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Conserved domains on  [gi|16758338|ref|NP_446019|]
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formimidoyltransferase-cyclodeaminase [Rattus norvegicus]

Protein Classification

cyclodeaminase/cyclohydrolase family protein( domain architecture ID 11493461)

cyclodeaminase/cyclohydrolase family protein such as formimidoyltetrahydrofolate cyclodeaminase that catalyzes the cyclization of formimidoyltetrahydrofolate to methenyltetrahydrofolate, and methenyltetrahydrofolate cyclohydrolase that catalyzes the interconversion of formyltetrahydrofolate and methylenetetrahydrofolate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FtcD TIGR02024
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent ...
1-328 0e+00

glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism. [Energy metabolism, Amino acids and amines]


:

Pssm-ID: 131079 [Multi-domain]  Cd Length: 298  Bit Score: 534.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338     1 MSQLVECVPNFSEGNNQEVIDAISQAISQTPGCVLLDVDAGPSTNRTVYTFVGQPECVVEGALSAARTASQLIDMRKHKG 80
Cdd:TIGR02024   1 MMKLVECVPNFSEGRNKEVIEKIVDAIIKTDNVKLLDVDMDPDHNRSVITFVGEPECVVNAALKLAKKAAELIDMRNHKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338    81 EHPRMGALDVCPFIPVRGVSMDECVLCAKAFGQRLAEELNVPVYLYGEAAQMPSRQTLPAIRAGEYEALPEKLKQAEWVP 160
Cdd:TIGR02024  81 EHPRMGAADVIPFIPVRNVTMEECVELAKEFGKRLGEELGVPVYLYEEAATRPERQTLAAIRKGQYEALFEKIKDPKWKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   161 DFGPSSFVPSWGATVTGARKFLIAFNINL-LSTKEQAHRIALNLREQGRGkdqpgrLKKVQGIGWYLEEKNLAQVSTNLL 239
Cdd:TIGR02024 161 DFGPSEFNPKAGATATGARKFLIAFNVNLgTSNLEIAKKIAKAIRFQGGG------LRFVKAIGLYLEEKNLVQVSMNLT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   240 DFEVTALHTVYEEARREAQELNLPVVGSQLVGLVPLKALLDAAAFYCDkeklfvleeehrirlvvnrlgLDSlapFDPKe 319
Cdd:TIGR02024 235 NYEKTPLYRVFELIKMEAQRYGVPVVGSELVGLVPLKALLDVAAYYLR---------------------LDS---FDPK- 289

                  ....*....
gi 16758338   320 RIIEYLVPD 328
Cdd:TIGR02024 290 QIIEYLLLE 298
FTCD_C pfam04961
Formiminotransferase-cyclodeaminase; Members of this family are thought to be ...
339-520 8.45e-58

Formiminotransferase-cyclodeaminase; Members of this family are thought to be Formiminotransferase- cyclodeaminase enzymes EC:4.3.1.4. This domain is found in the C-terminus of the bifunctional animal members of the family.


:

Pssm-ID: 461500  Cd Length: 182  Bit Score: 190.39  E-value: 8.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   339 SLRAFVREVGARSAAPGGGSVAAAVAALGAALASMVGQMTYGRRQFDHLDSTMRRLIPPFHAASAQLTSLVDADARAFAA 418
Cdd:pfam04961   1 SIKEFLEELASKSPAPGGGSAAALVGALGAALGSMVANLTIGKKKYADVEEEMEELLEKAEELREELLDLIDEDAEAFNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   419 CLGAIKLPKNTPEERDRRTCALQEGLRQAVAVPLKLAETVSQLWPALQELAQCGNLSCLSDLQVAAKALETGVFGAYFNV 498
Cdd:pfam04961  81 VMAAYKLPKETEEEKAARSEAIQEALKEAAEVPLEIARLCLELLELAEELAKKGNPNAISDAGVAALLARAALEGALLNV 160
                         170       180
                  ....*....|....*....|..
gi 16758338   499 LINLKDMTDDVFKEKTRHRISS 520
Cdd:pfam04961 161 KINLKSIKDEEFAEELRAEAEE 182
 
