|
Name |
Accession |
Description |
Interval |
E-value |
| nifD |
TIGR01282 |
nitrogenase molybdenum-iron protein alpha chain; Nitrogenase consists of alpha (NifD) and beta ... |
12-479 |
0e+00 |
|
nitrogenase molybdenum-iron protein alpha chain; Nitrogenase consists of alpha (NifD) and beta (NifK) subunits of the molybdenum-iron protein and an ATP-binding iron-sulfur protein (NifH). This model describes a large clade of NifD proteins, but excludes a lineage that contains putative NifD and NifD homologs from species with vanadium-dependent nitrogenases. [Central intermediary metabolism, Nitrogen fixation]
Pssm-ID: 162284 Cd Length: 466 Bit Score: 978.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 12 LIQEVLEVYPEKARKDRNKHLAVNDPAvTQSKKCIISNKKSQPGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQY 91
Cdd:TIGR01282 1 LIDEVLEVYPEKAAKKRSKHLVVNEPE-GKSDCGVKSNIKSVPGVMTIRGCAYAGSKGVVWGPIKDMVHISHGPVGCGQY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 92 SRAGRRNYYIGTTGVNAFVTMNFTSDFQEKDIVFGGDKKLAKLIDEVETLFPLNKGISVQSECPIGLIGDDIESVSKVKG 171
Cdd:TIGR01282 80 SWGGRRNYYKGETGVDNFGTMQFTSDFQEKDIVFGGDKKLKKAIDEIEELFPLNKGISIQSECPVGLIGDDIEAVAKKAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 172 AELSKTIVPVRCEGFRGVSQSLGHHIANDAVRDWVLGKRDEDTtFASTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVA 251
Cdd:TIGR01282 160 KELGKPVVPVRCEGFRGVSQSLGHHIANDAVRDWVLGKGDKEK-FEPTPYDVAIIGDYNIGGDAWESRILLEEIGLRVVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 252 QWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKTIESLRAIAAKFDESIQKKCEEVIAKY 331
Cdd:TIGR01282 239 QWSGDGTLNEMENAPKAKLNLIHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKIAESLRKIAEFFDDEIKEKAEEVIAKY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 332 KPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIGAYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEE 411
Cdd:TIGR01282 319 QPAVDAVIAKYRPRLEGKTVMLYVGGLRPRHVIGAFEDLGMEVIGTGYEFAHNDDYERTTKYMKDGTLIYDDVTHYEFEE 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 128239 412 FVKRIKPDLIGSGIKEKFIFQKMGIPFREMHSWDYSGPYHGFDGFAIFARDMDMTLNNPCWKKLQAPW 479
Cdd:TIGR01282 399 FVEKLKPDLVGSGIKEKYVFQKMGVPFRQMHSWDYSGPYHGYDGFAIFARDMDMALNSPTWKLIKAPW 466
|
|
| Nitrogenase_MoFe_alpha |
cd01976 |
Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar ... |
46-469 |
0e+00 |
|
Nitrogenase_MoFe_alpha_II: Nitrogenase MoFe protein, beta subunit. A group of proteins similar to the alpha subunit of the MoFe protein of the molybdenum (Mo-) nitrogenase. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. The Mo-nitrogenase is the most widespread and best characterized of these systems. Mo-nitrogenase consists of the MoFe protein (component 1) and the Fe protein (component 2). MoFe is an alpha2beta2 tetramer. Each alphabeta pair of MoFe contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction.
Pssm-ID: 238935 [Multi-domain] Cd Length: 421 Bit Score: 891.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 46 IISNKKSQPGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIGTTGVNAFVTMNFTSDFQEKDIVF 125
Cdd:cd01976 1 IKSNIKSVPGVMTIRGCAYAGSKGVVWGPIKDMVHISHGPVGCGQYSWATRRNYYRGETGVDNFGTMQFTTDFQEKDIVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 126 GGDKKLAKLIDEVETLFPLNKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGVSQSLGHHIANDAVRDW 205
Cdd:cd01976 81 GGDKKLAKAIDEAYELFPLNKGISVQSECPVGLIGDDIEAVARKASKELGIPVVPVRCEGFRGVSQSLGHHIANDAIRDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 206 VLGKRDEdttFASTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRH 285
Cdd:cd01976 161 ILGKRNE---FEPTPYDVNIIGDYNIGGDAWASRILLEEMGLRVVAQWSGDGTLNEMENAHKAKLNLIHCYRSMNYIARM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 286 MEEKYGIPWMEYNFFGPTKTIESLRAIAAKFDESIQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIG 365
Cdd:cd01976 238 MEEKYGIPWMEYNFFGPTKIAESLRKIAAYFDDEITAKTEEVIAEYKPAMEAVIAKYRPRLEGKTVMLYVGGLRPRHYIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 366 AYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREMHSWD 445
Cdd:cd01976 318 AYEDLGMEVVGTGYEFAHRDDYERTEVIPKEGTLLYDDVTHYELEEFVKRLKPDLIGSGIKEKYVFQKMGIPFRQMHSWD 397
|
410 420
....*....|....*....|....
