQRSGPLSNLIAPGLDSFGIMLPYSGIHLLLCDR---PLVVTSGNLSGEPVCTDNADALKKLGHIADAFILHDReIH 364
Cdd:pfam01300  79 LVLKASKKPLPKLLTPGLGTVGVRLPDHPLALLLLEAlgePLVATSANLSGEPSPTDAEEILEELGGRVDLILDGGR-IA 157


                  ....*..
gi 2021001947 365 VPVEDSV 371
Cdd:pfam01300 158 GGVPSTV 164
HypF_C pfam17788
HypF Kae1-like domain; This domain is found in the HypF protein. In the structure it is one of ...
 417-518 3.60e-39

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: 139.92  E-value: 3.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 417 TSQPTIFATGGELKNTFAIAHGDLAHVSAHIGDMGSWASQKAYQRAVDQLLSMRDATPELVVCDLHPGYATTAFAERFaa 496
Cdd:pfam17788   1 KAKPPVLALGAELKNTFALAKGGQAFLSQHIGDLDNLETLEAFEETLEHLLRLYGIKPEVIACDLHPDYLSTRLAEEL-- 78

                          90       100
                  ....*....|....*....|..
gi 2021001947 497 eHDIELLAVQHHFAHALSLLAE 518
Cdd:pfam17788  79 -NGLPLIEVQHHHAHIAAVMAE 99
Acylphosphatase pfam00708
Acylphosphatase;
7-88 1.15e-18

Acylphosphatase;


Pssm-ID: 425830  Cd Length: 85  Bit Score: 81.09  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   7 RIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTSDALAAFCSQLFTELPAlARIINHSAEPVAVLGHEHE 85
Cdd:pfam00708   4 LVTGRVQGVGFRPFVYRLAKELGLKGWVRNLPDGsVEIVVQGPEEDVDKFLEWLKSGPPP-ARVDKVEVTEIDEPGDFSG 82


                  ...
gi 2021001947  86 FTI 88
Cdd:pfam00708  83 FEI 85
zf-HYPF pfam07503
HypF finger; The HypF family of proteins are involved in the maturation and regulation of ...
 108-140 4.04e-18

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: 77.78  E-value: 4.04e-18
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2021001947 108 CPDCRREFFDPTNPRYLYPFISCTNCGPRLSII 140
Cdd:pfam07503   1 CPDCLREYFDPLDRRFHAQFIACTNCGPRLSLI 33
AcyP COG1254
Acylphosphatase [Energy production and conversion];
1-89 5.14e-18

Acylphosphatase [Energy production and conversion];


Pssm-ID: 440866  Cd Length: 89  Bit Score: 79.43  E-value: 5.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTSDALAAFCSQLFTElPALARIINHSAEPVAV 79
Cdd:COG1254     1 MKRVRIIVSGRVQGVGFRAFTRRQARRLGLTGWVRNLPDGsVEVVAEGEEEAVEAFLEWLRKG-PPAARVEDVEVEEEEP 79

                          90
                  ....*....|
gi 2021001947  80 LGHEHEFTIV 89
Cdd:COG1254    80 TGEFEGFEIR 89
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
 206-357 1.88e-16

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: 78.60  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 206 ALFRRAHALLDDGALLA-----VKGIGgfhlvCDATNDAACEKL-RLRKRRPDKPLAVMAPTVDTAAQLV-ELTEQEKRF 278
Cdd:COG0009    10 RLIEQAAEALRAGGVVAyptdtVYGLG-----CDALNKEAVERIfAIKGRPRDKPLIVLVADLSQLEEYAkEVPDAARRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 279 LDS--PeAPI-VIAPKQRSgpLSNLIAPGLDSFGIMLPYSGIHLLLC---DRPLVVTSGNLSGEPVCTDNADALKKLGHI 352
Cdd:COG0009    85 AKAfwP-GPLtLILPATKE--VPDLLTGGRDTVAVRVPDHPVALALLralGPPLASTSANLSGEPPPTTAEEVREQLGDR 161


