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Conserved domains on  [gi|1170892729|emb|SLW51435|]
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nitrogenase cofactor biosynthesis protein NifB [Klebsiella variicola]

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: 609.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  22 APRVADKVAAHPCYSRSGHHRFARMHLPVAPACNLQCNYCNRKFDCSNESRPGVSSTLLTPEQAVLKVRQVAQAIPQLSV 101
Cdd:TIGR01290   2 NPAIAEKIAQHPCYSVEAHHYFARMHLAVAPACNIQCNYCNRKYDCANESRPGVVSELLTPEQALRKARQVAAEIPQLSV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 102 VGIAGPGDPLANMTRTFRTLELVRDQLPDLKLCLSTNGLMLPDAVDRLLEIGVDHVTVTINTLDADIAGQIYAWLWLDGE 181
Cdd:TIGR01290  82 VGIAGPGDPLANIGKTFQTLELVARQLPDVKLCLSTNGLMLPEHVDRLVDLGVGHVTITINAIDPAVGEKIYPWVWYEGE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 182 RYCGREAGEILIARQLEGVRRLTAAGVLVKINSVLIPGINDGGMAEVGRRLRESGAFIHNIMPLIARPEHGTVFGLNGQP 261
Cdd:TIGR01290 162 RYTGREAADLLIERQLEGLEKLTERGILVKVNSVLIPGINDEHLVEVSKQVKELGAFLHNVMPLISAPEHGTVYGLNGQR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 262 EPDAGMLAAIRSQCGEVMPQMTHCHQCRADAIGMLGEDRSQQFT-------RLPDPDSLPDWLPILHQ--RAELHASLAT 332
Cdd:TIGR01290 242 EPDPDELAALRDRLEMGTPQMRHCHQCRADAVGLLGEDRNADFPletfpadEVYDLANRPQYLQELERrrRQTLHASIVA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 333 QGESDADDACLVAVASRHGEVIDCHFGHADRFSIYSLSAAGMVLVGERFTPKYCRGEEECDpQENEARLAALLALLADVK 412
Cdd:TIGR01290 322 RGGSEEADECLVAVATKGGGAVNQHFGHADEFTIFSLSAAGVMLIGQRKIDRYCRGPDDCE-EDAAQNLDAIIELLSDCK 400
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1170892729 413 AVFCVRIGHTPWQQLELQGIEPQVDGAWRPVAE 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: 609.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  22 APRVADKVAAHPCYSRSGHHRFARMHLPVAPACNLQCNYCNRKFDCSNESRPGVSSTLLTPEQAVLKVRQVAQAIPQLSV 101
Cdd:TIGR01290   2 NPAIAEKIAQHPCYSVEAHHYFARMHLAVAPACNIQCNYCNRKYDCANESRPGVVSELLTPEQALRKARQVAAEIPQLSV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 102 VGIAGPGDPLANMTRTFRTLELVRDQLPDLKLCLSTNGLMLPDAVDRLLEIGVDHVTVTINTLDADIAGQIYAWLWLDGE 181
Cdd:TIGR01290  82 VGIAGPGDPLANIGKTFQTLELVARQLPDVKLCLSTNGLMLPEHVDRLVDLGVGHVTITINAIDPAVGEKIYPWVWYEGE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 182 RYCGREAGEILIARQLEGVRRLTAAGVLVKINSVLIPGINDGGMAEVGRRLRESGAFIHNIMPLIARPEHGTVFGLNGQP 261
Cdd:TIGR01290 162 RYTGREAADLLIERQLEGLEKLTERGILVKVNSVLIPGINDEHLVEVSKQVKELGAFLHNVMPLISAPEHGTVYGLNGQR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 262 EPDAGMLAAIRSQCGEVMPQMTHCHQCRADAIGMLGEDRSQQFT-------RLPDPDSLPDWLPILHQ--RAELHASLAT 332
Cdd:TIGR01290 242 EPDPDELAALRDRLEMGTPQMRHCHQCRADAVGLLGEDRNADFPletfpadEVYDLANRPQYLQELERrrRQTLHASIVA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 333 QGESDADDACLVAVASRHGEVIDCHFGHADRFSIYSLSAAGMVLVGERFTPKYCRGEEECDpQENEARLAALLALLADVK 412
Cdd:TIGR01290 322 RGGSEEADECLVAVATKGGGAVNQHFGHADEFTIFSLSAAGVMLIGQRKIDRYCRGPDDCE-EDAAQNLDAIIELLSDCK 400
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1170892729 413 AVFCVRIGHTPWQQLELQGIEPQVDGAWRPVAE 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 7.30e-34