gi 128239 446 YSGPYHGFDGFAIFARDMDMTLNN 469
Cdd:cd01976 398 YSGPYHGFDGFAIFARDMDMAINS 421
|
|
| N2-ase-Ialpha |
TIGR01862 |
nitrogenase component I, alpha chain; This model represents the alpha chain of all three ... |
27-474 |
0e+00 |
|
nitrogenase component I, alpha chain; This model represents the alpha chain of all three varieties (Mo-Fe, V-Fe, and Fe-Fe) of component I of nitrogenase. [Central intermediary metabolism, Nitrogen fixation]
Pssm-ID: 273838 Cd Length: 443 Bit Score: 754.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 27 DRNKHLAVNDPAVTQSKKCIISNKKSQPGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIGTTGV 106
Cdd:TIGR01862 1 DRKKHIVVKDPGETQSEKLPIANTKTIPGLMTERGCAYAGAKGVIGGPIKDMIHISHGPVGCTYYTWGTKRYPSDNENGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 107 NAFVTMNFTSDFQEKDIVFGGDKKLAKLIDEVETLFPLNKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGF 186
Cdd:TIGR01862 81 GAFLKYVFSTDMQESDIVFGGEKKLKKLIHEAFTEFPLIKAISVYATCPTGLIGDDIEAVAKEVSKEIGKDVVAVNCPGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 187 RGVSQSLGHHIANDAVRDWVLGKRDEDTTfasTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTP 266
Cdd:TIGR01862 161 AGVSQSKGHHIANIAVINDKVGTREKEIT---TEYDVNIIGEYNIGGDAWVMRIYLEEMGIQVVATFTGDGTYDEIRLMH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 267 KVKLNLVHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKTIESLRAIAAKFDesIQKKCEEVIAKYKPEWEAVVAKYRPRL 346
Cdd:TIGR01862 238 KAKLNLVHCARSANYIANELEERYGIPWMKIDFFGFTYTAESLRAIAAFFG--IEKRAEEVIAEEKAKWKPELDYYKERL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 347 EGKRVMLYIGGLRPRHVIG-AYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPDLIGSGI 425
Cdd:TIGR01862 316 QGKRVCLYIGGSRLWHWIGsAEEDLGMEVVAVGYEFAHEDDYEKTMKRMGEGTLLIDDPNELEFEEILEKLKPDIIFSGI 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 128239 426 KEKFIFQKMGIPFREMHSWDYsGPYHGFDGFAIFARDMDMTLNNPCWKK 474
Cdd:TIGR01862 396 KEKFVAQKLGVPYRQMHSYDN-GPYHGFEGFVNFARDMYNAIYNPCWKL 443
|
|
| Nitrogenase_MoFe_alpha_like |
cd01967 |
Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase ... |
54-469 |
0e+00 |
|
Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Three genetically distinct types of nitrogenase systems are known to exist: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase). These nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). This group contains the alpha subunit of component 1 of all three different forms. The most widespread and best characterized of these systems is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers having alpha and beta subunits similar to the alpha and beta subunits of MoFe. The role of the delta subunit is unknown. For MoFe, each alphabeta pair of subunits contains one P-cluster (located at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein is a homodimer which contains, a single [4Fe-4S] cluster from which electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo- nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction.
Pssm-ID: 238929 [Multi-domain] Cd Length: 406 Bit Score: 643.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 54 PGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIGTTGvnaFVTMNFTSDFQEKDIVFGGDKKLAK 133
Cdd:cd01967 1 PGPMTERGCCAFGGAGVVLGPIKDAVHIVHGPIGCAYYTWDTRRNLSSGENL---FYKYGFSTDMQEKDIVFGGEKKLKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 134 LIDEVETLFPLnKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGVSQSLGHHIANDAVRDWVLGKRDED 213
Cdd:cd01967 78 AIKEAYERFPP-KAIFVYSTCPTGLIGDDIEAVAKEASKELGIPVIPVNCEGFRGVSQSLGHHIANDAILDHLVGTKEPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 214 TTfasTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIP 293
Cdd:cd01967 157 EK---TPYDVNIIGEYNIGGDAWVIKPLLEELGIRVNATFTGDGTVDELRRAHRAKLNLVHCSRSMNYLAREMEERYGIP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 294 WMEYNFFGPTKTIESLRAIAAKFDesIQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIGAYEDLGME 373
Cdd:cd01967 234 YMEVNFYGFEDTSESLRKIAKFFG--DEEKAEEVIAEEEARIKPELEKYRERLKGKKVIIYTGGARSWHVIAALRELGME 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 374 VVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREMHSWDySGPYHGF 453
Cdd:cd01967 312 VVAAGYEFGHDDDYERIRKILDEGTLLVDDYNDLELEELVEKLKPDLILSGIKEKYVAQKLGIPFLDLHSER-NGPYAGY 390
|
410
....*....|....*.
gi 128239 454 DGFAIFARDMDMTLNN 469
Cdd:cd01967 391 EGFLNFARDIDTALNS 406
|
|
| NifD/CfbD |
COG2710 |
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and ... |
49-473 |
1.23e-159 |
|
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 442027 [Multi-domain] Cd Length: 416 Bit Score: 458.81 E-value: 1.23e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 49 NKKSQpGLMTIRGCAYAGSKgVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIgttgvnaFVTMNFTSDFQEKDIVFGGD 128
Cdd:COG2710 1 NRKAL-GVNPAKGCQPLGAK-LALLGIKDAIPLVHGSQGCAAYSRVTRGRHFK-------EPIPLFSTDMTEDDVVFGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 129 KKLAKLIDEVETLFpLNKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGvSQSLGHHIANDAVRDWVLG 208
Cdd:COG2710 72 KNLEEAIKNIIERY-KPKLIFVYTTCLTETIGDDIEAVIKEAREELGIPVVPVSTPGFVG-SHSTGYHIAVEAIVEQLVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 209 KRDEdttfaSTPYDVAIIGDYN-IGGDAWSSRILLEEMGLRCVAQWS-GDGSISEIELTPKVKLNLVHCYRSMNYISRHM 286
Cdd:COG2710 150 TGEP-----KTPGKINLIGGYNlIPGDLWEIKRLLEEMGLRVIALPDlGGTTVEEIADAGRAKLNLVLCSRSGNYAARYL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 287 EEKYGIPWME-YNFFGPTKTIESLRAIAAKFDESIqkkcEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIG 365
Cdd:COG2710 225 EEKYGIPYLEfVSPIGLEATDEFLRKLAELFGKPV----PEVIARERGRLVDALADYHFYLGGKKVAIYGDPDLLWGLAS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 366 AYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTL--LYDDVTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREMHS 443
Cdd:COG2710 301 FLLELGMEPVAAVTTTGSPEDYERIKELLEELPEgtVIDDGDLEELEELLKELKPDLLIGGSKGKYLARKLGIPLLRVGF 380
|
410 420 430
....*....|....*....|....*....|....*.
