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Conserved domains on  [gi|2238915327|ref|WP_249246164|]
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carbamoyltransferase HypF [Brenneria tiliae]

Protein Classification

carbamoyltransferase HypF( domain architecture ID 11414624)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 3-772 0e+00

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


:

Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1135.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   3 KNGIQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAGVLIYLYQSE-NIEGFIEALSAGCPPLAHIDSITRQPWRWT 81
Cdd:COG0068     1 MKRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEeALEAFLEALRAEAPPLARIDSIEVEELPPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  82 AiPTAFVIEHS-GAGRMDTQVVPDAATCEACRRELNDPANRRYRYPFINCTHCGPRFTIIRRMPYDRPFTSMADFPLCPQ 160
Cdd:COG0068    81 G-FDGFRILESeAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 161 CLDEYRQPADRRFHAQPNACPQCGPQVWLENAASQRLAAGEDAIRQAAGALRAGKIVAIKGIGGFHLACDATNTQAVQRL 240
Cdd:COG0068   160 CAAEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEGDDAIAAAAELLRAGKIVAIKGLGGFHLACDATNEEAVARL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 241 RQRKHRPGKPLAVMAPDAAWLERCAAVDdmPAALRLLQSAAAPIVLLPWREDGPLSASVAPGLSEVGLMLPANPLQHLLL 320
Cdd:COG0068   240 RRRKRRPAKPFAVMARDLETARRLCEVS--EAEEALLTSPARPIVLLPKRPDSPLAPSVAPGLDTLGVMLPYTPLHHLLL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 321 AQVNLPLVMTSGNASGKPPALSNAQATEQLGAIADRWLMHNRDIVQRADDSLVRLRHQGLFksgaeMLRRARGYVPDALP 400
Cdd:COG0068   318 DELGRPLVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVVRVIDGKPR-----FLRRARGYAPLPIP 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 401 LPPGFagqPALLALGADLKNTFCLLRDENAVVSQHLGDLEDSDVERQYQQSIDLFEDIYRFTPGALAVDAHPGYISHRLG 480
Cdd:COG0068   393 LPFEL---PPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLSTRLA 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 481 KRLAEqRQIPCIEVLHHHAHIVSCLAEHQWprdAGPVIGLALDGIGYGADGQWWGGECLLADYAQCRHLGGLPTVALPGG 560
Cdd:COG0068   470 EELAE-RGLPLIEVQHHHAHIAAVMAEHGL---DGPVLGIALDGTGYGDDGTIWGGEFLLGDYAGFERVGHLRPFPLPGG 545

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 561 DLAARQPWRNLLAQWLRFVPDWQSLPQAAAIPASSAALLSRAIARGINAPPASSAGRLFDAVAAATGFPHEaQSWEGEAA 640
Cdd:COG0068   546 DKAAREPWRMALALLYEAGGEELLEPLLKRFSEKELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDE-ISYEGQAA 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 641 CWLESLAWRSERfqrqraqwRPPVALPVLADG---RLDLATFWRQWLDYRAA---PADRAYAFHYALAQGFGALARRTAR 714
Cdd:COG0068   625 MELEALADRAEE--------AEPYPFPLREIDgllVLDWAPLLRALLEDLQAgvpPAEIAARFHNTLAEAIAELALRLAE 696

                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 715 RHGIHTVALSGGVMHNRLLSVLLHQQL--SGLTVLQPQRLPAGDGGLSLGQALIAAAQLS 772
Cdd:COG0068   697 RTGIDTVALSGGVFQNRLLLELLRARLeaAGFKVLLHRQVPPNDGGISLGQAAIAAARLE 756
 
Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 3-772 0e+00

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


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1135.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   3 KNGIQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAGVLIYLYQSE-NIEGFIEALSAGCPPLAHIDSITRQPWRWT 81
Cdd:COG0068     1 MKRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEeALEAFLEALRAEAPPLARIDSIEVEELPPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  82 AiPTAFVIEHS-GAGRMDTQVVPDAATCEACRRELNDPANRRYRYPFINCTHCGPRFTIIRRMPYDRPFTSMADFPLCPQ 160
Cdd:COG0068    81 G-FDGFRILESeAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 161 CLDEYRQPADRRFHAQPNACPQCGPQVWLENAASQRLAAGEDAIRQAAGALRAGKIVAIKGIGGFHLACDATNTQAVQRL 240
Cdd:COG0068   160 CAAEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEGDDAIAAAAELLRAGKIVAIKGLGGFHLACDATNEEAVARL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 241 RQRKHRPGKPLAVMAPDAAWLERCAAVDdmPAALRLLQSAAAPIVLLPWREDGPLSASVAPGLSEVGLMLPANPLQHLLL 320
Cdd:COG0068   240 RRRKRRPAKPFAVMARDLETARRLCEVS--EAEEALLTSPARPIVLLPKRPDSPLAPSVAPGLDTLGVMLPYTPLHHLLL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 321 AQVNLPLVMTSGNASGKPPALSNAQATEQLGAIADRWLMHNRDIVQRADDSLVRLRHQGLFksgaeMLRRARGYVPDALP 400
Cdd:COG0068   318 DELGRPLVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVVRVIDGKPR-----FLRRARGYAPLPIP 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 401 LPPGFagqPALLALGADLKNTFCLLRDENAVVSQHLGDLEDSDVERQYQQSIDLFEDIYRFTPGALAVDAHPGYISHRLG 480
Cdd:COG0068   393 LPFEL---PPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLSTRLA 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 481 KRLAEqRQIPCIEVLHHHAHIVSCLAEHQWprdAGPVIGLALDGIGYGADGQWWGGECLLADYAQCRHLGGLPTVALPGG 560
Cdd:COG0068   470 EELAE-RGLPLIEVQHHHAHIAAVMAEHGL---DGPVLGIALDGTGYGDDGTIWGGEFLLGDYAGFERVGHLRPFPLPGG 545