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: 123.11  E-value: 7.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 343 LVAVASRHGEVIDCHFGHADRFSIYSLSAAGMVLVGERFTPKYCRGEeecDPQENEARLAALLALLADVKAVFCVRIGHT 422
Cdd:cd00852     1 LVAVASKGGGRVNQHFGHATEFQIYEVSGSGVKFVEHRKVDPYCGGG---DCGDEEDRLDAIIKLLSDCDAVLCAKIGDE 77
                          90       100
                  ....*....|....*....|....*....
gi 1170892729 423 PWQQLELQGIEPQVDGAWRPVAEVLPAWW 451
Cdd:cd00852    78 PKEKLEEAGIEVIEAYAGEYIEEALLELY 106
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
45-216 1.91e-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: 120.78  E-value: 1.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  45 RMHLPVAPACNLQCNYCNRKFDCSNESRpgvsstlLTPEQAVLKVRQVAQAipQLSVVGIAGpGDPLANmTRTFRTLELV 124
Cdd:COG0535     1 RLQIELTNRCNLRCKHCYADAGPKRPGE-------LSTEEAKRILDELAEL--GVKVVGLTG-GEPLLR-PDLFELVEYA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 125 RDQlpDLKLCLSTNGLMLPDA-VDRLLEIGVDHVTVTINTLDADIagqiyawlwldGERYCGREAGeilIARQLEGVRRL 203
Cdd:COG0535    70 KEL--GIRVNLSTNGTLLTEElAERLAEAGLDHVTISLDGVDPET-----------HDKIRGVPGA---FDKVLEAIKLL 133
                         170
                  ....*....|...
gi 1170892729 204 TAAGVLVKINSVL 216
Cdd:COG0535   134 KEAGIPVGINTVY 146
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
50-228 6.40e-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: 77.95  E-value: 6.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  50 VAPACNLQCNYCNRkfdcsNESRPGVSSTLLTPEQAVLKVRQVAQaiPQLSVVGIAGpGDPLANMTRTFRTLELV-RDQL 128
Cdd:pfam04055   1 ITRGCNLRCTYCAF-----PSIRARGKGRELSPEEILEEAKELKR--LGVEVVILGG-GEPLLLPDLVELLERLLkLELA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 129 PDLKLCLSTNGLML-PDAVDRLLEIGVDHVTVTINTLDADIAgqiyawlwldgeRYCGREAGeilIARQLEGVRRLTAAG 207
Cdd:pfam04055  73 EGIRITLETNGTLLdEELLELLKEAGLDRVSIGLESGDDEVL------------KLINRGHT---FEEVLEALELLREAG 137
                         170       180
                  ....*....|....*....|..
gi 1170892729 208 V-LVKINSVLIPGINDGGMAEV 228
Cdd:pfam04055 138 IpVVTDNIVGLPGETDEDLEET 159
moaA PRK00164
GTP 3',8-cyclase MoaA;
42-245 1.21e-14