gi 128239 444 WDY------SGPYHGFDGFAIFARDMDMTLNNPCWK 473
Cdd:COG2710 381 PIYdrvglqRRPYAGYRGALNLLEDIANALLSPVWE 416
|
|
| Oxidoreductase_nitrogenase |
cd00316 |
The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. ... |
57-468 |
1.28e-152 |
|
The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. This group contains both alpha and beta subunits of component 1 of the three known genetically distinct types of nitrogenase systems: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium-dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase) and, both subunits of Protochlorophyllide (Pchlide) reductase and chlorophyllide (chlide) reductase. The nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). The most widespread and best characterized nitrogenase is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers whose alpha and beta subunits are similar to the alpha and beta subunits of MoFe. For MoFe, each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster from which, electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo at the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. Pchlide reductase and chlide reductase participate in the Mg-branch of the tetrapyrrole biosynthetic pathway. Pchlide reductase catalyzes the reduction of the D-ring of Pchlide during the synthesis of chlorophylls (Chl) and bacteriochlorophylls (BChl). Chlide-a reductase catalyzes the reduction of the B-ring of Chlide-a during the synthesis of BChl-a. The Pchlide reductase NB complex is a an N2B2 heterotetramer resembling nitrogenase FeMo, N and B proteins are homologous to the FeMo alpha and beta subunits respectively. The NB complex may serve as a catalytic site for Pchlide reduction and, the ZY complex as a site of chlide reduction, similar to MoFe for nitrogen reduction.
Pssm-ID: 238193 [Multi-domain] Cd Length: 399 Bit Score: 440.56 E-value: 1.28e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 57 MTIRGCAYAGSKGVVWGpIKDMIHISHGPVGCGQYSRAGRRNYYigttgvnAFVTMNFTSDFQEKDIVFGG-DKKLAKLI 135
Cdd:cd00316 2 NPAKGCAPLGAARVALG-IKDAIPLVHGPQGCAYFTRLTLRRHF-------KEPIPLFTTSMTEKDVVFGGgEKLLEAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 136 DEVETLFPlnKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGvSQSLGHHIANDAVRDWVLGKRDEDTT 215
Cdd:cd00316 74 NELKRYKP--KVIFVYTTCTTELIGDDIEAVAKEASKEIGIPVVPASTPGFRG-SQSAGYDAAVKAIIDHLVGTAEPEET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 216 fasTPYDVAIIGDYNI-GGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIPW 294
Cdd:cd00316 151 ---EPGSVNLIGGYNLgGGDLRELKRLLEEMGIRVNALFDGGTTVEELRELGNAKLNLVLCRESGLYLARYLEEKYGIPY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 295 MEYNFFGPTKTIESLRAIAAKFDesIQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIGAYEDLGMEV 374
Cdd:cd00316 228 ILINPIGLEATDAFLRKLAELFG--IEKEVPEVIARERARLLDALADYHEYLGGKKVAIFGDGDLLLALARFLLELGMEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 375 VGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREMHSWDYSGPYHGFD 454
Cdd:cd00316 306 VAAGTTFGHKADYERREELLGEGTEVVDDGDLEELEELIRELKPDLIIGGSKGRYIAKKLGIPLVRIGFPIHRRPYVGYE 385
|
410
....*....|....
gi 128239 455 GFAIFARDMDMTLN 468
Cdd:cd00316 386 GALNLAEEIANALL 399
|
|
| Nitrogenase_NifE_I |
cd01968 |
Nitrogenase_NifE_I: a subgroup of the NifE subunit of the NifEN complex: NifE forms an ... |
54-472 |
2.10e-128 |
|
Nitrogenase_NifE_I: a subgroup of the NifE subunit of the NifEN complex: NifE forms an alpha2beta2 tetramer with NifN. NifE and NifN are structurally homologous to nitrogenase MoFe protein alpha and beta subunits respectively. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of the MoFe protein. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to the NifEN complex where it is further processed to FeMoco. The NifEN bound precursor of FeMoco has been identified as a molybdenum-free, iron- and sulfur- containing analog of FeMoco. It has been suggested that this NifEN bound precursor also acts as a cofactor precursor in nitrogenase systems which require a cofactor other than FeMoco: i.e. iron-vanadium cofactor (FeVco) or iron only cofactor (FeFeco).
Pssm-ID: 238930 [Multi-domain] Cd Length: 410 Bit Score: 379.36 E-value: 2.10e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 54 PGLMTIRGCAYAGSKgVVWGPIKDMIHISHGPVGCGQYS---RAGRrnyyigTTGVNAFvTMNFTSDFQEKDIVFGGDKK 130
Cdd:cd01968 2 PGGVTQRGCVFDGAR-VVLMPITDAAHLVHGPIGCAGYSwdiRGSR------SSGSELY-RMGFSTDLSEKDVIFGGEKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 131 LAKLIDE-VETLFPlnKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGvSQSLGHHIANDAVRDWVLGK 209
Cdd:cd01968 74 LYKAILEiIERYHP--KAVFVYSTCVVALIGDDIDAVCKTASEKFGIPVIPVHSPGFVG-NKNLGNKLACEALLDHVIGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 210 RDEDTTfasTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEK 289
Cdd:cd01968 151 EEPEPL---TPYDINLIGEFNVAGELWGVKPLLEKLGIRVLASITGDSRVDEIRRAHRAKLNVVQCSKSMIYLARKMEEK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 290 YGIPWMEYNFFGPTKTIESLRAIAAKF-DESIQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIGAYE 368
Cdd:cd01968 228 YGIPYIEVSFYGIRDTSKSLRNIAELLgDEELIERTEELIAREEARLRPELAPYRARLEGKKAALYTGGVKSWSLVSALQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 369 DLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREmHSWDYSG 448
Cdd:cd01968 308 DLGMEVVATGTQKGTKEDYERIKELLGEGTVIVDDANPRELKKLLKEKKADLLVAGGKERYLALKLGIPFCD-INHERKH 386
|
410 420
....*....|....*....|....
