|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
50-814 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 1647.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 50 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQRVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPP 129
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 130 RYGWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 209
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 210 YLLLSKPAKGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLV 289
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 290 ETYFADVPVEAYKTLTSLKSVTGFGFDLVRGTKTLELIK-GGFPSGKYLFAGVVDGRNIWANNLASSLDTLKALEGIVGK 368
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 369 DKLVVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKALAGQQDEAFFSANAAAQASRKSSPRVTNEAVQ 448
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 449 KAAVALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQE 528
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 529 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLT 608
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 609 GPVTILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVE 688
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 689 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKML 768
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 743796608 769 AVLESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKLGSAQ 814
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASAK 766
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
55-809 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes the cobalamin-independent methionine synthase. A family of uncharacterized archaeal proteins is homologous to the C-terminal region of this family. That family is excluded from this model but, along with this family, belongs to pfam01717. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273583 [Multi-domain] Cd Length: 750 Bit Score: 1284.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 55 VGYPRMGPKRELKFALESFWDGKSSAEDLQRVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRYGWN 134
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 135 GGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLS 214
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 215 KpakGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVETYFA 294
Cdd:TIGR01371 161 K---AVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 295 DVPvEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKALEGIVGKdkLVVS 374
Cdd:TIGR01371 238 SVG-DALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 375 TSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKALAGQQDEAFFSANAAAQA--SRKSSPRVTNEAVQKAAV 452
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAiaARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 453 ALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDI 532
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 533 DVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVT 612
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 613 ILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVEDTTQ 692
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 693 IHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLE 772
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 743796608 773 SNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTK 809
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
52-416 |
0e+00 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the N-terminal barrel, and a few single-barrel sequences most similar to the N-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239428 [Multi-domain] Cd Length: 360 Bit Score: 594.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 52 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQRVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRY 131
Cdd:cd03312 2 THILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPERF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 132 GWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYL 211
Cdd:cd03312 82 GALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 212 LLSKPAKGvekSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVET 291
Cdd:cd03312 162 KLSKAKGG---GFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 292 YFADVpVEAYKTLTSLkSVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKALEGIVGkDKL 371
Cdd:cd03312 239 YFGSL-GENLDLLASL-PVDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 743796608 372 VVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKA 416
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
481-804 |
0e+00 |
|
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent methionine synthases or 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferases, EC:2.1.1.14 from bacteria and plants. Plants are the only higher eukaryotes that have the required enzymes for methionine synthesis. This enzyme catalyzes the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to homocysteine. The aligned region makes up the carboxy region of the approximately 750 amino acid protein except in some hypothetical archaeal proteins present in the family, where this region corresponds to the entire length. This domain contains the catalytic residues of the enzyme.
Pssm-ID: 366771 [Multi-domain] Cd Length: 323 Bit Score: 556.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 481 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 560
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 561 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 640
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 641 EDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVEDTTQIHTHMCYSNFNDIIHSIIDMDADVITIE 720
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 721 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTRKYAEVKPALSNMV 800
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 743796608 801 AAAK 804
Cdd:pfam01717 320 DAAK 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
481-807 |
2.80e-144 |
|
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 427.63 E-value: 2.80e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 481 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 560
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 561 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 640
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 641 EDLEKAGITVIQIDEAALREGLPlrksehAFYLNWAVHSFRITNCGVEDtTQIHTHMCYSNFNDIIHSIIDMDADVITIE 720
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 721 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTR----KYAEVKPAL 796
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKL 312
|
330
....*....|.