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 74.79  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  42 RFARMH----LPVAPACNLQCNYCNRkfdcsNESRPGV-SSTLLTPEQavlkVRQVAQAIPQLSV--VGIAGpGDPL--A 112
Cdd:PRK00164   11 RFGRKFtylrISVTDRCNFRCTYCMP-----EGYLPFLpKEELLSLEE----IERLVRAFVALGVrkVRLTG-GEPLlrK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 113 NMTRTFRTLelvRDQLPDLKLCLSTNGLMLPDAVDRLLEIGVDHVTVTINTLDADIAGQIyawlwldgerycgreAGEIL 192
Cdd:PRK00164   81 DLEDIIAAL---AALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAI---------------TGRDR 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1170892729 193 IARQLEGVRRLTAAGVL-VKINSVLIPGINDGGMAEVGRRLRESGA---FIHnIMPL 245
Cdd:PRK00164  143 LDQVLAGIDAALAAGLTpVKVNAVLMKGVNDDEIPDLLEWAKDRGIqlrFIE-LMPT 198
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
48-255 2.20e-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: 48.55  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729   48 LPVAPACNLQCNYCnrkfDCSNESRPGVSSTLLTPEQAVLKVRQVAQAIPQLSVVGIAGPGDPLANMTRTFRTLELVRDQ 127
Cdd:smart00729   5 YIITRGCPRRCTFC----SFPSLRGKLRSRYLEALVREIELLAEKGEKEGLVGTVFIGGGTPTLLSPEQLEELLEAIREI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  128 LPDLK---LCLSTNGLML-PDAVDRLLEIGVDHVTVTINTLDADIAgqiyawlwldgeRYCGREAGeilIARQLEGVRRL 203
Cdd:smart00729  81 LGLAKdveITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVL------------KAINRGHT---VEDVLEAVELL 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1170892729  204 TAAGVLvKINSVLI---PGINDGGMAEVGRRLRESGAFIHNIMPLIARPehGTVF 255
Cdd:smart00729 146 REAGPI-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: 609.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  22 APRVADKVAAHPCYSRSGHHRFARMHLPVAPACNLQCNYCNRKFDCSNESRPGVSSTLLTPEQAVLKVRQVAQAIPQLSV 101
Cdd:TIGR01290   2 NPAIAEKIAQHPCYSVEAHHYFARMHLAVAPACNIQCNYCNRKYDCANESRPGVVSELLTPEQALRKARQVAAEIPQLSV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 102 VGIAGPGDPLANMTRTFRTLELVRDQLPDLKLCLSTNGLMLPDAVDRLLEIGVDHVTVTINTLDADIAGQIYAWLWLDGE 181
Cdd:TIGR01290  82 VGIAGPGDPLANIGKTFQTLELVARQLPDVKLCLSTNGLMLPEHVDRLVDLGVGHVTITINAIDPAVGEKIYPWVWYEGE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 182 RYCGREAGEILIARQLEGVRRLTAAGVLVKINSVLIPGINDGGMAEVGRRLRESGAFIHNIMPLIARPEHGTVFGLNGQP 261
Cdd:TIGR01290 162 RYTGREAADLLIERQLEGLEKLTERGILVKVNSVLIPGINDEHLVEVSKQVKELGAFLHNVMPLISAPEHGTVYGLNGQR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 262 EPDAGMLAAIRSQCGEVMPQMTHCHQCRADAIGMLGEDRSQQFT-------RLPDPDSLPDWLPILHQ--RAELHASLAT 332
Cdd:TIGR01290 242 EPDPDELAALRDRLEMGTPQMRHCHQCRADAVGLLGEDRNADFPletfpadEVYDLANRPQYLQELERrrRQTLHASIVA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 333 QGESDADDACLVAVASRHGEVIDCHFGHADRFSIYSLSAAGMVLVGERFTPKYCRGEEECDpQENEARLAALLALLADVK 412
Cdd:TIGR01290 322 RGGSEEADECLVAVATKGGGAVNQHFGHADEFTIFSLSAAGVMLIGQRKIDRYCRGPDDCE-EDAAQNLDAIIELLSDCK 400
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1170892729 413 AVFCVRIGHTPWQQLELQGIEPQVDGAWRPVAE 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 7.30e-34