gi 128239 449 PYHGFDGFAIFARDMDMTLNNPCW 472
Cdd:cd01968 387 PYAGYEGMLNFAKEVDLAVNSPVW 410
|
|
| nifE |
TIGR01283 |
nitrogenase molybdenum-iron cofactor biosynthesis protein NifE; This protein is part of the ... |
15-473 |
2.18e-128 |
|
nitrogenase molybdenum-iron cofactor biosynthesis protein NifE; This protein is part of the NifEN complex involved in biosynthesis of the molybdenum-iron cofactor used by the homologous NifDK complex of nitrogenase. In a few species, the protein is found as a NifEN fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]
Pssm-ID: 188126 [Multi-domain] Cd Length: 453 Bit Score: 380.55 E-value: 2.18e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 15 EVLEVYPEKArKDRNKHlavndpavTQSKKCIISNKKSQPGLMTIRGCAYAGSKgVVWGPIKDMIHISHGPVGCGQYSRA 94
Cdd:TIGR01283 4 KIAELLDEPA-CEHNKE--------KEEKGCKSGCANSLPGGATQRGCVFDGAR-IVLLPITDAAHLVHGPIGCAGSSWD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 95 GRRNYyigTTGVNAFvTMNFTSDFQEKDIVFGGDKKLAKLIDE-VETLFPlnKGISVQSECPIGLIGDDIESVSKVKGAE 173
Cdd:TIGR01283 74 IRGSR---SSGPELY-RLGFTTDLTEKDVIFGGEKKLFHAIREiVERYHP--PAVFVYSTCVPALIGDDLEAVCKAAAEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 174 LSKTIVPVRCEGFRGvSQSLGHHIANDAVRDWVLGKRDEDTT-FASTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQ 252
Cdd:TIGR01283 148 TGIPVIPVDSEGFYG-TKNLGNKLACDALLKHVIGTREPEPLpVGITVHDINLIGEFNVAGEFWHVLPLLEKLGIRVLAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 253 WSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKTIESLRAIAAKF-DESIQKKCEEVIAKY 331
Cdd:TIGR01283 227 ITGDSRYAEVQTAHRAKLNMVQCSKAMINLARKMEEKYGIPYFEGSFYGIEDTSKALRDIADLFgDPELLKRTEELIARE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 332 KPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIGAYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEE 411
Cdd:TIGR01283 307 EAKIRPALEPYRERLKGKKAAIYTGGVKSWSVVSALQDLGMEVVATGTQKSTEEDYARIRELMGEGTVMLDDANPRELLK 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 128239 412 FVKRIKPDLIGSGIKEKFIFQKMGIPFREmHSWDYSGPYHGFDGFAIFARDMDMTLNNPCWK 473
Cdd:TIGR01283 387 LLLEYKADILIAGGRERYTALKLGIPFLD-INHEREHPYAGYDGMVEFAREVDLTVESPIWQ 447
|
|
| Oxidored_nitro |
pfam00148 |
Nitrogenase component 1 type Oxidoreductase; |
62-468 |
2.34e-116 |
|
Nitrogenase component 1 type Oxidoreductase;
Pssm-ID: 395096 [Multi-domain] Cd Length: 398 Bit Score: 348.08 E-value: 2.34e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 62 CAYAGSKgVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYigttgvNAFVTMnFTSDFQEKDIVFGGDKKLAKLIDEVETL 141
Cdd:pfam00148 1 CAPAGAS-VALLGIKDAVPLVHGPQGCATYVRLLLTRHF------REPIPL-ATTSLTEKDVVFGGEENLKEAIKEVDKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 142 F-PlnKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGvSQSLGHHIANDAVRDWVLGKRDEDTtfastP 220
Cdd:pfam00148 73 YkP--KAIFVISTCLTETIGDDIEAVAREAREELGIPVIPVSTPGFVG-SHSTGYDVALEAIVRQLVGKKGEKE-----P 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 221 YDVAIIGDYNIG-GDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIPWMEY-N 298
Cdd:pfam00148 145 GTVNILGGFNLGpGDLREIKRLLEKLGIEVNPVFTGGTTLEDLRAAGNAAANLVLCPFSGEYAAEMLEEKFGVPYIRLgA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 299 FFGPTKTIESLRAIAAKFDESIqkkCEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIGAYEDLGMEVVGTG 378
Cdd:pfam00148 225 PIGLEATDRFLRALAKLFGKEV---APEVIARERGRLLDAMVDYHEYLAGKRVAIYGDPDLVLGLARFLLELGMEPVAVG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 379 YEFAHNDDYDRTMKEMGDST-LLYDDVTGYEFEEFVKRIKPDLIGSGIKEKFIFQKM-------GIPFREMHSWDYsGPY 450
Cdd:pfam00148 302 TGTGHPDDYERLKAELEEGDpEVIDGADLEELEELIKELKPDLLLGNSKGRYIARKLgiplvrvGFPIVDRHGLHR-RPY 380
|
410
....*....|....*...
gi 128239 451 HGFDGFAIFARDMDMTLN 468
Cdd:pfam00148 381 VGYRGALNLADRIANALL 398
|
|
| Nitrogenase_VFe_alpha |
cd01977 |
Nitrogenase_VFe_alpha -like: Nitrogenase VFe protein, alpha subunit like. This group contains ... |
54-473 |
3.08e-115 |
|
Nitrogenase_VFe_alpha -like: Nitrogenase VFe protein, alpha subunit like. This group contains proteins similar to the alpha subunits of, the VFe protein of the vanadium-dependent (V-) nitrogenase and the FeFe protein of the iron only (Fe-) nitrogenase Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. In addition to V- and Fe- nitrogenases there is a molybdenum (Mo)-dependent nitrogenase which is the most widespread and best characterized of these systems. These systems consist of component 1 (VFe protein, FeFe protein or, MoFe protein respectively) and, component 2 (Fe protein). MoFe is an alpha2beta2 tetramer, V-and Fe- nitrogenases are alpha2beta2delta2 hexamers. The alpha and beta subunits of VFe and FeFe are similar to the alpha and beta subunits of MoFe. For MoFe each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein which has a practically identical structure in all three systems, it contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction.