                  ....*
gi 2021001947 353 ADAFI 357
Cdd:COG0009   162 VDLIL 166
zf-HYPF pfam07503
HypF finger; The HypF family of proteins are involved in the maturation and regulation of ...
 158-189 3.58e-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: 72.38  E-value: 3.58e-16
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2021001947 158 CTPCEREYTDPTDRRYHAQPISCFDCGPRLSW 189
Cdd:pfam07503   1 CPDCLREYFDPLDRRFHAQFIACTNCGPRLSL 32
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
 196-357 2.78e-14

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: 72.36  E-value: 2.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 196 TTATSREEVLAlfrRAHALLDDGALLA-----VKGIGgfhlvCDATNDAACEKLRLRKRRP-DKPLAVMAPTVDTAAQLV 269
Cdd:TIGR00057   2 HPENPSQRGIE---QAVKILRKGGIVVyptdtVYGIG-----ADALDEDAVRRLYRIKGRPsNKPLTVLVSDLSEIEKYA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 270 ELTEQEKRFLD--SPEAPIVIAPKqrSGPLSNLIAPGLDSFGIMLPYSGIHL-LLCD--RPLVVTSGNLSGEPVCTDNAD 344
Cdd:TIGR00057  74 YVPDDAKRLMKkfWPGPLTLVLKK--TPEIPRRVSGKRKTIGIRVPDNPIALeLLEElgKPIVATSANLSGKPSATDVEE 151

                         170
                  ....*....|...
gi 2021001947 345 ALKKLGHIADAFI 357
Cdd:TIGR00057 152 AVDELGKLVDLII 164
PRK14435 PRK14435
acylphosphatase; Provisional
 1-88 3.88e-11

acylphosphatase; Provisional


Pssm-ID: 184681  Cd Length: 90  Bit Score: 59.92  E-value: 3.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGN-DEQGVFIEVEGTSDALAAFCSQLfTELPALARIINHSAEPVAV 79
Cdd:PRK14435    1 MKALKIRVEGIVQGVGFRYFTRRVAKSLGVKGYVMNmDDGSVFIHAEGDENALRRFLNEV-AKGPPAAVVTNVSVEETTP 79


                  ....*....
gi 2021001947  80 LGHEhEFTI 88
Cdd:PRK14435   80 EGYE-DFTI 87
PRK14420 PRK14420
acylphosphatase; Provisional
 1-89 2.35e-09

acylphosphatase; Provisional


Pssm-ID: 237710  Cd Length: 91  Bit Score: 54.81  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTSDALAAFCSQLFTELPaLARIINHSAEPVAV 79
Cdd:PRK14420    1 MLQYHIIVDGRVQGVGFRYFVQMEADKRKLTGWVKNRDDGtVEIEAEGPEEALQLFLDAIEKGSP-FSKVTDVHIEERDV 79

                          90
                  ....*....|
gi 2021001947  80 LGHEHEFTIV 89
Cdd:PRK14420   80 LSGEKQFRIM 89
PRK14428 PRK14428
acylphosphatase; Provisional
 8-59 6.15e-07

acylphosphatase; Provisional


Pssm-ID: 172904  Cd Length: 97  Bit Score: 48.20  E-value: 6.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2021001947   8 IEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTSDALAAFCSQL 59
Cdd:PRK14428   14 VTGLVQGVGFRYFTVTQARRLGVQGWVRNCRDGsVELEAQGSSDAVQALVEQL 66
PRK14440 PRK14440
acylphosphatase; Provisional
 1-69 2.24e-06

acylphosphatase; Provisional


Pssm-ID: 172916  Cd Length: 90  Bit Score: 46.35  E-value: 2.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTSDALAAFCSQLfTELPALARI 69
Cdd:PRK14440    2 LKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGsVEVVAEGYEEALSKLLERI-KQGPPAAEV 70
PRK14431 PRK14431
acylphosphatase; Provisional
 1-55 3.02e-06

acylphosphatase; Provisional


Pssm-ID: 184677  Cd Length: 89  Bit Score: 45.95  E-value: 3.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQGVFIEVEGTSDALAAF 55
Cdd:PRK14431    1 MRHIHLQVFGRVQGVGFRYFTQRIAMNYNIVGTVQNVDDYVEIYAQGDDADLERF 55
PRK14448 PRK14448
acylphosphatase; Provisional
 1-93 3.41e-06

acylphosphatase; Provisional


Pssm-ID: 172924  Cd Length: 90  Bit Score: 45.91  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTSDALAAFCSQLfTELPALARIINHSAEPVAv 79
Cdd:PRK14448    1 MLKKQFIVYGHVQGVGFRYFTWQEATKIGIKGYVKNRPDGsVEVVAVGSDAQIAAFRDWL-QHGPPTAVVCNVIEQDYQ- 78