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: 123.11  E-value: 7.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 343 LVAVASRHGEVIDCHFGHADRFSIYSLSAAGMVLVGERFTPKYCRGEeecDPQENEARLAALLALLADVKAVFCVRIGHT 422
Cdd:cd00852     1 LVAVASKGGGRVNQHFGHATEFQIYEVSGSGVKFVEHRKVDPYCGGG---DCGDEEDRLDAIIKLLSDCDAVLCAKIGDE 77
                          90       100
                  ....*....|....*....|....*....
gi 1170892729 423 PWQQLELQGIEPQVDGAWRPVAEVLPAWW 451
Cdd:cd00852    78 PKEKLEEAGIEVIEAYAGEYIEEALLELY 106
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
45-216 1.91e-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: 120.78  E-value: 1.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  45 RMHLPVAPACNLQCNYCNRKFDCSNESRpgvsstlLTPEQAVLKVRQVAQAipQLSVVGIAGpGDPLANmTRTFRTLELV 124
Cdd:COG0535     1 RLQIELTNRCNLRCKHCYADAGPKRPGE-------LSTEEAKRILDELAEL--GVKVVGLTG-GEPLLR-PDLFELVEYA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 125 RDQlpDLKLCLSTNGLMLPDA-VDRLLEIGVDHVTVTINTLDADIagqiyawlwldGERYCGREAGeilIARQLEGVRRL 203
Cdd:COG0535    70 KEL--GIRVNLSTNGTLLTEElAERLAEAGLDHVTISLDGVDPET-----------HDKIRGVPGA---FDKVLEAIKLL 133
                         170
                  ....*....|...
gi 1170892729 204 TAAGVLVKINSVL 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 5.96e-22

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: 90.00  E-value: 5.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 343 LVAVASRHGEVIDCHFGHADRFSIYSLSAAGMVLVGERFTPKYCRGeeecdpqENEARLAALLALLADVKAVFCVRIGHT 422
Cdd:cd00562     1 KIAVASSDGGRVDQHFGRAPEFLIYEVEPGGIKLVEVRENPAACGG-------GGEGKLAARLLALEGCDAVLVGGIGGP 73
                          90       100
                  ....*....|....*....|....*...
gi 1170892729 423 PWQQLELQGIEPQVDGAWRPVAEVLPAW 450
Cdd:cd00562    74 AAAKLEAAGIKPIKAAEGGTIEEALEAL 101
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
50-228 6.40e-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: 77.95  E-value: 6.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  50 VAPACNLQCNYCNRkfdcsNESRPGVSSTLLTPEQAVLKVRQVAQaiPQLSVVGIAGpGDPLANMTRTFRTLELV-RDQL 128
Cdd:pfam04055   1 ITRGCNLRCTYCAF-----PSIRARGKGRELSPEEILEEAKELKR--LGVEVVILGG-GEPLLLPDLVELLERLLkLELA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 129 PDLKLCLSTNGLML-PDAVDRLLEIGVDHVTVTINTLDADIAgqiyawlwldgeRYCGREAGeilIARQLEGVRRLTAAG 207
Cdd:pfam04055  73 EGIRITLETNGTLLdEELLELLKEAGLDRVSIGLESGDDEVL------------KLINRGHT---FEEVLEALELLREAG 137
                         170       180
                  ....*....|....*....|..
gi 1170892729 208 V-LVKINSVLIPGINDGGMAEV 228
Cdd:pfam04055 138 IpVVTDNIVGLPGETDEDLEET 159
moaA PRK00164
GTP 3',8-cyclase MoaA;
42-245 1.21e-14

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 74.79  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  42 RFARMH----LPVAPACNLQCNYCNRkfdcsNESRPGV-SSTLLTPEQavlkVRQVAQAIPQLSV--VGIAGpGDPL--A 112
Cdd:PRK00164   11 RFGRKFtylrISVTDRCNFRCTYCMP-----EGYLPFLpKEELLSLEE----IERLVRAFVALGVrkVRLTG-GEPLlrK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 113 NMTRTFRTLelvRDQLPDLKLCLSTNGLMLPDAVDRLLEIGVDHVTVTINTLDADIAGQIyawlwldgerycgreAGEIL 192
Cdd:PRK00164   81 DLEDIIAAL---AALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAI---------------TGRDR 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1170892729 193 IARQLEGVRRLTAAGVL-VKINSVLIPGINDGGMAEVGRRLRESGA---FIHnIMPL 245
Cdd:PRK00164  143 LDQVLAGIDAALAAGLTpVKVNAVLMKGVNDDEIPDLLEWAKDRGIqlrFIE-LMPT 198
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
54-272 2.23e-14

