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Conserved domains on  [gi|575523331|gb|AHG98023|]
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NifB [Cloning vector pCV_cistron14]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nifB super family cl26968
nitrogenase cofactor biosynthesis protein NifB; This model describes NifB, a protein required ...
22-445 0e+00

nitrogenase cofactor biosynthesis protein NifB; This model describes NifB, a protein required for the biosynthesis of the iron-molybdenum (or iron-vanadium) cofactor used by the nitrogen-fixing enzyme nitrogenase. NifB belongs to the radical SAM family, and the FeMo cluster biosynthesis process requires S-adenosylmethionine. Archaeal homologs lack the most C-terminal region and score between the trusted and noise cutoffs of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]


The actual alignment was detected with superfamily member TIGR01290:

Pssm-ID: 273539 [Multi-domain]  Cd Length: 442  Bit Score: 627.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   22 TPLVADKAAAHPCYSRHGHHRFARMHLPVAPACNLQCNYCNRKFDCSNESRPGVSSTLLTPEQAVVKVRQVAQAIPQLSV 101
Cdd:TIGR01290   2 NPAIAEKIAQHPCYSVEAHHYFARMHLAVAPACNIQCNYCNRKYDCANESRPGVVSELLTPEQALRKARQVAAEIPQLSV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  102 VGIAGPGDPLANIARTFRTLELIREQLPDLKLCLSTNGLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIYAWLWLDGE 181
Cdd:TIGR01290  82 VGIAGPGDPLANIGKTFQTLELVARQLPDVKLCLSTNGLMLPEHVDRLVDLGVGHVTITINAIDPAVGEKIYPWVWYEGE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  182 RYSGREAGEILIARQLEGVRRLTAKGVLVKINSVLIPGINDSGMAGVSRALRASGAFIHNIMPLIARPEHGTVFGLNGQP 261
Cdd:TIGR01290 162 RYTGREAADLLIERQLEGLEKLTERGILVKVNSVLIPGINDEHLVEVSKQVKELGAFLHNVMPLISAPEHGTVYGLNGQR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  262 EPDAETLAATRSRCGEVMPQMTHCHQCRADAIGMLGEDRSQQFT--QLPAPESL-----PAWLPILHQ--RAQLHASIAT 332
Cdd:TIGR01290 242 EPDPDELAALRDRLEMGTPQMRHCHQCRADAVGLLGEDRNADFPleTFPADEVYdlanrPQYLQELERrrRQTLHASIVA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  333 RGESEADDACLVAVASSRGDVIDCHFGHADRFYIYSLSAAGMVLVNERFTPKYCQGRDDCEpQDNAARFAAILELLADVK 412
Cdd:TIGR01290 322 RGGSEEADECLVAVATKGGGAVNQHFGHADEFTIFSLSAAGVMLIGQRKIDRYCRGPDDCE-EDAAQNLDAIIELLSDCK 400
                         410       420       430
                  ....*....|....*....|....*....|...
gi 575523331  413 AVFCVRIGHTPWQQLEQEGIEPCVDGAWRPVSE 445
Cdd:TIGR01290 401 ALLCSRIGLTPRKALEAAGVEPQVDYDGQPIET 433
 
Name Accession Description Interval E-value
nifB TIGR01290
nitrogenase cofactor biosynthesis protein NifB; This model describes NifB, a protein required ...
22-445 0e+00