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 561 DLAARQPWRNLLAQWLRFVPDWQSLPQAAAIPASSAALLSRAIARGINAPPASSAGRLFDAVAAATGFPHEaQSWEGEAA 640
Cdd:COG0068   546 DKAAREPWRMALALLYEAGGEELLEPLLKRFSEKELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDE-ISYEGQAA 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 641 CWLESLAWRSERfqrqraqwRPPVALPVLADG---RLDLATFWRQWLDYRAA---PADRAYAFHYALAQGFGALARRTAR 714
Cdd:COG0068   625 MELEALADRAEE--------AEPYPFPLREIDgllVLDWAPLLRALLEDLQAgvpPAEIAARFHNTLAEAIAELALRLAE 696

                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 715 RHGIHTVALSGGVMHNRLLSVLLHQQL--SGLTVLQPQRLPAGDGGLSLGQALIAAAQLS 772
Cdd:COG0068   697 RTGIDTVALSGGVFQNRLLLELLRARLeaAGFKVLLHRQVPPNDGGISLGQAAIAAARLE 756
hypF TIGR00143
[NiFe] hydrogenase maturation protein HypF; A previously described regulatory effect of HypF ...
 39-768 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: 804.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  39 DGAGVLIYLYQSENiEGFIEALSAGCPPLAHIDSITRQPWRWTAIPTAF-VIEHSGAGRMDTQVVP-DAATCEACRRELN 116
Cdd:TIGR00143   1 TGDGVEIVLEADKE-ESFLNRLKKGLPPLARIEKIIIEPFDGAEHFTTFrIRESKNGGLSLLSIIPaDVATCSDCLEEML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 117 DPANRRYRYPFINCTHCGPRFTIIRRMPYDRPFTSMADFPLCPQCLDEYRQPADRRFHAQPNACPQCGPQvwLENAASQR 196
Cdd:TIGR00143  80 DKNDRRYLYPFISCTHCGPRFTIIEALPYDRENTSMADFPLCPDCAKEYKDPLDRRFHAQPIACPRCGPQ--LNFVSRGG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 197 LAAGEDAIRQAAGALRAGKIVAIKGIGGFHLACDATNTQAVQRLRQRKHRPGKPLAVMAPDAAWLERCAAVDDMPAAlrL 276
Cdd:TIGR00143 158 HAEQDDALLEAAKLLKKGKIIAIKGIGGFHLACDARNDEVVERLRLRKNRPLKPFAVMSPDLESAEQHAELNNLECE--L 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 277 LQSAAAPIVLLPWREDGPLSASVAPGLSEVGLMLPANPLQHLLLAQVNLPLVMTSGNASGKPPALSNAQATEQLGAIADR 356
Cdd:TIGR00143 236 LTSPAAPIVLLRKKPDIKLAPNIAPNLPTIGVMLPYTPLHHLLLQLLAFPLVMTSANLPGLPMAIDNAEILDKLQGIADG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 357 WLMHNRDIVQRADDSLVRlrhqglFKSGA-EMLRRARGYVPDALPLPPgFAGQPALLALGADLKNTFCLLRDENAVVSQH 435
Cdd:TIGR00143 316 FLVHNRRIVNRVDDSVVQ------HVAGEiLFLRRSRGFAPQPLTLPP-NGNPKKILALGAELKNTFSLLKGGQAYLSQH 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 436 LGDLEDSDVERQYQQSIDLFEDIYRFTPGALAVDAHPGYISHrlgkRLAEQRQIPCIEVLHHHAHIVSCLAEHQWprDAG 515
Cdd:TIGR00143 389 IGDLSVYETYKFFKEALNFFLRIYDFEPQDIVCDLHPQYNTT----QYAEELSLPVLRVQHHHAHALAVMADAGV--LEE 462

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 516 PVIGLALDGIGYGADGQWWGGECLLADYAQCRHLGGLPTVALPGGDLAARQPWRNLLAQWLR-----FVPDWQSLpqaaA 590
Cdd:TIGR00143 463 AVIGITWDGVGYGEDGKIWGGECLLIDLGRIERLGRLEEFWLLGGDLATKYPLRILLSILLKhdlndFLKRYQKY----F 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 591 IPASSAALLSRAIARGINAPPASSAGRLFDAVAAATGFPHEaQSWEGEAACWLESLAWRSErfqrqrAQWRPPVALPvla 670
Cdd:TIGR00143 539 KQEKELSVLQQALEKKINAPLTTSTGRLFDAVAAALGLCGE-RTYEGEAAIALEALALRSD------GIANYPFEIK--- 608

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 671 DGRLDLATFWRQWLDYRAAPADR---AYAFHYALAQGFGALARRTARRHGIHTVALSGGVMHNRLLSVLLHQQLSGL--T 745
Cdd:TIGR00143 609 NKVLDLKEFYQRFLEDLLVGEDRskiAHIAHKFVASGLVEIATAIAVPFGIHKIVISGGVFYNRLLLERLAKYLKGLgfQ 688