Pssm-ID: 238936 [Multi-domain] Cd Length: 415 Bit Score: 345.58 E-value: 3.08e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 54 PGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRnyYIGTTGvNAFVTMNFTSDFQEKDIVFGGDKKLAK 133
Cdd:cd01977 1 PGSLSERGCAYCGAKLVIGGVIKDVIHVIHGPVGCTYDTWHTKR--YPSDND-NFQLKYIWSTDMKESHVVFGGEKKLKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 134 LIDEVETLFPLNKGISVQSECPIGLIGDDIESVSKVKGAEL-SKTIVPVRCEGFRGVSQSLGHHIANDAVRDWVLGKRDE 212
Cdd:cd01977 78 NIIEAFKEFPDIKRMTVYTTCTTALIGDDIKAVAKEVMEELpDVDIFVCNAPGFAGPSQSKGHHVLNIAWINQKVGTVEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 213 DTTfasTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGI 292
Cdd:cd01977 158 EIT---SDYTINYIGDYNIQGDTEVLQKYFERMGIQVLSTFTGNGTYDDLRWMHRAKLNVVNCARSAGYIANELKKRYGI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 293 PWMEYNFFGPTKTIESLRAIAAKFdeSIQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIGAYED-LG 371
Cdd:cd01977 235 PRLDVDGFGFEYCAESLRKIGAFF--GIEDRAEAVIAEEMAKWKPELDWYKERLKGKKVCIWTGGPKLWHWTKVIEDeLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 372 MEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREMHSWdYSGPYH 451
Cdd:cd01977 313 MQVVAMSSKFGHQEDFEKVIARGGEGTIYIDDPNELEFFEILEMLKPDIILTGPRVGELVKKLHVPYVNIHAY-HNGPYM 391
|
410 420
....*....|....*....|..
gi 128239 452 GFDGFAIFARDMDMTLNNPCWK 473
Cdd:cd01977 392 GFEGFVNLARDMYNAIYSPIWQ 413
|
|
| alt_nitrog_alph |
TIGR01284 |
nitrogenase alpha chain; This model represents the alpha chains of various forms of the ... |
27-472 |
1.00e-108 |
|
nitrogenase alpha chain; This model represents the alpha chains of various forms of the nitrogen-fixing enzyme nitrogenase: vanadium-iron, iron-iron, and molybdenum-iron. Most examples of NifD, the molybdenum-iron type nitrogenase alpha chain, are excluded from this model and described instead by equivalog model TIGR01282. It appears by phylogenetic and UPGMA trees that this model represents a distinct clade of NifD homologs, in which arose several molybdenum-independent forms. [Central intermediary metabolism, Nitrogen fixation]
Pssm-ID: 188127 Cd Length: 457 Bit Score: 330.65 E-value: 1.00e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 27 DRNKHLAVNDPAVTQSKKCIISNKKSQPGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRnyYIgTTGV 106
Cdd:TIGR01284 11 ERKKHIYVKKQGEPEGDFLPACNTTTIPGCMSERGCAFCGAKGVIGGAIKDAIHVIHGPVGCTYDTWHTKR--YP-TDNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 107 NAFVTMNFTSDFQEKDIVFGGDKKLAKLIDEVETLFPLNKGISVQSECPIGLIGDDIESVSKVKGAEL-SKTIVPVRCEG 185
Cdd:TIGR01284 88 KFNLKYITGTDLKESHVVFGGEKKLKRCILEAFREFPEIKRMYTYATCTTALIGDDIDAIAREVMEEIpDVDVFAINAPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 186 FRGVSQSLGHHIANDAVRDWVLGKRDEDTTfasTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELT 265
Cdd:TIGR01284 168 FAGPSQSKGHHVANITWINDKVGTAEPEIT---TEYDVNLIGEYNIQGDLWVLKKYFERMGIQVLSTFTGNGCYDELRWM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 266 PKVKLNLVHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKTIESLRAIAAKFdeSIQKKCEEVIAKYKPEWEAVVAKYRPR 345
Cdd:TIGR01284 245 HRAKLNVVRCARSANYIANELEERYGIPRLDIDFFGFEYCAKNLRKIGEFF--GIEERAERVIEEEMAKWKPELDWYKER 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 346 LEGKRVMLYIGGLRPRHVIGAYED-LGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPDLIGSG 424
Cdd:TIGR01284 323 LRGKKVWVWSGGPKLWHWPRPLEDeLGMEVVAVSTKFGHEDDYEKIIARVREGTVIIDDPNELELEEIIEKYKPDIILTG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 128239 425 IKEKFIFQKMGIPFREMHSWdYSGPYHGFDGFAIFARDMDMTLNNPCW 472
Cdd:TIGR01284 403 IREGELAKKLGVPYINIHSY-HNGPYIGFEGFVNLARDMYNAIYNPVW 449
|
|
| PRK14477 |
PRK14477 |
bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional |
50-492 |
3.46e-103 |
|
bifunctional nitrogenase molybdenum-cofactor biosynthesis protein NifE/NifN; Provisional
Pssm-ID: 172952 [Multi-domain] Cd Length: 917 Bit Score: 329.01 E-value: 3.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 50 KKSQPGLMTIRGCAYAGSKgVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIGTTgvnaFVTMNFTSDFQEKDIVFGGDK 129
Cdd:PRK14477 24 KKSEPGEGAERSCAYDGAR-VVLMPITDVIHLVHGPIACAGNSWDNRGARSSGSQ----LYRRGFTTEMLENDVIFGGEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 130 KLAKLIDEVETLFPlNKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGvSQSLGHHIANDAVRDWVLGK 209
Cdd:PRK14477 99 KLYRAILELAERYQ-PKAVFVYATCVTALTGDDVEAVCKAAAEKVGIPVIPVNTPGFIG-DKNIGNRLAGEALLKHVIGT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 210 RDEDTTfasTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEK 289
Cdd:PRK14477 177 AEPEVT---TPYDINLIGEYNIAGDLWGMLPLFDRLGIRVLSCISGDAKFEELRYAHRAKLNVIICSKSLTNLARKMEKR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 290 YGIPWMEYNFFGPTKTIESLRAIAAKFDES--------IQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPR 361
Cdd:PRK14477 254 YGIPYLEESFYGMTDTAKALRDIARELDDAggglekrvLQDRVEKLIAEEEAKCRAALAPYRARLEGKRVVLFTGGVKTW 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 362 HVIGAYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREM 441
Cdd:PRK14477 334 SMVNALRELGVEVLAAGTQNSTLEDFARMKALMHKDAHIIEDTSTAGLLRVMREKMPDLIVAGGKTKFLALKTRTPFLDI 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 128239 442 HSwDYSGPYHGFDGFAIFARDMDMTLNNPCWKKLQ--APWEASEGAEKVAASA 492
Cdd:PRK14477 414 NH-GRSHPYAGYEGMVTFARQLDLTVNNPIWPALRapAPWEKGAGELRADLAL 465
|
|
| Nitrogenase_VnfE_like |
cd01972 |
Nitrogenase_VnfE_like: VnfE subunit of the VnfEN complex_like. This group in addition to VnfE ... |
60-421 |
7.58e-34 |
|
Nitrogenase_VnfE_like: VnfE subunit of the VnfEN complex_like. This group in addition to VnfE contains a subset of the alpha subunit of the nitrogenase MoFe protein and NifE-like proteins. The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of MoFe protein of the molybdenum(Mo)-nitrogenase. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to NifEN where it is further processed to FeMoco. VnfEN may similarly be a scaffolding protein for the iron-vanadium cofactor (FeVco) of the vanadium-dependent (V)-nitrogenase. NifE and NifN are essential for the Mo-nitrogenase, VnfE and VnfN are not essential for the V-nitrogenase. NifE and NifN can substitute when the vnfEN genes are inactivated.