nitrogenase cofactor biosynthesis protein NifB; This model describes NifB, a protein required for the biosynthesis of the iron-molybdenum (or iron-vanadium) cofactor used by the nitrogen-fixing enzyme nitrogenase. NifB belongs to the radical SAM family, and the FeMo cluster biosynthesis process requires S-adenosylmethionine. Archaeal homologs lack the most C-terminal region and score between the trusted and noise cutoffs of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 273539 [Multi-domain]  Cd Length: 442  Bit Score: 627.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   22 TPLVADKAAAHPCYSRHGHHRFARMHLPVAPACNLQCNYCNRKFDCSNESRPGVSSTLLTPEQAVVKVRQVAQAIPQLSV 101
Cdd:TIGR01290   2 NPAIAEKIAQHPCYSVEAHHYFARMHLAVAPACNIQCNYCNRKYDCANESRPGVVSELLTPEQALRKARQVAAEIPQLSV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  102 VGIAGPGDPLANIARTFRTLELIREQLPDLKLCLSTNGLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIYAWLWLDGE 181
Cdd:TIGR01290  82 VGIAGPGDPLANIGKTFQTLELVARQLPDVKLCLSTNGLMLPEHVDRLVDLGVGHVTITINAIDPAVGEKIYPWVWYEGE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  182 RYSGREAGEILIARQLEGVRRLTAKGVLVKINSVLIPGINDSGMAGVSRALRASGAFIHNIMPLIARPEHGTVFGLNGQP 261
Cdd:TIGR01290 162 RYTGREAADLLIERQLEGLEKLTERGILVKVNSVLIPGINDEHLVEVSKQVKELGAFLHNVMPLISAPEHGTVYGLNGQR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  262 EPDAETLAATRSRCGEVMPQMTHCHQCRADAIGMLGEDRSQQFT--QLPAPESL-----PAWLPILHQ--RAQLHASIAT 332
Cdd:TIGR01290 242 EPDPDELAALRDRLEMGTPQMRHCHQCRADAVGLLGEDRNADFPleTFPADEVYdlanrPQYLQELERrrRQTLHASIVA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  333 RGESEADDACLVAVASSRGDVIDCHFGHADRFYIYSLSAAGMVLVNERFTPKYCQGRDDCEpQDNAARFAAILELLADVK 412
Cdd:TIGR01290 322 RGGSEEADECLVAVATKGGGAVNQHFGHADEFTIFSLSAAGVMLIGQRKIDRYCRGPDDCE-EDAAQNLDAIIELLSDCK 400
                         410       420       430
                  ....*....|....*....|....*....|...
gi 575523331  413 AVFCVRIGHTPWQQLEQEGIEPCVDGAWRPVSE 445
Cdd:TIGR01290 401 ALLCSRIGLTPRKALEAAGVEPQVDYDGQPIET 433
NifB cd00852
NifB belongs to a family of iron-molybdenum cluster-binding proteins that includes NifX, and ...
343-451 1.40e-43

NifB belongs to a family of iron-molybdenum cluster-binding proteins that includes NifX, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme as part of nitrogen fixation in bacteria. This domain is sometimes found fused to a N-terminal domain (the Radical SAM domain) in nifB-like proteins.


Pssm-ID: 238432  Cd Length: 106  Bit Score: 148.92  E-value: 1.40e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 343 LVAVASSRGDVIDCHFGHADRFYIYSLSAAGMVLVNERFTPKYCQGRDdcePQDNAARFAAILELLADVKAVFCVRIGHT 422
Cdd:cd00852    1 LVAVASKGGGRVNQHFGHATEFQIYEVSGSGVKFVEHRKVDPYCGGGD---CGDEEDRLDAIIKLLSDCDAVLCAKIGDE 77
                         90       100
                 ....*....|....*....|....*....
gi 575523331 423 PWQQLEQEGIEPCVDGAWRPVSEVLPAWW 451
Cdd:cd00852   78 PKEKLEEAGIEVIEAYAGEYIEEALLELY 106
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
45-216 5.37e-32

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 119.62  E-value: 5.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  45 RMHLPVAPACNLQCNYCNRKFDCSNESRpgvsstlLTPEQAVVKVRQVAQAipQLSVVGIAGpGDPLANiARTFRTLELI 124
Cdd:COG0535    1 RLQIELTNRCNLRCKHCYADAGPKRPGE-------LSTEEAKRILDELAEL--GVKVVGLTG-GEPLLR-PDLFELVEYA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 125 REQlpDLKLCLSTNGLVLPDA-VDRLLDVGVDHVTVTINTLDAEIaaqiyawlwldGERYSGREAGeilIARQLEGVRRL 203
Cdd:COG0535   70 KEL--GIRVNLSTNGTLLTEElAERLAEAGLDHVTISLDGVDPET-----------HDKIRGVPGA---FDKVLEAIKLL 133
                        170
                 ....*....|...
gi 575523331 204 TAKGVLVKINSVL 216
Cdd:COG0535  134 KEAGIPVGINTVY 146
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
50-223 8.74e-17