                         730       740
                  ....*....|....*....|...
gi 2238915327 746 VLQPQRLPAGDGGLSLGQALIAA 768
Cdd:TIGR00143 689 FLFHRHLPPGDGGISLGQAVAAA 711
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
 210-375 5.17e-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: 173.08  E-value: 5.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 210 ALRAGKIVAIKGIGGFHLACDATNTQAVQRLRQRKHRP-GKPLAVMAPDAAWLERCAAVDDmPAALRLLQSA-AAPIVLL 287
Cdd:pfam01300   2 ALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPrDKPLAVMVADLEDLKEYAEEVE-EAALRLAERFwPGPLTLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 288 PWREDGPLSASVAPGLSEVGLMLPANPLQHLLLAQVNLPLVMTSGNASGKPPALSNAQATEQLGAIADRWLMHNRdIVQR 367
Cdd:pfam01300  81 LKASKKPLPKLLTPGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDGGR-IAGG 159


                  ....*...
gi 2238915327 368 ADDSLVRL 375
Cdd:pfam01300 160 VPSTVVDL 167
PRK14426 PRK14426
acylphosphatase; Provisional
 1-89 2.76e-11

acylphosphatase; Provisional


Pssm-ID: 184675  Cd Length: 92  Bit Score: 60.42  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   1 MGKNGIQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGVLIYLYQSENIEGFIEALSAGCPPLAHIDSITRQPW 78
Cdd:PRK14426    1 MSKVCIIAWVYGRVQGVGFRYHTQHEALKLGLTGYAKNldDGSVEVVACGEEEQVEKLMEWLKEGGPRSARVDRVLTEPH 80

                          90
                  ....*....|.
gi 2238915327  79 RWTAIPTAFVI 89
Cdd:PRK14426   81 SPRGELTGFSI 91
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 691-770 2.06e-05

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: 46.91  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 691 ADRAYAFHYALAQGFGALARRTARRHGIHTVALSGGVMHNRLLSVLLHQQLSGLTVLQPqrlPA-GDGGLSLGQALIAAA 769
Cdd:cd24033   191 ADLAATVQKVFEEALLELIKKLLERTGSDNLCLSGGCALNCVANSKLAEEGLFKNVFVP---PApGDSGLSLGAALYVYH 267


                  .
gi 2238915327 770 Q 770
Cdd:cd24033   268 Q 268
 
Name Accession Description Interval E-value
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 3-772 0e+00

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


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 1135.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   3 KNGIQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAGVLIYLYQSE-NIEGFIEALSAGCPPLAHIDSITRQPWRWT 81
Cdd:COG0068     1 MKRLRIRVRGIVQGVGFRPFVYRLAKELGLKGWVRNDGGGVEIEVEGEEeALEAFLEALRAEAPPLARIDSIEVEELPPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  82 AiPTAFVIEHS-GAGRMDTQVVPDAATCEACRRELNDPANRRYRYPFINCTHCGPRFTIIRRMPYDRPFTSMADFPLCPQ 160
Cdd:COG0068    81 G-FDGFRILESeAGGGGRTLIPPDLATCDDCLRELFDPADRRYRYPFINCTNCGPRYTIIRALPYDRPNTSMAAFPMCPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 161 CLDEYRQPADRRFHAQPNACPQCGPQVWLENAASQRLAAGEDAIRQAAGALRAGKIVAIKGIGGFHLACDATNTQAVQRL 240
Cdd:COG0068   160 CAAEYEDPADRRFHAQPNACPVCGPQLWLLDADGKPLAEGDDAIAAAAELLRAGKIVAIKGLGGFHLACDATNEEAVARL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 241 RQRKHRPGKPLAVMAPDAAWLERCAAVDdmPAALRLLQSAAAPIVLLPWREDGPLSASVAPGLSEVGLMLPANPLQHLLL 320
Cdd:COG0068   240 RRRKRRPAKPFAVMARDLETARRLCEVS--EAEEALLTSPARPIVLLPKRPDSPLAPSVAPGLDTLGVMLPYTPLHHLLL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 321 AQVNLPLVMTSGNASGKPPALSNAQATEQLGAIADRWLMHNRDIVQRADDSLVRLRHQGLFksgaeMLRRARGYVPDALP 400
Cdd:COG0068   318 DELGRPLVMTSGNLSGEPICIDNEEALERLSGIADYFLLHNRPIVNRVDDSVVRVIDGKPR-----FLRRARGYAPLPIP 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 401 LPPGFagqPALLALGADLKNTFCLLRDENAVVSQHLGDLEDSDVERQYQQSIDLFEDIYRFTPGALAVDAHPGYISHRLG 480
Cdd:COG0068   393 LPFEL---PPVLALGAELKNTFCLAKGDQAFLSQHIGDLDNLETLEAFEETIEHLLRLYDVRPEVIACDLHPDYLSTRLA 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 481 KRLAEqRQIPCIEVLHHHAHIVSCLAEHQWprdAGPVIGLALDGIGYGADGQWWGGECLLADYAQCRHLGGLPTVALPGG 560
Cdd:COG0068   470 EELAE-RGLPLIEVQHHHAHIAAVMAEHGL---DGPVLGIALDGTGYGDDGTIWGGEFLLGDYAGFERVGHLRPFPLPGG 545