Pssm-ID: 238932 [Multi-domain] Cd Length: 426 Bit Score: 132.16 E-value: 7.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 60 RGCAYAGSKGVVWGpIKDMIHISHGPVGCGQYSRAGRRNYYIGTTGVNAFVTMnFTSDFQEKDIVFGGDKKLAKLIDEVE 139
Cdd:cd01972 8 SMCKFWTAFCILSG-IRDAVVVQHGPIGCAAGQSFFNRLYRCGEMRRGLNEPV-LSTNLTEKDVVFGGEKKLEDTIKEAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 140 TLF-PlnKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGVSQSLGHhianDAVRDWVLGKRDEDTTFAS 218
Cdd:cd01972 86 SRYkP--KAIFVATSCATGIIGDDVESVVEELEDEIGIPVVALHCEGFKGKHWRSGF----DAAFHGILRHLVPPQDPTK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 219 TPYDVAIIG-----DYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIP 293
Cdd:cd01972 160 QEDSVNIIGlwggpERTEQEDVDEFKRLLNELGLRVNAIIAGGCSVEELERASEAAANVTLCLDLGYYLGAALEQRFGVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 294 WME----YNFFGptkTIESLRAIAakfdeSIQKKCEEVIAKYKPEWEAV---VAKYRPRLEGKRVMLYIGGLrPRHVIGA 366
Cdd:cd01972 240 EIKapqpYGIEA---TDKWLREIA-----KVLGMEAEAEAVIEREHERVapeIEELRKALKGKKAIVETGAA-YGHLLIA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 128239 367 Y--EDLGMEVVGTgYEFAHNDDYDRTMKE---MGDSTLLYDDVTGY--------EFEEFVKRIKPDLI 421
Cdd:cd01972 311 VlrELGFGEVPVV-LVFHHDPTYDRGDSEkdlLEHGVDPEIDITKYtvsngqyyQFYNLLKRVKPDFI 377
|
|
| Nitrogenase_VnfN_like |
cd01971 |
Nitrogenase_vnfN_like: VnfN subunit of the VnfEN complex-like. This group in addition to VnfN ... |
61-330 |
4.25e-26 |
|
Nitrogenase_vnfN_like: VnfN subunit of the VnfEN complex-like. This group in addition to VnfN contains a subset of the beta subunit of the nitrogenase MoFe protein and NifN-like proteins. The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of MoFe protein of the molybdenum(Mo)-nitrogenase. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to NifEN where it is further processed to FeMoco. VnfEN may similarly be a scaffolding protien for the iron-vanadium cofactor (FeVco) of the vanadium-dependent (V)-nitrogenase. NifE and NifN are essential for the Mo-nitrogenase, VnfE and VnfN are not essential for the V-nitrogenase. NifE and NifN can substitute when the vnfEN genes are inactivated.
Pssm-ID: 238931 [Multi-domain] Cd Length: 427 Bit Score: 110.20 E-value: 4.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 61 GCAYAGSKGVVWGpIKDMIHISHGPVGCG--QYSRAGRRNYYIGTtGVNAFVTMNFTsdfqEKDIVFGGDKKLAKLIDEV 138
Cdd:cd01971 8 GCALGGALYTVSA-IPRAVPIIHSGPGCAskQSGAVAFGNGYQGG-GYGVAPCTNAT----ETEIVFGGEDRLRELIKST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 139 ETLFPlNKGISVQSECPIGLIGDDIESVSKvKGAELSKTIVPVRCEGFRGvSQSLGHHIANDAVRDWVLGKRDED----- 213
Cdd:cd01971 82 LSIID-ADLFVVLTGCIAEIIGDDVGAVVS-EFQEGGAPIVYLETGGFKG-NNYAGHEIVLKAIIDQYVGQSEEKepglv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 214 TTFASTPY-DVAIIGDYniggdAWSSRiLLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGI 292
Cdd:cd01971 159 NLWGPVPYqDPFWRGDL-----EEIKR-VLEGIGLKVNILFGPESNGEELRSIPKAQFNLVLSPWVGLEFAQHLEEKYGQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 128239 293 PWMEYNFF--GPTKTIESLRAIAAKFDESIQkKCEEVIAK 330
Cdd:cd01971 233 PYIHSPTLpiGAKATAEFLRQVAKFAGIEKA-KVEAFIKA 271
|
|
| Nitrogenase_MoFe_beta_like |
cd01965 |
Nitrogenase_MoFe_beta_like: Nitrogenase MoFe protein, beta subunit_like. The nitrogenase ... |
75-461 |
6.69e-18 |
|
Nitrogenase_MoFe_beta_like: Nitrogenase MoFe protein, beta subunit_like. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. This group contains the beta subunits of component 1 of the three known genetically distinct types of nitrogenase systems: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium-dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase). These nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). The most widespread and best characterized of these systems is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers having alpha and beta subunits similar to the alpha and beta subunits of MoFe. For MoFe, each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains, a single [4Fe-4S] cluster from which electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during N2-reduction and, ethane as a minor product during acetylene reduction
Pssm-ID: 238927 [Multi-domain] Cd Length: 428 Bit Score: 85.69 E-value: 6.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 75 IKDMIHISHGPVGCGQYSRAGRRNYYIGTTGVNafvtmnfTSDFQEKDIVFGGDKKLAKLIDEVETLFPlNKGISVQSEC 154