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 77.57  E-value: 8.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   50 VAPACNLQCNYCNRkfdcsNESRPGVSSTLLTPEQAVVKVRQVAQaiPQLSVVGIAGpGDPLANIARTFRTLELI-REQL 128
Cdd:pfam04055   1 ITRGCNLRCTYCAF-----PSIRARGKGRELSPEEILEEAKELKR--LGVEVVILGG-GEPLLLPDLVELLERLLkLELA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  129 PDLKLCLSTNGLVL-PDAVDRLLDVGVDHVTVTINTLDAEIAAQIyawlwldgerysgreAGEILIARQLEGVRRLTAKG 207
Cdd:pfam04055  73 EGIRITLETNGTLLdEELLELLKEAGLDRVSIGLESGDDEVLKLI---------------NRGHTFEEVLEALELLREAG 137
                         170
                  ....*....|....*..
gi 575523331  208 V-LVKINSVLIPGINDS 223
Cdd:pfam04055 138 IpVVTDNIVGLPGETDE 154
moaA PRK00164
GTP 3',8-cyclase MoaA;
42-222 7.31e-13

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 69.40  E-value: 7.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  42 RFARMH----LPVAPACNLQCNYCNRkfdcsNESRPGV-SSTLLTPEQavvkVRQVAQAIPQLSV--VGIAGpGDPL--A 112
Cdd:PRK00164  11 RFGRKFtylrISVTDRCNFRCTYCMP-----EGYLPFLpKEELLSLEE----IERLVRAFVALGVrkVRLTG-GEPLlrK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 113 NIARTFRTlelIREQLPDLKLCLSTNGLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIyawlwldgerysgreAGEIL 192
Cdd:PRK00164  81 DLEDIIAA---LAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAI---------------TGRDR 142
                        170       180       190
                 ....*....|....*....|....*....|.
gi 575523331 193 IARQLEGVRRLTAKGVL-VKINSVLIPGIND 222
Cdd:PRK00164 143 LDQVLAGIDAALAAGLTpVKVNAVLMKGVND 173
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
48-255 1.08e-06

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 49.32  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331    48 LPVAPACNLQCNYCnrkfDCSNESRPGVSstllTPEQAVVK-----VRQVAQAIPqLSVVGIAGPGDPLANIARTFRTLE 122
Cdd:smart00729   5 YIITRGCPRRCTFC----SFPSLRGKLRS----RYLEALVReiellAEKGEKEGL-VGTVFIGGGTPTLLSPEQLEELLE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   123 LIREQLPDLK---LCLSTN-GLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIyawlwldGERYSGREAgeiliarqLE 198
Cdd:smart00729  76 AIREILGLAKdveITIETRpDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAI-------NRGHTVEDV--------LE 140
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   199 GVRRLTAKGVLvKINSVLI---PGINDSGMAGVSRALRASGAFIHNIMPLIARPehGTVF 255
Cdd:smart00729 141 AVELLREAGPI-KVSTDLIvglPGETEEDFEETLKLLKELGPDRVSIFPLSPRP--GTPL 197
 
Name Accession Description Interval E-value
nifB TIGR01290
nitrogenase cofactor biosynthesis protein NifB; This model describes NifB, a protein required ...
22-445 0e+00