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 561 DLAARQPWRNLLAQWLRFVPDWQSLPQAAAIPASSAALLSRAIARGINAPPASSAGRLFDAVAAATGFPHEaQSWEGEAA 640
Cdd:COG0068   546 DKAAREPWRMALALLYEAGGEELLEPLLKRFSEKELALLRQMLERGINSPLTSSAGRLFDAVAALLGICDE-ISYEGQAA 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 641 CWLESLAWRSERfqrqraqwRPPVALPVLADG---RLDLATFWRQWLDYRAA---PADRAYAFHYALAQGFGALARRTAR 714
Cdd:COG0068   625 MELEALADRAEE--------AEPYPFPLREIDgllVLDWAPLLRALLEDLQAgvpPAEIAARFHNTLAEAIAELALRLAE 696

                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 715 RHGIHTVALSGGVMHNRLLSVLLHQQL--SGLTVLQPQRLPAGDGGLSLGQALIAAAQLS 772
Cdd:COG0068   697 RTGIDTVALSGGVFQNRLLLELLRARLeaAGFKVLLHRQVPPNDGGISLGQAAIAAARLE 756
hypF TIGR00143
[NiFe] hydrogenase maturation protein HypF; A previously described regulatory effect of HypF ...
 39-768 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: 804.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  39 DGAGVLIYLYQSENiEGFIEALSAGCPPLAHIDSITRQPWRWTAIPTAF-VIEHSGAGRMDTQVVP-DAATCEACRRELN 116
Cdd:TIGR00143   1 TGDGVEIVLEADKE-ESFLNRLKKGLPPLARIEKIIIEPFDGAEHFTTFrIRESKNGGLSLLSIIPaDVATCSDCLEEML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 117 DPANRRYRYPFINCTHCGPRFTIIRRMPYDRPFTSMADFPLCPQCLDEYRQPADRRFHAQPNACPQCGPQvwLENAASQR 196
Cdd:TIGR00143  80 DKNDRRYLYPFISCTHCGPRFTIIEALPYDRENTSMADFPLCPDCAKEYKDPLDRRFHAQPIACPRCGPQ--LNFVSRGG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 197 LAAGEDAIRQAAGALRAGKIVAIKGIGGFHLACDATNTQAVQRLRQRKHRPGKPLAVMAPDAAWLERCAAVDDMPAAlrL 276
Cdd:TIGR00143 158 HAEQDDALLEAAKLLKKGKIIAIKGIGGFHLACDARNDEVVERLRLRKNRPLKPFAVMSPDLESAEQHAELNNLECE--L 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 277 LQSAAAPIVLLPWREDGPLSASVAPGLSEVGLMLPANPLQHLLLAQVNLPLVMTSGNASGKPPALSNAQATEQLGAIADR 356
Cdd:TIGR00143 236 LTSPAAPIVLLRKKPDIKLAPNIAPNLPTIGVMLPYTPLHHLLLQLLAFPLVMTSANLPGLPMAIDNAEILDKLQGIADG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 357 WLMHNRDIVQRADDSLVRlrhqglFKSGA-EMLRRARGYVPDALPLPPgFAGQPALLALGADLKNTFCLLRDENAVVSQH 435
Cdd:TIGR00143 316 FLVHNRRIVNRVDDSVVQ------HVAGEiLFLRRSRGFAPQPLTLPP-NGNPKKILALGAELKNTFSLLKGGQAYLSQH 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 436 LGDLEDSDVERQYQQSIDLFEDIYRFTPGALAVDAHPGYISHrlgkRLAEQRQIPCIEVLHHHAHIVSCLAEHQWprDAG 515
Cdd:TIGR00143 389 IGDLSVYETYKFFKEALNFFLRIYDFEPQDIVCDLHPQYNTT----QYAEELSLPVLRVQHHHAHALAVMADAGV--LEE 462

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 516 PVIGLALDGIGYGADGQWWGGECLLADYAQCRHLGGLPTVALPGGDLAARQPWRNLLAQWLR-----FVPDWQSLpqaaA 590
Cdd:TIGR00143 463 AVIGITWDGVGYGEDGKIWGGECLLIDLGRIERLGRLEEFWLLGGDLATKYPLRILLSILLKhdlndFLKRYQKY----F 538

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 591 IPASSAALLSRAIARGINAPPASSAGRLFDAVAAATGFPHEaQSWEGEAACWLESLAWRSErfqrqrAQWRPPVALPvla 670
Cdd:TIGR00143 539 KQEKELSVLQQALEKKINAPLTTSTGRLFDAVAAALGLCGE-RTYEGEAAIALEALALRSD------GIANYPFEIK--- 608

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 671 DGRLDLATFWRQWLDYRAAPADR---AYAFHYALAQGFGALARRTARRHGIHTVALSGGVMHNRLLSVLLHQQLSGL--T 745
Cdd:TIGR00143 609 NKVLDLKEFYQRFLEDLLVGEDRskiAHIAHKFVASGLVEIATAIAVPFGIHKIVISGGVFYNRLLLERLAKYLKGLgfQ 688

                         730       740
                  ....*....|....*....|...
gi 2238915327 746 VLQPQRLPAGDGGLSLGQALIAA 768
Cdd:TIGR00143 689 FLFHRHLPPGDGGISLGQAVAAA 711
Sua5_yciO_yrdC pfam01300
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
 210-375 5.17e-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: 173.08  E-value: 5.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 210 ALRAGKIVAIKGIGGFHLACDATNTQAVQRLRQRKHRP-GKPLAVMAPDAAWLERCAAVDDmPAALRLLQSA-AAPIVLL 287
Cdd:pfam01300   2 ALRKGGIVAYPTDTVYGLGCDATNEEAVERLYEIKGRPrDKPLAVMVADLEDLKEYAEEVE-EAALRLAERFwPGPLTLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 288 PWREDGPLSASVAPGLSEVGLMLPANPLQHLLLAQVNLPLVMTSGNASGKPPALSNAQATEQLGAIADRWLMHNRdIVQR 367
Cdd:pfam01300  81 LKASKKPLPKLLTPGLGTVGVRLPDHPLALLLLEALGEPLVATSANLSGEPSPTDAEEILEELGGRVDLILDGGR-IAGG 159