                          90
                  ....*....|....
gi 2021001947  80 lgHEHEFTIVPSRH 93
Cdd:PRK14448   79 --GSRQFTHFSVRR 90
PRK14452 PRK14452
acylphosphatase; Provisional
 2-58 8.02e-06

acylphosphatase; Provisional


Pssm-ID: 237716  Cd Length: 107  Bit Score: 45.22  E-value: 8.02e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021001947   2 QRIRWRIEGIVQGVGFRpfvATIARRA---GLVGFCGNDEQG-VFIEVEGTSDALA---AFCSQ 58
Cdd:PRK14452   20 ERWRFLIEGRVQGVGFR---ASCCRRAldlGLSGWVRNLSDGsVEVQAEGPPLALSelrAWCER 80
PRK14450 PRK14450
acylphosphatase; Provisional
 1-64 8.57e-06

acylphosphatase; Provisional


Pssm-ID: 184683  Cd Length: 91  Bit Score: 44.84  E-value: 8.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQGVFIEV--EGTSDALAAFCSQLFTELP 64
Cdd:PRK14450    1 MHCLKAIVKGKVQGVYFRDFTRTQATRLGLCGYAKNLANGNEVEVvaEGDKDSLLEFLDLLRSGPP 66
PRK14429 PRK14429
acylphosphatase; Provisional
 1-58 2.09e-05

acylphosphatase; Provisional


Pssm-ID: 184676  Cd Length: 90  Bit Score: 43.56  E-value: 2.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTS---DALAAFCSQ 58
Cdd:PRK14429    1 MKRVLIKLTGKVQGVGCRRATLTKARALGVTGYVTNCEDGsVEILAQGSDpavDNLIAWCEV 62
ASKHA_NBD_MJ1051-like_N cd24100
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ...
 461-559 1.34e-04

N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and similar proteins; The family includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ1051 and protein MJ1058. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.


Pssm-ID: 466950 [Multi-domain]  Cd Length: 238  Bit Score: 44.00  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947 461 RAVDQLLSMRDATPE---LVVcdlhpgYATTAFAERFaaeHDIEllavqHHFAHALSLLAehrlLSPNADRAVVATLDGT 537
Cdd:cd24100    42 RAIEEVLKLAGISPSdidAVA------VAGLFSKAKI---IFVD-----HHLAHAASAYY----TSPGFDDALVITLDGG 103

                          90       100
                  ....*....|....*....|....*
gi 2021001947 538 GYGTDGSIW---GGEILTLSRSSAN 559
Cdd:cd24100   104 GDGLSGTVSigeGGKLERLATSPAL 128
PRK14426 PRK14426
acylphosphatase; Provisional
 8-77 4.70e-04

acylphosphatase; Provisional


Pssm-ID: 184675  Cd Length: 92  Bit Score: 40.01  E-value: 4.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021001947   8 IEGIVQGVGFRPFVATIARRAGLVGFCGNDEQGvfiEVE----GTSDALAAFCSQLFTELPALARIINHSAEPV 77
Cdd:PRK14426   10 VYGRVQGVGFRYHTQHEALKLGLTGYAKNLDDG---SVEvvacGEEEQVEKLMEWLKEGGPRSARVDRVLTEPH 80
PRK14421 PRK14421
acylphosphatase; Provisional
 8-79 5.21e-04