Name Accession Description Interval E-value
FtcD TIGR02024
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent ...
1-328 0e+00

glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131079 [Multi-domain]  Cd Length: 298  Bit Score: 534.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338     1 MSQLVECVPNFSEGNNQEVIDAISQAISQTPGCVLLDVDAGPSTNRTVYTFVGQPECVVEGALSAARTASQLIDMRKHKG 80
Cdd:TIGR02024   1 MMKLVECVPNFSEGRNKEVIEKIVDAIIKTDNVKLLDVDMDPDHNRSVITFVGEPECVVNAALKLAKKAAELIDMRNHKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338    81 EHPRMGALDVCPFIPVRGVSMDECVLCAKAFGQRLAEELNVPVYLYGEAAQMPSRQTLPAIRAGEYEALPEKLKQAEWVP 160
Cdd:TIGR02024  81 EHPRMGAADVIPFIPVRNVTMEECVELAKEFGKRLGEELGVPVYLYEEAATRPERQTLAAIRKGQYEALFEKIKDPKWKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   161 DFGPSSFVPSWGATVTGARKFLIAFNINL-LSTKEQAHRIALNLREQGRGkdqpgrLKKVQGIGWYLEEKNLAQVSTNLL 239
Cdd:TIGR02024 161 DFGPSEFNPKAGATATGARKFLIAFNVNLgTSNLEIAKKIAKAIRFQGGG------LRFVKAIGLYLEEKNLVQVSMNLT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   240 DFEVTALHTVYEEARREAQELNLPVVGSQLVGLVPLKALLDAAAFYCDkeklfvleeehrirlvvnrlgLDSlapFDPKe 319
Cdd:TIGR02024 235 NYEKTPLYRVFELIKMEAQRYGVPVVGSELVGLVPLKALLDVAAYYLR---------------------LDS---FDPK- 289

                  ....*....
gi 16758338   320 RIIEYLVPD 328
Cdd:TIGR02024 290 QIIEYLLLE 298
GluFT COG3643
Glutamate formiminotransferase [Amino acid transport and metabolism];
1-311 6.41e-170

Glutamate formiminotransferase [Amino acid transport and metabolism];


Pssm-ID: 442860 [Multi-domain]  Cd Length: 303  Bit Score: 482.74  E-value: 6.41e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   1 MSQLVECVPNFSEGNNQEVIDAISQAISQTPGCVLLDVDAGPSTNRTVYTFVGQPECVVEGALSAARTASQLIDMRKHKG 80
Cdd:COG3643   1 MMKIVECVPNFSEGRDKEVIEAIVDAIRSVEGVKLLDYSPDADHNRTVVTFVGEPEAVKEAAFNAAKKAAELIDMTKHKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338  81 EHPRMGALDVCPFIPVRGVSMDECVLCAKAFGQRLAEELNVPVYLYGEAAQMPSRQTLPAIRAGEYEALPEKLKQAEWVP 160
Cdd:COG3643  81 EHPRMGATDVIPFVPIRNVTMEECVELARELGKRIGEELGIPVYLYEEAATRPERKNLADIRKGEYEGLKEKIKDPEWKP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338 161 DFGPSSFVPSWGATVTGARKFLIAFNINLLST-KEQAHRIALNLREQGrgkdqpGRLKKVQGIGWYLEEKNLAQVSTNLL 239
Cdd:COG3643 161 DFGPAELHPTAGATAVGARMFLIAYNVNLNTDdVEIAKKIAKAVRESS------GGLRYVKAIGVYLEERGIAQVSMNLT 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758338 240 DFEVTALHTVYEEARREAQELNLPVVGSQLVGLVPLKALLDAAAFYCDKEKLFvleEEHRIRLVVNRLGLDS 311
Cdd:COG3643 235 DYTKTPLYRVFELVKREAARYGVNVVGSELVGLVPLEALLDAAEYYLQLENFD---EDQILENRLLELGLDE 303
FTCD_N pfam07837
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of ...
4-179 2.15e-114

Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of formiminotransferase- cyclodeaminase (FTCD) forms a homodimer, and each protomer comprises two subdomains. The N-terminal subdomain is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.