                  ....*...
gi 2238915327 368 ADDSLVRL 375
Cdd:pfam01300 160 VPSTVVDL 167
HypF_C pfam17788
HypF Kae1-like domain; This domain is found in the HypF protein. In the structure it is one of ...
 409-507 1.60e-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: 141.07  E-value: 1.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 409 PALLALGADLKNTFCLLRDENAVVSQHLGDLEDSDVERQYQQSIDLFEDIYRFTPGALAVDAHPGYISHRLGKrlaEQRQ 488
Cdd:pfam17788   4 PPVLALGAELKNTFALAKGGQAFLSQHIGDLDNLETLEAFEETLEHLLRLYGIKPEVIACDLHPDYLSTRLAE---ELNG 80

                          90
                  ....*....|....*....
gi 2238915327 489 IPCIEVLHHHAHIVSCLAE 507
Cdd:pfam17788  81 LPLIEVQHHHAHIAAVMAE 99
TsaC COG0009
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal ...
 194-355 2.85e-23

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: 98.24  E-value: 2.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 194 SQRLAAGEDAIRQAAGALRAGKIVAIK-----GIGgfhlaCDATNTQAVQRLRQRKHRP-GKPLAVMAPDAAWLERCAAV 267
Cdd:COG0009     2 ATILKIQPRLIEQAAEALRAGGVVAYPtdtvyGLG-----CDALNKEAVERIFAIKGRPrDKPLIVLVADLSQLEEYAKE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 268 DDmPAALRLLQsAAAP----IVL-----LPWRedgplsasVAPGLSEVGLMLPANPLQHLLLAQVNLPLVMTSGNASGKP 338
Cdd:COG0009    77 VP-DAARRLAK-AFWPgpltLILpatkeVPDL--------LTGGRDTVAVRVPDHPVALALLRALGPPLASTSANLSGEP 146

                         170
                  ....*....|....*..
gi 2238915327 339 PALSNAQATEQLGAIAD 355
Cdd:COG0009   147 PPTTAEEVREQLGDRVD 163
TIGR00057 TIGR00057
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
 201-355 6.71e-22

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: 94.32  E-value: 6.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 201 EDAIRQAAGALRAGKIVAIKGIGGFHLACDATNTQAVQRLRQRKHRP-GKPLAVMAPDAAWLERCAAVDDmpAALRLLQS 279
Cdd:TIGR00057   8 QRGIEQAVKILRKGGIVVYPTDTVYGIGADALDEDAVRRLYRIKGRPsNKPLTVLVSDLSEIEKYAYVPD--DAKRLMKK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 280 ---AAAPIVL-----LPWRedgplsasVAPGLSEVGLMLPANPLQHLLLAQVNLPLVMTSGNASGKPPALSNAQATEQLG 351
Cdd:TIGR00057  86 fwpGPLTLVLkktpeIPRR--------VSGKRKTIGIRVPDNPIALELLEELGKPIVATSANLSGKPSATDVEEAVDELG 157


                  ....
gi 2238915327 352 AIAD 355
Cdd:TIGR00057 158 KLVD 161
zf-HYPF pfam07503
HypF finger; The HypF family of proteins are involved in the maturation and regulation of ...
 108-140 3.93e-19

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: 80.86  E-value: 3.93e-19
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2238915327 108 CEACRRELNDPANRRYRYPFINCTHCGPRFTII 140
Cdd:pfam07503   1 CPDCLREYFDPLDRRFHAQFIACTNCGPRLSLI 33
Acylphosphatase pfam00708
Acylphosphatase;
6-89 1.49e-17

Acylphosphatase;


Pssm-ID: 425830  Cd Length: 85  Bit Score: 78.01  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   6 IQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAG-VLIYLyQS--ENIEGFIEALSAGcPPLAHIDSITRQPWRWTA 82
Cdd:pfam00708   1 KKVLVTGRVQGVGFRPFVYRLAKELGLKGWVRNLPDGsVEIVV-QGpeEDVDKFLEWLKSG-PPPARVDKVEVTEIDEPG 78


                  ....*..
gi 2238915327  83 IPTAFVI 89
Cdd:pfam00708  79 DFSGFEI 85
AcyP COG1254
Acylphosphatase [Energy production and conversion];
6-89 6.62e-17

Acylphosphatase [Energy production and conversion];


Pssm-ID: 440866  Cd Length: 89  Bit Score: 76.35  E-value: 6.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   6 IQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAgVLIYLY-QSENIEGFIEALSAGcPPLAHIDSITRQPWRWTA 82
Cdd:COG1254     4 VRIIVSGRVQGVGFRAFTRRQARRLGLTGWVRNlpDGS-VEVVAEgEEEAVEAFLEWLRKG-PPAARVEDVEVEEEEPTG 81