Cdd:cd01965 20 IEGCMPLVHGSQGCSSFARVLFTRHFKEPIPIA-------STSMTEDAAVFGGEDNLIEALKNLLSRYK-PDVIGVLTTC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 155 PIGLIGDDIESV---SKVKGAELSKT-IVPVRCEGFRGvSQSLGHHIANDAVRDWVLGKRDED--------TTFASTPYD 222
Cdd:cd01965 92 LTETIGDDVAGFikeFRAEGPEPADFpVVYASTPSFKG-SHETGYDNAVKAIIEQLAKPSEVKkngkvnllPGFPLTPGD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 223 VAIIGDyniggdawssriLLEEMGLRCVA--------------QWS----GDGSISEIELTPKVKLNLVHCYRSMNYISR 284
Cdd:cd01965 171 VREIKR------------ILEAFGLEPIIlpdlsdsldghltdGYSpltkGGTTLEEIRDAGNAKATIALGEYSGRKAAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 285 HMEEKYGIPWMEYNF-FGPTKTIESLRAIAAKFDesiqkkcEEVIAKYKPEweavvakyRPRLE-----------GKRVM 352
Cdd:cd01965 239 ALEEKFGVPYILFPTpIGLKATDEFLRALSKLSG-------KPIPEELERE--------RGRLLdamldshfylgGKRVA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 353 LYiggLRPRHVIGAYE---DLGMEVVgtgYEFAHNDD---YDRTMKEMGDSTLLYDDVTG---YEFEEFVKRIKPDL-IG 422
Cdd:cd01965 304 IA---GDPDLLLGLSRfllEMGAEPV---AAVTGTDNppfEKRMELLASLEGIPAEVVFVgdlWDLESLAKEEPVDLlIG 377
|
410 420 430
....*....|....*....|....*....|....*....
gi 128239 423 SGiKEKFIFQKMGIPFREMhswdysgpyhgfdGFAIFAR 461
Cdd:cd01965 378 NS-HGRYLARDLGIPLVRV-------------GFPIFDR 402
|
|
| Pchlide_reductase_B |
cd01981 |
Pchlide_reductase_B: B protein of the NB protein complex of Protochlorophyllide (Pchlide) ... |
64-471 |
1.24e-08 |
|
Pchlide_reductase_B: B protein of the NB protein complex of Protochlorophyllide (Pchlide)_reductase. Pchlide reductase catalyzes the reductive formation of chlorophyllide (chlide) from protochlorophyllide (pchlide) during biosynthesis of chlorophylls and bacteriochlorophylls. This group contains both the light-independent Pchlide reductase (DPOR) and light-dependent Pchlide reductase (LPOR). Angiosperms contain only LPOR, cyanobacteria, algae and gymnosperms contain both DPOR and LPOR, primitive anoxygenic photosynthetic bacteria contain only DPOR. NB is structurally similar to the FeMo protein of nitrogenase, forming an N2B2 heterotetramer. N and B are homologous to the FeMo alpha and beta subunits respectively. Also in common with nitrogenase in vitro DPOR activity requires ATP hydrolysis and dithoionite or ferredoxin as electron donor. The NB protein complex may serve as a catalytic site for Pchlide reduction similar to MoFe for nitrogen reduction.
Pssm-ID: 238939 [Multi-domain] Cd Length: 430 Bit Score: 57.01 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 64 YAGSK--GV--VWGPIKDMIHISHGPvgcgqysragrrnyyIGTTGVNAFVTM-----NFT----SDFQEKDIVFGGDKK 130
Cdd:cd01981 8 YEGPAhiGTlrVASSFKNVHAVMHAP---------------LGDDYFNVMRSMlererDFTpvtaSTVDRHVLARGSQEK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 131 LaklideVETLFPLNK-----GISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFR--------GVSQSLGHHI 197
Cdd:cd01981 73 V------VENITRKDKeekpdLIVLTPTCTSSILQEDLQNFVRAAGLSSKSPVLPLDVNHYRvnelqaadETFEQLVRFY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 198 ANDAVRDWVLGKRDEDTTfastpydVAIIGDYNIG----GDAWSSRILLEEMGLR--CVAQWsgDGSISEIELTPKVKLN 271
Cdd:cd01981 147 AEKARPQGTPREKTEKPS-------VNLIGPSSLGfhnrHDCRELKRLLHTLGIEvnVVIPE--GASVDDLNELPKAWFN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 272 LVHcYRSMnYIS--RHMEEKYGIPWMEYNFFGPTKTIESLRAIaaKFDESIQKKCEEV-IAKYK---PEWEAVVAkYRPR 345
Cdd:cd01981 218 IVP-YREY-GLSaaLYLEEEFGMPSVKITPIGVVATARFLREI--QELLGIQIIPELVnVEPYIdsqTRWVSQSA-RSSR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 346 ------LEGKRVMLYIGGLrprHVIGA----YEDLGMEVVGTGYEFAHNDDYDRT-MKEMGDSTLLYDDVTgyEFEEFVK 414
Cdd:cd01981 293 sidsqnLTGKRAFVFGDAT---HVAAAtrilAREMGFRVVGAGTYCKEDAKWFREqATGYCDEALITDDHT--EVGDMIA 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 128239 415 RIKPDLIGSGIKEKFIFQKMGIP----FREMHSWDYSG---PYHGFDGfaifARDMDMTLNNPC 471
Cdd:cd01981 368 RTEPELIFGTQMERHIGKRLDIPcaviSAPVHIQNFPLgyrPFLGYEG----TNVIADTVYNSL 427
|
|
| PRK02910 |
PRK02910 |
ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit B; |
241-455 |
5.08e-06 |
|
ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit B;
Pssm-ID: 235085 [Multi-domain] Cd Length: 519 Bit Score: 49.11 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 241 LLEEMGL--RCVAQWSGdgSISEIELTPKVKLNLVhCYRSMNYIS-RHMEEKYGIPWMEYNFFGPTKTIESLRAIA---- 313
Cdd:PRK02910 183 LLATLGIdvNVVAPLGA--SPADLKRLPAAWFNVV-LYREIGESAaRYLEREFGQPYVKTVPIGVGATARFIREVAelln 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 314 ---AKFDESIQkkcEEVIAKYKPEWEA--VVAKYrprLEGKRVMLYIGGlrpRHVIGA----YEDLGMEVVGTG-YEFAH 383