Pssm-ID: 462283  Cd Length: 176  Bit Score: 336.37  E-value: 2.15e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338     4 LVECVPNFSEGNNQEVIDAISQAISQTPGCVLLDVDAGPSTNRTVYTFVGQPECVVEGALSAARTASQLIDMRKHKGEHP 83
Cdd:pfam07837   1 LVECVPNFSEGRDKEVIEAIARAARSVPGVKLLDVFSDADHNRTVVTLVGEPEAVVEAALAAAKKAFELIDMRKHKGEHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338    84 RMGALDVCPFIPVRGVSMDECVLCAKAFGQRLAEELNVPVYLYGEAAQMPSRQTLPAIRAGEYEALPEKLKQAEWVPDFG 163
Cdd:pfam07837  81 RMGAVDVIPFVPLRGVTMEECVELAKELAKRIGEELGVPVYLYEAAATRPERRNLAAIRKGQYEGLAEKIKDPEWKPDFG 160
                         170
                  ....*....|....*.
gi 16758338   164 PSSFVPSWGATVTGAR 179
Cdd:pfam07837 161 PAEFHPTAGATAVGAR 176
FTCD_C pfam04961
Formiminotransferase-cyclodeaminase; Members of this family are thought to be ...
339-520 8.45e-58

Formiminotransferase-cyclodeaminase; Members of this family are thought to be Formiminotransferase- cyclodeaminase enzymes EC:4.3.1.4. This domain is found in the C-terminus of the bifunctional animal members of the family.


Pssm-ID: 461500  Cd Length: 182  Bit Score: 190.39  E-value: 8.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   339 SLRAFVREVGARSAAPGGGSVAAAVAALGAALASMVGQMTYGRRQFDHLDSTMRRLIPPFHAASAQLTSLVDADARAFAA 418
Cdd:pfam04961   1 SIKEFLEELASKSPAPGGGSAAALVGALGAALGSMVANLTIGKKKYADVEEEMEELLEKAEELREELLDLIDEDAEAFNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   419 CLGAIKLPKNTPEERDRRTCALQEGLRQAVAVPLKLAETVSQLWPALQELAQCGNLSCLSDLQVAAKALETGVFGAYFNV 498
Cdd:pfam04961  81 VMAAYKLPKETEEEKAARSEAIQEALKEAAEVPLEIARLCLELLELAEELAKKGNPNAISDAGVAALLARAALEGALLNV 160
                         170       180
                  ....*....|....*....|..
gi 16758338   499 LINLKDMTDDVFKEKTRHRISS 520
Cdd:pfam04961 161 KINLKSIKDEEFAEELRAEAEE 182
FtcD COG3404
Formiminotetrahydrofolate cyclodeaminase [Amino acid transport and metabolism];
333-539 5.99e-44

Formiminotetrahydrofolate cyclodeaminase [Amino acid transport and metabolism];


Pssm-ID: 442631  Cd Length: 209  Bit Score: 154.96  E-value: 5.99e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338 333 QSLLDASLRAFVREVGARSAAPGGGSVAAAVAALGAALASMVGQMTYGRRQFDHLDSTMRRLIPPFHAASAQLTSLVDAD 412
Cdd:COG3404   1 MMLLDLTIKEFLEELASKSPAPGGGSAAALVGALGAALGSMVANLTIGKKKYADVEEEMKEILEKAEKLREELLALIDED 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338 413 ARAFAACLGAIKLPKNTPEERDRRTCALQEGLRQAVAVPLKLAETVSQLWPALQELAQCGNLSCLSDLQVAAKALETGVF 492
Cdd:COG3404  81 AEAFNEVMAAYKLPKETEEEKAARSEAIQEALKEAAEVPLEVARLCLEVLELAEELAEKGNPNAISDAGVAALLARAALK 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16758338 493 GAYFNVLINLKDMTDDVFKEKTRHRISSLLQEAKTQAALVLGSLEAR 539
Cdd:COG3404 161 GALLNVKINLKSIKDEEFVEELRAEAEELLKEAEELADEVLAIVEEK 207
 