nitrogenase cofactor biosynthesis protein NifB; This model describes NifB, a protein required for the biosynthesis of the iron-molybdenum (or iron-vanadium) cofactor used by the nitrogen-fixing enzyme nitrogenase. NifB belongs to the radical SAM family, and the FeMo cluster biosynthesis process requires S-adenosylmethionine. Archaeal homologs lack the most C-terminal region and score between the trusted and noise cutoffs of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 273539 [Multi-domain]  Cd Length: 442  Bit Score: 627.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   22 TPLVADKAAAHPCYSRHGHHRFARMHLPVAPACNLQCNYCNRKFDCSNESRPGVSSTLLTPEQAVVKVRQVAQAIPQLSV 101
Cdd:TIGR01290   2 NPAIAEKIAQHPCYSVEAHHYFARMHLAVAPACNIQCNYCNRKYDCANESRPGVVSELLTPEQALRKARQVAAEIPQLSV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  102 VGIAGPGDPLANIARTFRTLELIREQLPDLKLCLSTNGLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIYAWLWLDGE 181
Cdd:TIGR01290  82 VGIAGPGDPLANIGKTFQTLELVARQLPDVKLCLSTNGLMLPEHVDRLVDLGVGHVTITINAIDPAVGEKIYPWVWYEGE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  182 RYSGREAGEILIARQLEGVRRLTAKGVLVKINSVLIPGINDSGMAGVSRALRASGAFIHNIMPLIARPEHGTVFGLNGQP 261
Cdd:TIGR01290 162 RYTGREAADLLIERQLEGLEKLTERGILVKVNSVLIPGINDEHLVEVSKQVKELGAFLHNVMPLISAPEHGTVYGLNGQR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  262 EPDAETLAATRSRCGEVMPQMTHCHQCRADAIGMLGEDRSQQFT--QLPAPESL-----PAWLPILHQ--RAQLHASIAT 332
Cdd:TIGR01290 242 EPDPDELAALRDRLEMGTPQMRHCHQCRADAVGLLGEDRNADFPleTFPADEVYdlanrPQYLQELERrrRQTLHASIVA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  333 RGESEADDACLVAVASSRGDVIDCHFGHADRFYIYSLSAAGMVLVNERFTPKYCQGRDDCEpQDNAARFAAILELLADVK 412
Cdd:TIGR01290 322 RGGSEEADECLVAVATKGGGAVNQHFGHADEFTIFSLSAAGVMLIGQRKIDRYCRGPDDCE-EDAAQNLDAIIELLSDCK 400
                         410       420       430
                  ....*....|....*....|....*....|...
gi 575523331  413 AVFCVRIGHTPWQQLEQEGIEPCVDGAWRPVSE 445
Cdd:TIGR01290 401 ALLCSRIGLTPRKALEAAGVEPQVDYDGQPIET 433
NifB cd00852
NifB belongs to a family of iron-molybdenum cluster-binding proteins that includes NifX, and ...
343-451 1.40e-43

NifB belongs to a family of iron-molybdenum cluster-binding proteins that includes NifX, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme as part of nitrogen fixation in bacteria. This domain is sometimes found fused to a N-terminal domain (the Radical SAM domain) in nifB-like proteins.


Pssm-ID: 238432  Cd Length: 106  Bit Score: 148.92  E-value: 1.40e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 343 LVAVASSRGDVIDCHFGHADRFYIYSLSAAGMVLVNERFTPKYCQGRDdcePQDNAARFAAILELLADVKAVFCVRIGHT 422
Cdd:cd00852    1 LVAVASKGGGRVNQHFGHATEFQIYEVSGSGVKFVEHRKVDPYCGGGD---CGDEEDRLDAIIKLLSDCDAVLCAKIGDE 77
                         90       100
                 ....*....|....*....|....*....
gi 575523331 423 PWQQLEQEGIEPCVDGAWRPVSEVLPAWW 451
Cdd:cd00852   78 PKEKLEEAGIEVIEAYAGEYIEEALLELY 106
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
45-216 5.37e-32

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 119.62  E-value: 5.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  45 RMHLPVAPACNLQCNYCNRKFDCSNESRpgvsstlLTPEQAVVKVRQVAQAipQLSVVGIAGpGDPLANiARTFRTLELI 124
Cdd:COG0535    1 RLQIELTNRCNLRCKHCYADAGPKRPGE-------LSTEEAKRILDELAEL--GVKVVGLTG-GEPLLR-PDLFELVEYA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 125 REQlpDLKLCLSTNGLVLPDA-VDRLLDVGVDHVTVTINTLDAEIaaqiyawlwldGERYSGREAGeilIARQLEGVRRL 203
Cdd:COG0535   70 KEL--GIRVNLSTNGTLLTEElAERLAEAGLDHVTISLDGVDPET-----------HDKIRGVPGA---FDKVLEAIKLL 133
                        170
                 ....*....|...
gi 575523331 204 TAKGVLVKINSVL 216
Cdd:COG0535  134 KEAGIPVGINTVY 146
NifX_NifB cd00562
This CD represents a family of iron-molybdenum cluster-binding proteins that includes NifB, ...
343-450 4.08e-28

This CD represents a family of iron-molybdenum cluster-binding proteins that includes NifB, NifX, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme. This domain is a predicted small-molecule-binding domain (SMBD) with an alpha/beta fold that is present either as a stand-alone domain (e.g. NifX and NifY) or fused to another conserved domain (e.g. NifB) however, its function is still undetermined.The SCOP database suggests that this domain is most similar to structures within the ribonuclease H superfamily. This conserved domain is represented in two of the three major divisions of life (bacteria and archaea).