acylphosphatase; Provisional


Pssm-ID: 237711 [Multi-domain]  Cd Length: 99  Bit Score: 39.79  E-value: 5.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2021001947   8 IEGIVQGVGFRPFVATIARRAGLVGFCGNDEQGvfiEVE----GTSDALAAFCSQLFTElPALARIINHSAEPVAV 79
Cdd:PRK14421   10 IRGRVQGVGYRAWVARTAEALGLEGWVRNRRDG---SVEalfaGPADAVAEMIARCRRG-PSAARVDAVEDEPAAP 81
PRK14445 PRK14445
acylphosphatase; Provisional
 2-52 6.37e-04

acylphosphatase; Provisional


Pssm-ID: 172921  Cd Length: 91  Bit Score: 39.44  E-value: 6.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2021001947   2 QRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTSDAL 52
Cdd:PRK14445    4 KRVHLIVSGLVQGVGFRMFIDRAASELNLSGWVRNLPDGtVEIEAQGSSGMI 55
PRK14427 PRK14427
acylphosphatase; Provisional
 3-55 1.28e-03

acylphosphatase; Provisional


Pssm-ID: 172903  Cd Length: 94  Bit Score: 38.70  E-value: 1.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2021001947   3 RIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTSDALAAF 55
Cdd:PRK14427    7 RLSARVFGVVQGVGFRYWTMRKAEELGLTGTVRNLDDGsVALVAEGTGEQVEKL 60
PRK14433 PRK14433
acylphosphatase; Provisional
 3-69 3.14e-03

acylphosphatase; Provisional


Pssm-ID: 184679  Cd Length: 87  Bit Score: 37.48  E-value: 3.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2021001947   3 RIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTSDALAAFCSQLfTELPALARI 69
Cdd:PRK14433    2 RLTALVSGRVQGVGYRAFVQKKARELGLSGYAENLSDGrVEVVAEGPKEALERLLHWL-RRGPRHARV 68
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 499-549 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
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2021001947 499 DIELLAVQHHFAHALSLLaehrLLSPNaDRAVVATLDGTGYGTDGSIWGGE 549
Cdd:cd24033   100 EVPIYYVDHHLAHAASAF----YTSPF-EEALVLVIDGGGDDESFSIYYGD 145
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 720-779 4.57e-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: 4.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2021001947 720 QAAEKSGTDVVGVSGGCANNALL-MELLRHevategfTLLQHQIVPP--GDGGLSLGQAVAGR 779
Cdd:cd24033   211 KLLERTGSDNLCLSGGCALNCVAnSKLAEE-------GLFKNVFVPPapGDSGLSLGAALYVY 266
PRK14432 PRK14432
acylphosphatase; Provisional
 1-40 4.83e-03

acylphosphatase; Provisional


Pssm-ID: 184678  Cd Length: 93  Bit Score: 37.19  E-value: 4.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG 40
Cdd:PRK14432    1 MYKQQYFISGKVQGVGFRFFTEQIANNMKLKGFVKNLNDG 40
PRK14444 PRK14444
acylphosphatase; Provisional
 1-89 7.15e-03

acylphosphatase; Provisional


Pssm-ID: 172920  Cd Length: 92  Bit Score: 36.40  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021001947   1 MQRIRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQGVFIEV-EGTSDALAAFCSQLFTElPALARIIN---HSAEP 76
Cdd:PRK14444    3 MVRAHVFISGRVQGVNFRAYTRDRAREAGVKGWVRNLSDGRVEAVfEGSRPAVQKMISWCYSG-PSHARVERvevHWEEP 81

                          90
                  ....*....|...
gi 2021001947  77 VavlGHEHEFTIV 89
Cdd:PRK14444   82 T---GEERTFTIV 91
PRK14425 PRK14425
acylphosphatase; Provisional
 4-59 8.73e-03

acylphosphatase; Provisional


Pssm-ID: 172901  Cd Length: 94  Bit Score: 36.37  E-value: 8.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2021001947   4 IRWRIEGIVQGVGFRPFVATIARRAGLVGFCGNDEQG-VFIEVEGTSDALAAFCSQL 59
Cdd:PRK14425    8 VRVRITGRVQGVGFRDWTRDEAERLGLTGWVRNESDGsVTALIAGPDSAISAMIERF 64
 
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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