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 72.52  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  54 CNLQCNYC-NRkfDCSNeSRPGVSSTLLTPEQAVLKVRQVAQAIpqLSVVGIA--GpGDPLANMTRTFRTLELVRDQlpD 130
Cdd:COG1180    31 CNLRCPYChNP--EISQ-GRPDAAGRELSPEELVEEALKDRGFL--DSCGGVTfsG-GEPTLQPEFLLDLAKLAKEL--G 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 131 LKLCLSTNGLMLPDAVDRLLEiGVDHVTVTINTLDADIagqiYawlwldgERYCGREAGEILiarqlEGVRRLTAAGVLV 210
Cdd:COG1180   103 LHTALDTNGYIPEEALEELLP-YLDAVNIDLKAFDDEF----Y-------RKLTGVSLEPVL-----ENLELLAESGVHV 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1170892729 211 KINSVLIPGINDGG--MAEVGRRLRESGAFIH-NIMPliARPEhgtvFGLNGQPEPDAGMLAAIR 272
Cdd:COG1180   166 EIRTLVIPGLNDSEeeLEAIARFIAELGDVIPvHLLP--FHPL----YKLEDVPPPSPETLERAR 224
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
42-245 3.53e-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: 70.33  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  42 RFAR----MHLPVAPACNLQCNYCNRKFDcsnESRPGVSSTLLTPEQavlkVRQVAQAIPQLSV--VGIAGpGDPL---- 111
Cdd:TIGR02666   4 RFGRridyLRISVTDRCNLRCVYCMPEGG---GLDFLPKEELLTFEE----IERLVRAFVGLGVrkVRLTG-GEPLlrkd 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 112 -ANMTRTFRTLELVRDqlpdlkLCLSTNGLMLPDAVDRLLEIGVDHVTVTINTLDADIAGQIyawlwldgeryCGREAGe 190
Cdd:TIGR02666  76 lVELVARLAALPGIED------IALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKI-----------TRRGGR- 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1170892729 191 ilIARQLEGVRRLTAAGVL-VKINSVLIPGINDGGMAEVGRRLRESGA---FIHnIMPL 245
Cdd:TIGR02666 138 --LEQVLAGIDAALAAGLEpVKLNTVVMRGVNDDEIVDLAEFAKERGVtlrFIE-LMPL 193
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
48-244 7.00e-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: 67.36  E-value: 7.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  48 LPVAPACNLQCNYCNRkfdcSNESRPGVSSTLLTPEQAVLKVRQVAQAIPQLSVVGiagpGDPLANMTRTfRTLELVRDQ 127
Cdd:cd01335     1 LELTRGCNLNCGFCSN----PASKGRGPESPPEIEEILDIVLEAKERGVEVVILTG----GEPLLYPELA-ELLRRLKKE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 128 LPDLKLCLSTNGLML-PDAVDRLLEIGVDHVTVTINTLDADIAGQIyawlwldgerycgrEAGEILIARQLEGVRRLTAA 206
Cdd:cd01335    72 LPGFEISIETNGTLLtEELLKELKELGLDGVGVSLDSGDEEVADKI--------------RGSGESFKERLEALKELREA 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1170892729 207 GVLVKINSVLIPGINDGGMAEVGRRL-----RESGAFIHNIMP 244
Cdd:cd01335   138 GLGLSTTLLVGLGDEDEEDDLEELELlaefrSPDRVSLFRLLP 180
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
54-223 1.90e-11

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: 65.08  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  54 CNLQCNYCNRKFDCSNESRpgvsSTLLTPEQavlkVRQVAQAIPQLSV--VGIAGpGDPLanmtrtfrtlelVRDQLPDL 131
Cdd:COG2896    24 CNFRCTYCMPEEGYQFLPK----EELLSFEE----IERLVRAFVELGVrkIRLTG-GEPL------------LRKDLPEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 132 -----------KLCLSTNGLMLPDAVDRLLEIGVDHVTVTINTLDADIAGQIyawlwldgeryCGREAgeilIARQLEGV 200
Cdd:COG2896    83 iarlaalpgieDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRI-----------TRRDD----LDKVLAGI 147
                         170       180
                  ....*....|....*....|....
gi 1170892729 201 RRLTAAGVL-VKINSVLIPGINDG 223
Cdd:COG2896   148 DAALAAGLTpVKINAVVMRGVNDD 171
Nitro_FeMo-Co pfam02579
Dinitrogenase iron-molybdenum cofactor; This family contains several NIF (B, Y and X) proteins ...
351-451 2.84e-11