                  ....*..
gi 2238915327  83 IPTAFVI 89
Cdd:COG1254    82 EFEGFEI 88
zf-HYPF pfam07503
HypF finger; The HypF family of proteins are involved in the maturation and regulation of ...
 158-189 5.86e-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: 71.61  E-value: 5.86e-16
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2238915327 158 CPQCLDEYRQPADRRFHAQPNACPQCGPQVWL 189
Cdd:pfam07503   1 CPDCLREYFDPLDRRFHAQFIACTNCGPRLSL 32
PRK14426 PRK14426
acylphosphatase; Provisional
 1-89 2.76e-11

acylphosphatase; Provisional


Pssm-ID: 184675  Cd Length: 92  Bit Score: 60.42  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   1 MGKNGIQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGVLIYLYQSENIEGFIEALSAGCPPLAHIDSITRQPW 78
Cdd:PRK14426    1 MSKVCIIAWVYGRVQGVGFRYHTQHEALKLGLTGYAKNldDGSVEVVACGEEEQVEKLMEWLKEGGPRSARVDRVLTEPH 80

                          90
                  ....*....|.
gi 2238915327  79 RWTAIPTAFVI 89
Cdd:PRK14426   81 SPRGELTGFSI 91
PRK14431 PRK14431
acylphosphatase; Provisional
 6-72 1.67e-09

acylphosphatase; Provisional


Pssm-ID: 184677  Cd Length: 89  Bit Score: 55.19  E-value: 1.67e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2238915327   6 IQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAGVLIYLYQSEN-IEGFIEALSAGCPPLAHIDS 72
Cdd:PRK14431    4 IHLQVFGRVQGVGFRYFTQRIAMNYNIVGTVQNVDDYVEIYAQGDDAdLERFIQGVIEGASPASNVTS 71
PRK14448 PRK14448
acylphosphatase; Provisional
 7-91 6.03e-07

acylphosphatase; Provisional


Pssm-ID: 172924  Cd Length: 90  Bit Score: 47.83  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   7 QIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGVLIYLYQSENIEGFIEALSAGcPPLAHIDSITRQPWRWTAIP 84
Cdd:PRK14448    5 QFIVYGHVQGVGFRYFTWQEATKIGIKGYVKNrpDGSVEVVAVGSDAQIAAFRDWLQHG-PPTAVVCNVIEQDYQGSRQF 83


                  ....*..
gi 2238915327  85 TAFVIEH 91
Cdd:PRK14448   84 THFSVRR 90
PRK14435 PRK14435
acylphosphatase; Provisional
 6-74 8.12e-07

acylphosphatase; Provisional


Pssm-ID: 184681  Cd Length: 90  Bit Score: 47.59  E-value: 8.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2238915327   6 IQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN-DGAGVLIYLYQSEN-IEGFIEALSAGcPPLAHIDSIT 74
Cdd:PRK14435    4 LKIRVEGIVQGVGFRYFTRRVAKSLGVKGYVMNmDDGSVFIHAEGDENaLRRFLNEVAKG-PPAAVVTNVS 73
PRK14450 PRK14450
acylphosphatase; Provisional
 10-80 2.16e-06

acylphosphatase; Provisional


Pssm-ID: 184683  Cd Length: 91  Bit Score: 46.38  E-value: 2.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2238915327  10 VKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGV-LIYLYQSENIEGFIEALSAGcPPLAHIDSITrqpWRW 80
Cdd:PRK14450    8 VKGKVQGVYFRDFTRTQATRLGLCGYAKNlaNGNEVeVVAEGDKDSLLEFLDLLRSG-PPRAEVKEVE---TSW 77
PRK14433 PRK14433
acylphosphatase; Provisional
 10-76 1.09e-05

acylphosphatase; Provisional


Pssm-ID: 184679  Cd Length: 87  Bit Score: 44.41  E-value: 1.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238915327  10 VKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGVLIYLYQSENIEGFIEALSAGcPPLAHIDSITRQ 76
Cdd:PRK14433    7 VSGRVQGVGYRAFVQKKARELGLSGYAENlsDGRVEVVAEGPKEALERLLHWLRRG-PRHARVEAVDVQ 74
PRK14443 PRK14443
acylphosphatase; Provisional
 1-73 1.37e-05

acylphosphatase; Provisional


Pssm-ID: 172919  Cd Length: 93  Bit Score: 44.28  E-value: 1.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2238915327   1 MGKNGIQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGVLIYLYQSENIEGFIEALSAGCPPLAHIDSI 73
Cdd:PRK14443    1 MARDTAILRVTGFVQGVGFRYTTKHVAYKYDISGTVKNldDGSVEIHAIAEEENLNKFIDAIKKGPSPGCRIEHV 75
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 691-770 2.06e-05

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: 46.91  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 691 ADRAYAFHYALAQGFGALARRTARRHGIHTVALSGGVMHNRLLSVLLHQQLSGLTVLQPqrlPA-GDGGLSLGQALIAAA 769
Cdd:cd24033   191 ADLAATVQKVFEEALLELIKKLLERTGSDNLCLSGGCALNCVANSKLAEEGLFKNVFVP---PApGDSGLSLGAALYVYH 267