Pssm-ID: 238315  Cd Length: 102  Bit Score: 107.33  E-value: 4.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 343 LVAVASSRGDVIDCHFGHADRFYIYSLSAAGMVLVNERFTPKYCQGrddcepqDNAARFAAILELLADVKAVFCVRIGHT 422
Cdd:cd00562    1 KIAVASSDGGRVDQHFGRAPEFLIYEVEPGGIKLVEVRENPAACGG-------GGEGKLAARLLALEGCDAVLVGGIGGP 73
                         90       100
                 ....*....|....*....|....*...
gi 575523331 423 PWQQLEQEGIEPCVDGAWRPVSEVLPAW 450
Cdd:cd00562   74 AAAKLEAAGIKPIKAAEGGTIEEALEAL 101
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
50-223 8.74e-17

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 77.57  E-value: 8.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   50 VAPACNLQCNYCNRkfdcsNESRPGVSSTLLTPEQAVVKVRQVAQaiPQLSVVGIAGpGDPLANIARTFRTLELI-REQL 128
Cdd:pfam04055   1 ITRGCNLRCTYCAF-----PSIRARGKGRELSPEEILEEAKELKR--LGVEVVILGG-GEPLLLPDLVELLERLLkLELA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  129 PDLKLCLSTNGLVL-PDAVDRLLDVGVDHVTVTINTLDAEIAAQIyawlwldgerysgreAGEILIARQLEGVRRLTAKG 207
Cdd:pfam04055  73 EGIRITLETNGTLLdEELLELLKEAGLDRVSIGLESGDDEVLKLI---------------NRGHTFEEVLEALELLREAG 137
                         170
                  ....*....|....*..
gi 575523331  208 V-LVKINSVLIPGINDS 223
Cdd:pfam04055 138 IpVVTDNIVGLPGETDE 154
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
54-268 1.70e-15

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 75.99  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  54 CNLQCNYC-NRkfDCSNeSRPGVSSTLLTPEQAVVKVRQVAQAIpqLSVVGIA--GpGDPLANIARTFRTLELIREQlpD 130
Cdd:COG1180   31 CNLRCPYChNP--EISQ-GRPDAAGRELSPEELVEEALKDRGFL--DSCGGVTfsG-GEPTLQPEFLLDLAKLAKEL--G 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 131 LKLCLSTNGLVLPDAVDRLLDVgVDHVTVTINTLDAEIaaqiYawlwldgERYSGREAGEILiarqlEGVRRLTAKGVLV 210
Cdd:COG1180  103 LHTALDTNGYIPEEALEELLPY-LDAVNIDLKAFDDEF----Y-------RKLTGVSLEPVL-----ENLELLAESGVHV 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575523331 211 KINSVLIPGINDSgmagvSRALRASGAFIHNIMPLIA------RPEhgtvFGLNGQPEPDAETL 268
Cdd:COG1180  166 EIRTLVIPGLNDS-----EEELEAIARFIAELGDVIPvhllpfHPL----YKLEDVPPPSPETL 220
Nitro_FeMo-Co pfam02579
Dinitrogenase iron-molybdenum cofactor; This family contains several NIF (B, Y and X) proteins ...
351-451 2.96e-15

Dinitrogenase iron-molybdenum cofactor; This family contains several NIF (B, Y and X) proteins which are iron-molybdenum cofactors (FeMo-co) in the dinitrogenase enzyme which catalyzes the reduction of dinitrogen to ammonium. Dinitrogenase is a hetero-tetrameric (alpha(2)beta(2)) enzyme which contains the iron-molybdenum cofactor (FeMo-co) at its active site.