Cdd:PRK02910 260 ldgADLEAFIL---DGLSAPSRLPWFSrsVDSTY---LTGKRVFVFGDA---THAVAAarilSDELGFEVVGAGtYLRED 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 384 NDDYDRTMKEMGDSTLLYDDVTgyEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPF----REMHSWD----YSgPYHGFDG 455
Cdd:PRK02910 331 ARWVRAAAKEYGDEALITDDYL--EVEDAIAEAAPELVLGTQMERHSAKRLGIPCavisAPTHVQDfparYS-PQMGFEG 407
|
|
| Nitrogenase_NifN_2 |
cd03466 |
Nitrogenase_nifN_2: A subgroup of the NifN subunit of the NifEN complex: NifN forms an ... |
75-437 |
4.86e-05 |
|
Nitrogenase_nifN_2: A subgroup of the NifN subunit of the NifEN complex: NifN forms an alpha2beta2 tetramer with NifE. NifN and nifE are structurally homologous to nitrogenase MoFe protein beta and alpha subunits respectively. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of the MoFe protein. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to the NifEN complex where it is further processed to FeMoco. The nifEN bound precursor of FeMoco has been identified as a molybdenum-free, iron- and sulfur- containing analog of FeMoco. It has been suggested that this nifEN bound precursor also acts as a cofactor precursor in nitrogenase systems which require a cofactor other than FeMoco: i.e. iron-vanadium cofactor (FeVco) or iron only cofactor (FeFeco). This group also contains the Clostidium fused NifN-NifB protein.
Pssm-ID: 239549 [Multi-domain] Cd Length: 429 Bit Score: 45.84 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 75 IKDMIHISHGPVGCGQYSRagrrnYYIGTTGVNAfvtMNF-TSDFQEKDIVFGGDKKLAKLIDEVETLF-PlnKGISVQS 152
Cdd:cd03466 23 IEGCMPLLHGSQGCSTYIR-----RHMARHYNEP---VDIaSSSLNEETTVYGGEKNLKKGLKNVIEQYnP--EVIGIAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 153 ECPIGLIGDDIESVSKVKGAELS---KTIVPVRCEGFRGvSQSLGHHIANDAVRDWVLGKRDEDTTfastpydVAIIGDY 229
Cdd:cd03466 93 TCLSETIGEDVPRIIREFREEVDdsePKIIPASTPGYGG-THVEGYDTAVRSIVKNIAVDPDKIEK-------INVIAGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 230 NIGGDAWSSRILLEEMGLRCV-----------AQW-------SGDGSISEIELTPKVKLNLVHCYRSMNYIS--RHMEEK 289
Cdd:cd03466 165 MSPADIREIKEILREFGIEYIllpdtsetldgPFWgeyhrlpSGGTPISEIKGMGGAKATIELGMFVDHGLSagSYLEEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 290 YGIPWMEYNF-FGPTKTIESLRAIAAKFDESIQKKCEEVIAKYkpeWEAVV--AKYrprLEGKRVMLYIgglRPRHVIGA 366
Cdd:cd03466 245 FGIPNYRLPLpIGLRATDEFMSLLSKLTGKPIPEKYTRERGRL---LDAMIdaHKY---NFGRKAAIYG---EPDFVVAI 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 128239 367 YE---DLGM--EVVGTGYEFAH-NDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPD-LIGSGiKEKFIFQKMGIP 437
Cdd:cd03466 316 TRfvlENGMvpVLIATGSESKKlKEKLEEDLKEYVEKCVILDGADFFDIESYAKELKIDvLIGNS-YGRRIAEKLGIP 392
|
|
| Nitrogenase_VFe_beta_like |
cd01973 |
Nitrogenase_VFe_beta -like: Nitrogenase VFe protein, beta subunit like. This group contains ... |
62-206 |
6.50e-05 |
|
Nitrogenase_VFe_beta -like: Nitrogenase VFe protein, beta subunit like. This group contains proteins similar to the beta subunits of the VFe protein of the vanadium-dependent (V-) nitrogenase. Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. In addition to V-nitrogenase there is a molybdenum (Mo)-dependent nitrogenase and an iron only (Fe-) nitrogenase. The Mo-nitrogenase is the most widespread and best characterized of these systems. These systems consist of component 1 (VFe protein, FeFe protein or, MoFe protein respectively) and, component 2 (Fe protein). MoFe is an alpha2beta2 tetramer, V-and Fe- nitrogenases are alpha2beta2delta2 hexamers. The alpha and beta subunits of VFe and FeFe are similar to the alpha and beta subunits of MoFe. For MoFe each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein which has a practically identical structure in all three systems, it contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction.
Pssm-ID: 238933 [Multi-domain] Cd Length: 454 Bit Score: 45.17 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128239 62 CAYAGSKGVVWGpIKDMIHISHGPVGCGQYSRAGRRNYYigttgvnafvTMNF---TSDFQEKDIVFGGDKKLAKLIDEV 138
Cdd:cd01973 13 CQPAGAQYAGIG-IKDCIPLVHGGQGCTMFVRLLFAQHF----------KENFdiaSSSLHEDSAVFGGAKRVEEGVLVL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 128239 139 ETLFPLNKGISVQSECPIGLIGDDIESVSKVKGAELSKT-------IVPVRCEGFRGvSQSLGHhiaNDAVRDWV 206
Cdd:cd01973 82 ARRYPDLRVIPIITTCSTEIIGDDIEGVIRKLNEALKEEfpdrevhLIPVHTPSFKG-SMVTGY---DEAVRSVV 152
|
|
| |