Name Accession Description Interval E-value
FtcD TIGR02024
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent ...
1-328 0e+00

glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131079 [Multi-domain]  Cd Length: 298  Bit Score: 534.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338     1 MSQLVECVPNFSEGNNQEVIDAISQAISQTPGCVLLDVDAGPSTNRTVYTFVGQPECVVEGALSAARTASQLIDMRKHKG 80
Cdd:TIGR02024   1 MMKLVECVPNFSEGRNKEVIEKIVDAIIKTDNVKLLDVDMDPDHNRSVITFVGEPECVVNAALKLAKKAAELIDMRNHKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338    81 EHPRMGALDVCPFIPVRGVSMDECVLCAKAFGQRLAEELNVPVYLYGEAAQMPSRQTLPAIRAGEYEALPEKLKQAEWVP 160
Cdd:TIGR02024  81 EHPRMGAADVIPFIPVRNVTMEECVELAKEFGKRLGEELGVPVYLYEEAATRPERQTLAAIRKGQYEALFEKIKDPKWKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   161 DFGPSSFVPSWGATVTGARKFLIAFNINL-LSTKEQAHRIALNLREQGRGkdqpgrLKKVQGIGWYLEEKNLAQVSTNLL 239
Cdd:TIGR02024 161 DFGPSEFNPKAGATATGARKFLIAFNVNLgTSNLEIAKKIAKAIRFQGGG------LRFVKAIGLYLEEKNLVQVSMNLT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   240 DFEVTALHTVYEEARREAQELNLPVVGSQLVGLVPLKALLDAAAFYCDkeklfvleeehrirlvvnrlgLDSlapFDPKe 319
Cdd:TIGR02024 235 NYEKTPLYRVFELIKMEAQRYGVPVVGSELVGLVPLKALLDVAAYYLR---------------------LDS---FDPK- 289

                  ....*....
gi 16758338   320 RIIEYLVPD 328
Cdd:TIGR02024 290 QIIEYLLLE 298
GluFT COG3643
Glutamate formiminotransferase [Amino acid transport and metabolism];
1-311 6.41e-170

Glutamate formiminotransferase [Amino acid transport and metabolism];


Pssm-ID: 442860 [Multi-domain]  Cd Length: 303  Bit Score: 482.74  E-value: 6.41e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   1 MSQLVECVPNFSEGNNQEVIDAISQAISQTPGCVLLDVDAGPSTNRTVYTFVGQPECVVEGALSAARTASQLIDMRKHKG 80
Cdd:COG3643   1 MMKIVECVPNFSEGRDKEVIEAIVDAIRSVEGVKLLDYSPDADHNRTVVTFVGEPEAVKEAAFNAAKKAAELIDMTKHKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338  81 EHPRMGALDVCPFIPVRGVSMDECVLCAKAFGQRLAEELNVPVYLYGEAAQMPSRQTLPAIRAGEYEALPEKLKQAEWVP 160
Cdd:COG3643  81 EHPRMGATDVIPFVPIRNVTMEECVELARELGKRIGEELGIPVYLYEEAATRPERKNLADIRKGEYEGLKEKIKDPEWKP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338 161 DFGPSSFVPSWGATVTGARKFLIAFNINLLST-KEQAHRIALNLREQGrgkdqpGRLKKVQGIGWYLEEKNLAQVSTNLL 239
Cdd:COG3643 161 DFGPAELHPTAGATAVGARMFLIAYNVNLNTDdVEIAKKIAKAVRESS------GGLRYVKAIGVYLEERGIAQVSMNLT 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758338 240 DFEVTALHTVYEEARREAQELNLPVVGSQLVGLVPLKALLDAAAFYCDKEKLFvleEEHRIRLVVNRLGLDS 311
Cdd:COG3643 235 DYTKTPLYRVFELVKREAARYGVNVVGSELVGLVPLEALLDAAEYYLQLENFD---EDQILENRLLELGLDE 303
FTCD_N pfam07837
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of ...
4-179 2.15e-114

Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of formiminotransferase- cyclodeaminase (FTCD) forms a homodimer, and each protomer comprises two subdomains. The N-terminal subdomain is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.


Pssm-ID: 462283  Cd Length: 176  Bit Score: 336.37  E-value: 2.15e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338     4 LVECVPNFSEGNNQEVIDAISQAISQTPGCVLLDVDAGPSTNRTVYTFVGQPECVVEGALSAARTASQLIDMRKHKGEHP 83
Cdd:pfam07837   1 LVECVPNFSEGRDKEVIEAIARAARSVPGVKLLDVFSDADHNRTVVTLVGEPEAVVEAALAAAKKAFELIDMRKHKGEHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338    84 RMGALDVCPFIPVRGVSMDECVLCAKAFGQRLAEELNVPVYLYGEAAQMPSRQTLPAIRAGEYEALPEKLKQAEWVPDFG 163
Cdd:pfam07837  81 RMGAVDVIPFVPLRGVTMEECVELAKELAKRIGEELGVPVYLYEAAATRPERRNLAAIRKGQYEGLAEKIKDPEWKPDFG 160
                         170
                  ....*....|....*.
gi 16758338   164 PSSFVPSWGATVTGAR 179
Cdd:pfam07837 161 PAEFHPTAGATAVGAR 176
FTCD pfam02971
Formiminotransferase domain;
181-324 5.19e-90