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: 59.58  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 351 GEVIDCHFGHADRFSIYSLSAAGMVLVGERftpkycrgEEECDPQENEARLAALLALLADVKAVFCVRIGHTPWQQLELQ 430
Cdd:pfam02579   2 GSRVDQHFGRAPYFAIYDVEEGGVEVVENR--------EPACAAGGGGGGKLAQLLADEGVDAVIVGGIGPNAAARLKAA 73
                          90       100
                  ....*....|....*....|.
gi 1170892729 431 GIEPqVDGAWRPVAEVLPAWW 451
Cdd:pfam02579  74 GIKV-YKGAGGTVEEALEAYL 93
NifX COG1433
Predicted Fe-Mo cluster-binding protein, NifX family [Posttranslational modification, protein ...
344-450 1.79e-09

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


Pssm-ID: 441042  Cd Length: 108  Bit Score: 54.89  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 344 VAVASRHGEVIDCHFGHADRFSIYSLSAAGMVLVGERFTPkycrGEEECdpqeNEARLAALLALLADVKAVFCVRIGHTP 423
Cdd:COG1433     3 IAIPSDGGSRVSPHFGRAPYFLIYDVEDGEIVLVEVIENP----GEAGG----GAGGLLAQLLAELGVDVVIAGGIGPGA 74
                          90       100
                  ....*....|....*....|....*..
gi 1170892729 424 WQQLELQGIEPqVDGAWRPVAEVLPAW 450
Cdd:COG1433    75 LEALEAAGIKV-YTGAEGTVEEALEAY 100
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
54-237 4.78e-07

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 51.45  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  54 CNLQCNYCNrkFDCSNESRPGVSSTLLTPEQAVLKVRQVAQAIPQLSVVGIAGPGDPLANmtrtFRTLELVR--DQLPDL 131
Cdd:COG2100    46 CNLNCIFCS--VDAGPHSRTRQAEYIVDPEYLVEWFEKVARFKGKGVEAHIDGVGEPLLY----PYIVELVKglKEIKGV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 132 KL-CLSTNGLMLP-DAVDRLLEIGVDHVTVTINTLDADIAGQIYAWLWLDGER------YCGREAG-EILIArqlegvrr 202
Cdd:COG2100   120 KVvSMQTNGTLLSeKLIDELEEAGLDRINLSIDTLDPEKAKKLAGTKWYDVEKvlelaeYIARETKiDLLIA-------- 191
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1170892729 203 ltaagvlvkinSVLIPGINDGGMAEVGRRLRESGA 237
Cdd:COG2100   192 -----------PVWLPGINDEDIPKIIEWALEIGA 215
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
48-255 2.20e-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: 48.55  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729   48 LPVAPACNLQCNYCnrkfDCSNESRPGVSSTLLTPEQAVLKVRQVAQAIPQLSVVGIAGPGDPLANMTRTFRTLELVRDQ 127
Cdd:smart00729   5 YIITRGCPRRCTFC----SFPSLRGKLRSRYLEALVREIELLAEKGEKEGLVGTVFIGGGTPTLLSPEQLEELLEAIREI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  128 LPDLK---LCLSTNGLML-PDAVDRLLEIGVDHVTVTINTLDADIAgqiyawlwldgeRYCGREAGeilIARQLEGVRRL 203
Cdd:smart00729  81 LGLAKdveITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVL------------KAINRGHT---VEDVLEAVELL 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1170892729  204 TAAGVLvKINSVLI---PGINDGGMAEVGRRLRESGAFIHNIMPLIARPehGTVF 255
Cdd:smart00729 146 REAGPI-KVSTDLIvglPGETEEDFEETLKLLKELGPDRVSIFPLSPRP--GTPL 197
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
3-222 9.16e-06