Pssm-ID: 460602  Cd Length: 93  Bit Score: 71.14  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  351 GDVIDCHFGHADRFYIYSLSAAGMVLVNERFTPkycqgrdDCEPQDNAARFAAILElLADVKAVFCVRIGHTPWQQLEQE 430
Cdd:pfam02579   2 GSRVDQHFGRAPYFAIYDVEEGGVEVVENREPA-------CAAGGGGGGKLAQLLA-DEGVDAVIVGGIGPNAAARLKAA 73
                          90       100
                  ....*....|....*....|.
gi 575523331  431 GIEPcVDGAWRPVSEVLPAWW 451
Cdd:pfam02579  74 GIKV-YKGAGGTVEEALEAYL 93
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
42-245 2.06e-13

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 71.10  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   42 RFAR----MHLPVAPACNLQCNYCNRKFDcsnESRPGVSSTLLTPEQavvkVRQVAQAIPQLSV--VGIAGpGDPL---- 111
Cdd:TIGR02666   4 RFGRridyLRISVTDRCNLRCVYCMPEGG---GLDFLPKEELLTFEE----IERLVRAFVGLGVrkVRLTG-GEPLlrkd 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  112 -ANIARTFRTLELIREqlpdlkLCLSTNGLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIyawlwldgerySGREAGe 190
Cdd:TIGR02666  76 lVELVARLAALPGIED------IALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKI-----------TRRGGR- 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 575523331  191 ilIARQLEGVRRLTAKGVL-VKINSVLIPGIND---SGMAGVSRALRASGAFIHnIMPL 245
Cdd:TIGR02666 138 --LEQVLAGIDAALAAGLEpVKLNTVVMRGVNDdeiVDLAEFAKERGVTLRFIE-LMPL 193
moaA PRK00164
GTP 3',8-cyclase MoaA;
42-222 7.31e-13

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 69.40  E-value: 7.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  42 RFARMH----LPVAPACNLQCNYCNRkfdcsNESRPGV-SSTLLTPEQavvkVRQVAQAIPQLSV--VGIAGpGDPL--A 112
Cdd:PRK00164  11 RFGRKFtylrISVTDRCNFRCTYCMP-----EGYLPFLpKEELLSLEE----IERLVRAFVALGVrkVRLTG-GEPLlrK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 113 NIARTFRTlelIREQLPDLKLCLSTNGLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIyawlwldgerysgreAGEIL 192
Cdd:PRK00164  81 DLEDIIAA---LAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAI---------------TGRDR 142
                        170       180       190
                 ....*....|....*....|....*....|.
gi 575523331 193 IARQLEGVRRLTAKGVL-VKINSVLIPGIND 222
Cdd:PRK00164 143 LDQVLAGIDAALAAGLTpVKVNAVLMKGVND 173
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
48-225 9.22e-13

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 66.97  E-value: 9.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  48 LPVAPACNLQCNYCNRKFDcsnESRPGVSSTLLTPEQAVVKVRQVAQAipqlSVVGIAGpGDPLANIARTfRTLELIREQ 127
Cdd:cd01335    1 LELTRGCNLNCGFCSNPAS---KGRGPESPPEIEEILDIVLEAKERGV----EVVILTG-GEPLLYPELA-ELLRRLKKE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 128 LPDLKLCLSTNG-LVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIYAwlwlDGERYSGReageiliarqLEGVRRLTAK 206
Cdd:cd01335   72 LPGFEISIETNGtLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRG----SGESFKER----------LEALKELREA 137
                        170
                 ....*....|....*....
gi 575523331 207 GVLVKINSVLIPGINDSGM 225
Cdd:cd01335  138 GLGLSTTLLVGLGDEDEED 156
NifX COG1433
Predicted Fe-Mo cluster-binding protein, NifX family [Posttranslational modification, protein ...
344-450 9.70e-13

Predicted Fe-Mo cluster-binding protein, NifX family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441042  Cd Length: 108  Bit Score: 64.52  E-value: 9.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 344 VAVASSRGDVIDCHFGHADRFYIYSLSAAGMVLVNERFTPKYCQGRDDCepqdnaarfaAILELLAD--VKAVFCVRIGH 421
Cdd:COG1433    3 IAIPSDGGSRVSPHFGRAPYFLIYDVEDGEIVLVEVIENPGEAGGGAGG----------LLAQLLAElgVDVVIAGGIGP 72
                         90       100
                 ....*....|....*....|....*....
gi 575523331 422 TPWQQLEQEGIEPCVDGAwRPVSEVLPAW 450
Cdd:COG1433   73 GALEALEAAGIKVYTGAE-GTVEEALEAY 100
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
54-222 6.21e-12