Formiminotransferase domain;


Pssm-ID: 460770  Cd Length: 146  Bit Score: 272.55  E-value: 5.19e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   181 FLIAFNINLLST-KEQAHRIALNLREQGRGKDQ-PGRLKKVQGIGWYLEEKNLAQVSTNLLDFEVTALHTVYEEARREAQ 258
Cdd:pfam02971   1 FLIAYNVNLNTTsKEQAHRIALNIRESGRGKREePGRLKGVKAIGWYLEEYNLAQVSMNLTDIEVTPLHVVFEEVCKEAE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758338   259 ELNLPVVGSQLVGLVPLKALLDAAAFYCDKEKLFVLEEEHRIRLVVNRLGLDSLAPFDPKERIIEY 324
Cdd:pfam02971  81 ELGLRVTGSEIVGLVPLKALLDAADYYIEKEQLFILEEEEKIRLAIKRLGLDSLAPFDPKEKIIEY 146
FTCD_C pfam04961
Formiminotransferase-cyclodeaminase; Members of this family are thought to be ...
339-520 8.45e-58

Formiminotransferase-cyclodeaminase; Members of this family are thought to be Formiminotransferase- cyclodeaminase enzymes EC:4.3.1.4. This domain is found in the C-terminus of the bifunctional animal members of the family.


Pssm-ID: 461500  Cd Length: 182  Bit Score: 190.39  E-value: 8.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   339 SLRAFVREVGARSAAPGGGSVAAAVAALGAALASMVGQMTYGRRQFDHLDSTMRRLIPPFHAASAQLTSLVDADARAFAA 418
Cdd:pfam04961   1 SIKEFLEELASKSPAPGGGSAAALVGALGAALGSMVANLTIGKKKYADVEEEMEELLEKAEELREELLDLIDEDAEAFNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338   419 CLGAIKLPKNTPEERDRRTCALQEGLRQAVAVPLKLAETVSQLWPALQELAQCGNLSCLSDLQVAAKALETGVFGAYFNV 498
Cdd:pfam04961  81 VMAAYKLPKETEEEKAARSEAIQEALKEAAEVPLEIARLCLELLELAEELAKKGNPNAISDAGVAALLARAALEGALLNV 160
                         170       180
                  ....*....|....*....|..
gi 16758338   499 LINLKDMTDDVFKEKTRHRISS 520
Cdd:pfam04961 161 KINLKSIKDEEFAEELRAEAEE 182
FtcD COG3404
Formiminotetrahydrofolate cyclodeaminase [Amino acid transport and metabolism];
333-539 5.99e-44

Formiminotetrahydrofolate cyclodeaminase [Amino acid transport and metabolism];


Pssm-ID: 442631  Cd Length: 209  Bit Score: 154.96  E-value: 5.99e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338 333 QSLLDASLRAFVREVGARSAAPGGGSVAAAVAALGAALASMVGQMTYGRRQFDHLDSTMRRLIPPFHAASAQLTSLVDAD 412
Cdd:COG3404   1 MMLLDLTIKEFLEELASKSPAPGGGSAAALVGALGAALGSMVANLTIGKKKYADVEEEMKEILEKAEKLREELLALIDED 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758338 413 ARAFAACLGAIKLPKNTPEERDRRTCALQEGLRQAVAVPLKLAETVSQLWPALQELAQCGNLSCLSDLQVAAKALETGVF 492
Cdd:COG3404  81 AEAFNEVMAAYKLPKETEEEKAARSEAIQEALKEAAEVPLEVARLCLEVLELAEELAEKGNPNAISDAGVAALLARAALK 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16758338 493 GAYFNVLINLKDMTDDVFKEKTRHRISSLLQEAKTQAALVLGSLEAR 539
Cdd:COG3404 161 GALLNVKINLKSIKDEEFVEELRAEAEELLKEAEELADEVLAIVEEK 207
 
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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