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 47.83  E-value: 9.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729   3 SCSSFSGGNACQSADASALAPRVADK----VAAHPCYSRSGHHRFARMHLpvAPACNLQCNYCnrkfdcsnesRP--GV- 75
Cdd:PLN02951   15 SFQLQEPGSSIFSASSSYAADQVDPEasnpVSDMLVDSFGRRHNYLRISL--TERCNLRCQYC----------MPeeGVe 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  76 ---SSTLLTPEQAVLKVRQ-VAQAIPQLSVVGiagpGDPlanmtrTFRT--LELVR--DQLPDLK-LCLSTNGLMLPDAV 146
Cdd:PLN02951   83 ltpKSHLLSQDEIVRLAGLfVAAGVDKIRLTG----GEP------TLRKdiEDICLqlSSLKGLKtLAMTTNGITLSRKL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1170892729 147 DRLLEIGVDHVTVTINTLDADIAGQIyawlwldgERYCGREageiliaRQLEGVRRLTAAGV-LVKINSVLIPGIND 222
Cdd:PLN02951  153 PRLKEAGLTSLNISLDTLVPAKFEFL--------TRRKGHD-------RVLESIDTAIELGYnPVKVNCVVMRGFND 214
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
50-165 5.66e-05

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 44.98  E-value: 5.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  50 VAPACNLQCNYC--NRKFDCSNEsrpgvsstLLTPEqaVLK--VRQVAQAIPQLSVVGIA--GpGDPLANMTRTFRTLEL 123
Cdd:COG0641     7 PTSRCNLRCSYCyySEGDEGSRR--------RMSEE--TAEkaIDFLIESSGPGKELTITffG-GEPLLNFDFIKEIVEY 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1170892729 124 VRDQLP---DLKLCLSTNGLMLPDAVDRLLeigVDH-VTVTInTLD 165
Cdd:COG0641    76 ARKYAKkgkKIRFSIQTNGTLLDDEWIDFL---KENgFSVGI-SLD 117
NifX cd00853
NifX belongs to a family of iron-molybdenum cluster-binding proteins that includes NifB, and ...
344-447 7.70e-05

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: 41.82  E-value: 7.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 344 VAVASRHGEVIDCHFGHADRFSIYSLSAAGMVLVGERFTPkycrgeeECDPQENEARLAALLALLADVKAVFCVRIGHTP 423
Cdd:cd00853     2 VAFASSDLERVDAHFGSARRFAIYEVSPEGARLVEVRSFG-------GALEDGNEDKLAARLEALEDCAILYCAAIGGPA 74
                          90       100
                  ....*....|....*....|....
gi 1170892729 424 WQQLELQGIEPQVDGAWRPVAEVL 447
Cdd:cd00853    75 AARLVRAGIHPIKVPEGEPIAELL 98
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
54-237 2.98e-03

SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the more distant in sequence.


Pssm-ID: 211974 [Multi-domain]  Cd Length: 353  Bit Score: 39.82  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729  54 CNLQCNYC--NRKFDCSNESRPGVSSTLLtpeQAVLKvrqvaQAIP-QLSVVGIAGpGDPLANmTRTFRTLELVRDQlpD 130
Cdd:TIGR04251  14 CNLKCRHCwiDPKYQGEGEQHPSLDPSLF---RSIIR-----QAIPlGLTSVKLTG-GEPLLH-PAIGEILECIGEN--N 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892729 131 LKLCLSTNGLML-PDAVDRLLEIGVDHVTVTINTLDADIAGqiyawlWLDGERYCgreageilIARQLEGVRRLTAAGVL 209
Cdd:TIGR04251  82 LQLSVETNGLLCtPQTARDLASCETPFVSVSLDGVDAATHD------WMRGVKGA--------FDKAVRGIHNLVEAGIH 147
                         170       180
                  ....*....|....*....|....*...
gi 1170892729 210 VKInSVLIPGINDGGMAEVGRRLRESGA 237
Cdd:TIGR04251 148 PQI-IMTVTRRNVGQMEQIVRLAESLGA 174
 
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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