                  .
gi 2238915327 770 Q 770
Cdd:cd24033   268 Q 268
PRK14420 PRK14420
acylphosphatase; Provisional
 7-65 3.25e-05

acylphosphatase; Provisional


Pssm-ID: 237710  Cd Length: 91  Bit Score: 43.25  E-value: 3.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2238915327   7 QIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAGVLIYLYQ--SENIEGFIEALSAGCP 65
Cdd:PRK14420    5 HIIVDGRVQGVGFRYFVQMEADKRKLTGWVKNRDDGTVEIEAEgpEEALQLFLDAIEKGSP 65
PRK14429 PRK14429
acylphosphatase; Provisional
 8-49 3.93e-05

acylphosphatase; Provisional


Pssm-ID: 184676  Cd Length: 90  Bit Score: 42.79  E-value: 3.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2238915327   8 IRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAGVLIYLYQ 49
Cdd:PRK14429    6 IKLTGKVQGVGCRRATLTKARALGVTGYVTNCEDGSVEILAQ 47
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 235-778 5.19e-05

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 47.17  E-value: 5.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  235 QAVQRLRQRKHR------PGKPLAVMAPDAAWLERCAAV-----DDMPAALRLLQSAAAPIVL---LPWredgplsASVA 300
Cdd:COG3321    781 DAVEALLADGVRvflevgPGPVLTGLVRQCLAAAGDAVVlpslrRGEDELAQLLTALAQLWVAgvpVDW-------SALY 853

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  301 PGLSEVGLMLPANPLQH--LLLAQVNLPLVMTSGNASGKPPALSNAQATEQLGAIADRWLMHNRDIVQRADDSLVRLRHQ 378
Cdd:COG3321    854 PGRGRRRVPLPTYPFQRedAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  379 GLFKSGAEMLRRARGYVPDALPLPPGFAGQPALLALGADLKNTFCLLRDENAVVSQHLGDLEDSDVERQYQQSIDLFEDI 458
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  459 YRFTPGALAVDAHPGYISHRLGKRLAEQR--QIPCIEVLHHHAHIVSCLAEHQWPRDAGPVIGLALDGIGYGADGQWWGG 536
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAaaAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  537 ECLLADYAQCRHLGGLPTVALPGGDLAARQPWRNLLAQWLRFVPDWQSLPQAAAIPASSAALLSRAIARGINAPPASSAG 616
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  617 RLFDAVAAATGFPHEAQSWEGEAACWLESLAWRSERFQRQRAQWRPPVALPVLADGRLDLATFWRQWLDYRAAPADRAYA 696
Cdd:COG3321   1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327  697 FHYALAQGFGALARRTARRHGIHTVALSGGVMHNRLLSVLLHQQLSGLTVLQPQRLPAGDGGLSLGQALIAAAQLSTADA 776
Cdd:COG3321   1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333


                   ..
gi 2238915327  777 QG 778
Cdd:COG3321   1334 AA 1335
PRK14425 PRK14425
acylphosphatase; Provisional
 6-89 7.43e-05

acylphosphatase; Provisional


Pssm-ID: 172901  Cd Length: 94  Bit Score: 42.15  E-value: 7.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   6 IQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAGVLIYLYQSEN--IEGFIEALSAGcPPLAHIDSITRQPWRWTAI 83
Cdd:PRK14425    8 VRVRITGRVQGVGFRDWTRDEAERLGLTGWVRNESDGSVTALIAGPDsaISAMIERFRRG-PPGASVSGVETEAAQLEEA 86


                  ....*.
gi 2238915327  84 PTAFVI 89
Cdd:PRK14425   87 PTDFRI 92
PRK14451 PRK14451
acylphosphatase; Provisional
 4-79 1.34e-04

acylphosphatase; Provisional


Pssm-ID: 237715  Cd Length: 89  Bit Score: 41.45  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   4 NGIQIR--VKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGVLIYLYQSENIEGFIEALSAGcPPLAHIDSITRQ--P 77
Cdd:PRK14451    1 KELCMRcyISGRVQGVWFRASAKKLAEQLMISGWARNlaDGRVEVFACGKEDKLEEFYTWLQKG-PLNARVDVCTREnlP 79


                  ..
gi 2238915327  78 WR 79
Cdd:PRK14451   80 WQ 81
ASKHA_NBD_MJ1051-like_N cd24100
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ...
 707-770 2.16e-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: 43.62  E-value: 2.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238915327 707 ALARRTARRHGIHTVALSGGVMHNrllsVLLHQQLSGLTVL-----QPqrlPAGDGGLSLGQALIAAAQ 770
Cdd:cd24100   177 EWVKNALKKTGIKNLALAGGVFAN----VKLNQRIAELPEVenlfvFP---SMGDGGLALGAALLALAE 238
PRK14432 PRK14432
acylphosphatase; Provisional
 7-63 2.86e-04

acylphosphatase; Provisional


Pssm-ID: 184678  Cd Length: 93  Bit Score: 40.66  E-value: 2.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   7 QIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAG---VLIYLYQSENIEGFIEALSAG 63
Cdd:PRK14432    5 QYFISGKVQGVGFRFFTEQIANNMKLKGFVKNLNDGrveIVAFFNTKEQMKKFEKLLKNG 64
PRK14421 PRK14421
acylphosphatase; Provisional
 7-77 2.86e-04

acylphosphatase; Provisional


Pssm-ID: 237711 [Multi-domain]  Cd Length: 99  Bit Score: 40.56  E-value: 2.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238915327   7 QIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGVLIYLYQSENIEGFIEALSAGcPPLAHIDSITRQP 77
Cdd:PRK14421    7 QVTIRGRVQGVGYRAWVARTAEALGLEGWVRNrrDGSVEALFAGPADAVAEMIARCRRG-PSAARVDAVEDEP 78
PRK14434 PRK14434
acylphosphatase; Provisional
 6-70 3.35e-04