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 66.62  E-value: 6.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  54 CNLQCNYCNRKFDCSNESRpgvsSTLLTPEQavvkVRQVAQAIPQLSV--VGIAGpGDPL--ANIartfrtLELIRE--Q 127
Cdd:COG2896   24 CNFRCTYCMPEEGYQFLPK----EELLSFEE----IERLVRAFVELGVrkIRLTG-GEPLlrKDL------PELIARlaA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 128 LPDLK-LCLSTNGLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIyawlwldgerySGREAgeilIARQLEGVRRLTAK 206
Cdd:COG2896   89 LPGIEdLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRI-----------TRRDD----LDKVLAGIDAALAA 153
                        170
                 ....*....|....*..
gi 575523331 207 GVL-VKINSVLIPGIND 222
Cdd:COG2896  154 GLTpVKINAVVMRGVND 170
NifX cd00853
NifX belongs to a family of iron-molybdenum cluster-binding proteins that includes NifB, and ...
344-447 1.43e-09

NifX belongs to a family of iron-molybdenum cluster-binding proteins that includes NifB, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme. The protein is part of the nitrogen fixation gene cluster in nitrogen-fixing bacteria and has sequence similarity to other members of the cluster.


Pssm-ID: 238433  Cd Length: 102  Bit Score: 55.30  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 344 VAVASSRGDVIDCHFGHADRFYIYSLSAAGMVLVNERFTpkycqgrDDCEPQDNAARFAAILELLADVKAVFCVRIGHTP 423
Cdd:cd00853    2 VAFASSDLERVDAHFGSARRFAIYEVSPEGARLVEVRSF-------GGALEDGNEDKLAARLEALEDCAILYCAAIGGPA 74
                         90       100
                 ....*....|....*....|....
gi 575523331 424 WQQLEQEGIEPCVDGAWRPVSEVL 447
Cdd:cd00853   75 AARLVRAGIHPIKVPEGEPIAELL 98
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
48-255 1.08e-06

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 49.32  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331    48 LPVAPACNLQCNYCnrkfDCSNESRPGVSstllTPEQAVVK-----VRQVAQAIPqLSVVGIAGPGDPLANIARTFRTLE 122
Cdd:smart00729   5 YIITRGCPRRCTFC----SFPSLRGKLRS----RYLEALVReiellAEKGEKEGL-VGTVFIGGGTPTLLSPEQLEELLE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   123 LIREQLPDLK---LCLSTN-GLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIyawlwldGERYSGREAgeiliarqLE 198
Cdd:smart00729  76 AIREILGLAKdveITIETRpDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAI-------NRGHTVEDV--------LE 140
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   199 GVRRLTAKGVLvKINSVLI---PGINDSGMAGVSRALRASGAFIHNIMPLIARPehGTVF 255
Cdd:smart00729 141 AVELLREAGPI-KVSTDLIvglPGETEEDFEETLKLLKELGPDRVSIFPLSPRP--GTPL 197
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
2-222 1.11e-06

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 50.52  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331   2 TSCSSFSGGKACRPADDSALTPLVADKaaahpcysrHG-HHRFARMHLpvAPACNLQCNYCnrkfdcsnesRP--GV--- 75
Cdd:PLN02951  26 FSASSSYAADQVDPEASNPVSDMLVDS---------FGrRHNYLRISL--TERCNLRCQYC----------MPeeGVelt 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  76 -SSTLLTPEQAVVKVRQ-VAQAIPQLSVVGiagpGDPlaniarTFRT--LELIRE--QLPDLK-LCLSTNGLVLPDAVDR 148
Cdd:PLN02951  85 pKSHLLSQDEIVRLAGLfVAAGVDKIRLTG----GEP------TLRKdiEDICLQlsSLKGLKtLAMTTNGITLSRKLPR 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575523331 149 LLDVGVDHVTVTINTLDAEIAAQIyawlwldgERYSGREageiliaRQLEGVRR-LTAKGVLVKINSVLIPGIND 222
Cdd:PLN02951 155 LKEAGLTSLNISLDTLVPAKFEFL--------TRRKGHD-------RVLESIDTaIELGYNPVKVNCVVMRGFND 214
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
54-228 1.31e-06

Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function prediction only];


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 50.29  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  54 CNLQCNYCNrkFDCSNESRPGVSSTLLTPEQAVVKVRQVAQAIPQLSVVGIAGPGDPLANiartFRTLELIRE--QLPDL 131
Cdd:COG2100   46 CNLNCIFCS--VDAGPHSRTRQAEYIVDPEYLVEWFEKVARFKGKGVEAHIDGVGEPLLY----PYIVELVKGlkEIKGV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 132 KL-CLSTNGLVLP-DAVDRLLDVGVDHVTVTINTLDAEIAAQIYAWLWLDGERYsgREAGEIlIARQLegvrrltakGVL 209
Cdd:COG2100  120 KVvSMQTNGTLLSeKLIDELEEAGLDRINLSIDTLDPEKAKKLAGTKWYDVEKV--LELAEY-IARET---------KID 187
                        170
                 ....*....|....*....
gi 575523331 210 VKINSVLIPGINDSGMAGV 228
Cdd:COG2100  188 LLIAPVWLPGINDEDIPKI 206
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
50-165 1.76e-05

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 46.90  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  50 VAPACNLQCNYC--NRKFDCSNEsrpgvsstLLTPEqaVVK--VRQVAQAIPQLSVVGIA--GpGDPLANIARTFRTLEL 123
Cdd:COG0641    7 PTSRCNLRCSYCyySEGDEGSRR--------RMSEE--TAEkaIDFLIESSGPGKELTITffG-GEPLLNFDFIKEIVEY 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 575523331 124 IREQLP---DLKLCLSTNGLVLPDAVDRLLdvgVDH-VTVTInTLD 165
Cdd:COG0641   76 ARKYAKkgkKIRFSIQTNGTLLDDEWIDFL---KENgFSVGI-SLD 117
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
53-244 2.17e-05

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]; Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 45.95  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331  53 ACNLQCNYC--NRKFDCSNESRPgvsstLLTPEQAVVKVRQVAQAIPQ----LSVVGIAGPGDPlaniartfrTL----- 121
Cdd:COG0731   33 TCNFDCVYCqrGRTTDLTRERRE-----FDDPEEILEELIEFLRKLPEearePDHITFSGSGEP---------TLypnlg 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 122 ELIRE--QLPDLKLCLSTNG--LVLPDAVDRLLDvgVDHVTVTINTLDAEIAAQIyawlwldgerysGREAGEILIARQL 197
Cdd:COG0731   99 ELIEEikKLRGIKTALLTNGslLHRPEVREELLK--ADQVYPSLDAADEETFRKI------------NRPHPGLSWERII 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 575523331 198 EGVRRLTA--KGVLVkINSVLIPGINDSGmagvsRALRASGAFIHNIMP 244
Cdd:COG0731  165 EGLELFRKlyKGRTV-IETMLVKGINDSE-----EELEAYAELIKRINP 207
MTH1175 cd00851
This uncharacterized conserved protein belongs to a family of iron-molybdenum cluster-binding ...
344-450 5.80e-04

This uncharacterized conserved protein belongs to a family of iron-molybdenum cluster-binding proteins that includes NifX, NifB, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme. This domain is a predicted small-molecule-binding domain (SMBD) with an alpha/beta fold that is present either as a stand-alone domain (e.g. NifX and NifY) or fused to another conserved domain (e.g. NifB) however, its function is still undetermined.The SCOP database suggests that this domain is most similar to structures within the ribonuclease H superfamily. This conserved domain is represented in two of the three major divisions of life (bacteria and archaea).


Pssm-ID: 238431  Cd Length: 103  Bit Score: 39.18  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523331 344 VAVASSRGD-VIDCHFGHADRFYIYSLSaaGMVLVNERFTPKYcqgrddcEPQDNAARFAAILELLAD--VKAVFCVRIG 420
Cdd:cd00851    3 IAIPVSGNGgKVSPHFGRAPYFLIYDVE--TGKIKNVEVIENP-------AAHATGGAGGKAAEFLADegVDVVIVGGIG 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 575523331 421 HTPWQQLEQEGIEpCVDGAWRPVSEVLPAW 450
Cdd:cd00851   74 PRALNKLRNAGIK-VYKGAEGTVEEAIEAL 102
 
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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