acylphosphatase; Provisional


Pssm-ID: 184680  Cd Length: 92  Bit Score: 40.13  E-value: 3.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238915327   6 IQIRVKGKVQGVGFRPYVWQLAQQL-KLCGSVSNDGAGVLIYLYQSEN---IEGFIEALSAGCPPLAHI 70
Cdd:PRK14434    4 VRMIVSGRVQGVGFRYSVYSLALEIgDIYGRVWNNDDGTVEILAQSDDsakLAKFIQEIRKGPSKWAKV 72
PRK14424 PRK14424
acylphosphatase; Provisional
 8-76 4.36e-04

acylphosphatase; Provisional


Pssm-ID: 184674  Cd Length: 94  Bit Score: 40.21  E-value: 4.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2238915327   8 IRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAGVLIYLYQ--SENIEGFIEALSAGcPPLAHIDSITRQ 76
Cdd:PRK14424   11 VRVRGVVQGVGFRHATVREAHALGLRGWVANLEDGTVEAMIQgpAAQIDRMLAWLRHG-PPAARVTEVTFE 80
PRK14440 PRK14440
acylphosphatase; Provisional
 8-74 4.54e-04

acylphosphatase; Provisional


Pssm-ID: 172916  Cd Length: 90  Bit Score: 39.80  E-value: 4.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238915327   8 IRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGVLIYLYQSENIEGFIEALSAGcPPLAHIDSIT 74
Cdd:PRK14440    7 ARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNlpDGSVEVVAEGYEEALSKLLERIKQG-PPAAEVEKVD 74
PRK14438 PRK14438
acylphosphatase; Provisional
 8-79 4.80e-04

acylphosphatase; Provisional


Pssm-ID: 172914  Cd Length: 91  Bit Score: 39.82  E-value: 4.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2238915327   8 IRVKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAGVLIYLYQSEniEGFIEALSAGC---PPLAHIDSIT--RQPWR 79
Cdd:PRK14438    7 VTVKGLVQGVAFRHHTQQTAQRLNVSGWVKNLPNGSVQGCFEGE--ETDVAALIDWChhgPSRARVSGVIveREEFR 81
PRK14449 PRK14449
acylphosphatase; Provisional
 3-63 8.65e-04

acylphosphatase; Provisional


Pssm-ID: 184682  Cd Length: 90  Bit Score: 39.04  E-value: 8.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238915327   3 KNGIQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGVLIYLYQSENIEGFIEALSAG 63
Cdd:PRK14449    2 KKTVHLRITGHVQGVGLRYSVYQKAVSLGITGYAENlyDGSVEVVAEGDEENIKELINFIKTG 64
PRK14436 PRK14436
acylphosphatase; Provisional
 1-80 2.16e-03

acylphosphatase; Provisional


Pssm-ID: 172912  Cd Length: 91  Bit Score: 38.02  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327   1 MGKNGIQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DGAGVLIYLYQSENIEGFIEALSAGcPPLAHidsITRQPW 78
Cdd:PRK14436    1 MEIVRAHLRIYGRVQGVGFRWSMQREARKLGVNGWVRNlpDGSVEAVLEGDEERVEALIGWAHQG-PPLAR---VTRVEV 76


                  ..
gi 2238915327  79 RW 80
Cdd:PRK14436   77 KW 78
PRK14445 PRK14445
acylphosphatase; Provisional
 1-40 4.75e-03

acylphosphatase; Provisional


Pssm-ID: 172921  Cd Length: 91  Bit Score: 37.13  E-value: 4.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2238915327   1 MGKNgIQIRVKGKVQGVGFRPYVWQLAQQLKLCGSVSN--DG 40
Cdd:PRK14445    2 MEKR-VHLIVSGLVQGVGFRMFIDRAASELNLSGWVRNlpDG 42
ASKHA_NBD_TobZ_N cd24098
N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar ...
 707-771 4.83e-03

N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar proteins; TobZ (EC 6.1.2.2), also called kanamycin A carbamoyltransferase, or tobramycin carbamoyltransferase, is involved in the biosynthesis of the 2-deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. It catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O-carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5'. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. TobZ consists of two major domains: the N-terminal Kae1-like domain is involved in the transfer of carbamoyl from O-carbamoyladenylate to tobramycin or kanamycin; the C-terminal YrdC-like domain is involved in the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP. The model corresponds to the N-terminal domain.


Pssm-ID: 466948 [Multi-domain]  Cd Length: 243  Bit Score: 39.36  E-value: 4.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238915327 707 ALARRTARRHGIHTVALSGGV-----MHNRLLSVLLHQQLsgltVLQPqrlPAGDGGLSLGQALIAAAQL 771
Cdd:cd24098   181 HLARYLRKKTGERNLCLAGGValncvANGKLLREGPFDNI----FIQP---AAGDAGTALGAALAVWHQL 243
PRK14422 PRK14422
acylphosphatase; Provisional
 10-76 8.54e-03

acylphosphatase; Provisional


Pssm-ID: 237712  Cd Length: 93  Bit Score: 36.26  E-value: 8.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238915327  10 VKGKVQGVGFRPYVWQLAQQLKLCGSVSNDGAGVLIYLYQS--ENIEGFIEALSAGCPPlAHIDSITRQ 76
Cdd:PRK14422   12 VHGHVQGVGFRWWTRSRALELGLTGYAANLADGRVQVVAEGprAACEKLLQLLRGDDTP-GRVDKVVED 79
 
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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