gi 743796608 797 SNMVAAAKHLR 807
Cdd:COG0620 313 RNMVAFAREVR 323
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
50-814 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 1647.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 50 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQRVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPP 129
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 130 RYGWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 209
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 210 YLLLSKPAKGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLV 289
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 290 ETYFADVPVEAYKTLTSLKSVTGFGFDLVRGTKTLELIK-GGFPSGKYLFAGVVDGRNIWANNLASSLDTLKALEGIVGK 368
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 369 DKLVVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKALAGQQDEAFFSANAAAQASRKSSPRVTNEAVQ 448
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 449 KAAVALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQE 528
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 529 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLT 608
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 609 GPVTILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVE 688
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 689 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKML 768
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 743796608 769 AVLESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKLGSAQ 814
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASAK 766
|
|
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
49-812 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1351.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 49 AMASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQRVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVP 128
Cdd:PRK05222 1 MIKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 129 PRYGWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPV 208
Cdd:PRK05222 81 ERFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDPDTQFKLTSNKLLDEFEEAKALGINTKPVLLGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 209 SYLLLSKpakGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVL 288
Cdd:PRK05222 161 TFLWLSK---SKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 289 VETYFADVpVEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKALEGIVgk 368
Cdd:PRK05222 238 LATYFGSL-NDALDLLASLP-VDGLHLDLVRGPEQLAALLKYFPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKV-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 369 DKLVVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKALAGQQD--EAFFSANAAAQASRKSSPRVTNEA 446
Cdd:PRK05222 314 DRLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGavAEALAANRAAIAARRTSPRVHNPA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 447 VQKAAVALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKI 526
Cdd:PRK05222 394 VRARLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 527 QEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGM 606
Cdd:PRK05222 474 QEELGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGM 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 607 LTGPVTILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCG 686
Cdd:PRK05222 554 LTGPVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSG 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 687 VEDTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEK 766
Cdd:PRK05222 634 VKDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFED-FGYPNEIGPGVYDIHSPRVPSVEEIEELLRK 712
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 743796608 767 MLAVLESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKLGS 812
Cdd:PRK05222 713 ALEVIPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELAA 758
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
55-809 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes the cobalamin-independent methionine synthase. A family of uncharacterized archaeal proteins is homologous to the C-terminal region of this family. That family is excluded from this model but, along with this family, belongs to pfam01717. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273583 [Multi-domain] Cd Length: 750 Bit Score: 1284.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 55 VGYPRMGPKRELKFALESFWDGKSSAEDLQRVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRYGWN 134
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 135 GGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLS 214
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 215 KpakGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVETYFA 294
Cdd:TIGR01371 161 K---AVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 295 DVPvEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKALEGIVGKdkLVVS 374
Cdd:TIGR01371 238 SVG-DALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 375 TSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKALAGQQDEAFFSANAAAQA--SRKSSPRVTNEAVQKAAV 452
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAiaARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 453 ALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDI 532
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 533 DVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVT 612
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 613 ILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVEDTTQ 692
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 693 IHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLE 772
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 743796608 773 SNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTK 809
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
52-416 |
0e+00 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the N-terminal barrel, and a few single-barrel sequences most similar to the N-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239428 [Multi-domain] Cd Length: 360 Bit Score: 594.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 52 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQRVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRY 131
Cdd:cd03312 2 THILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPERF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 132 GWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYL 211
Cdd:cd03312 82 GALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 212 LLSKPAKGvekSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVET 291
Cdd:cd03312 162 KLSKAKGG---GFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 292 YFADVpVEAYKTLTSLkSVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKALEGIVGkDKL 371
Cdd:cd03312 239 YFGSL-GENLDLLASL-PVDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 743796608 372 VVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKA 416
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
481-804 |
0e+00 |
|
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent methionine synthases or 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferases, EC:2.1.1.14 from bacteria and plants. Plants are the only higher eukaryotes that have the required enzymes for methionine synthesis. This enzyme catalyzes the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to homocysteine. The aligned region makes up the carboxy region of the approximately 750 amino acid protein except in some hypothetical archaeal proteins present in the family, where this region corresponds to the entire length. This domain contains the catalytic residues of the enzyme.
Pssm-ID: 366771 [Multi-domain] Cd Length: 323 Bit Score: 556.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 481 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 560
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 561 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 640
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 641 EDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVEDTTQIHTHMCYSNFNDIIHSIIDMDADVITIE 720
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 721 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTRKYAEVKPALSNMV 800
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 743796608 801 AAAK 804
Cdd:pfam01717 320 DAAK 323
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
52-366 |
1.16e-174 |
|
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal domains of cobalamin-independent synthases together define a catalytic cleft in the enzyme. The N-terminal domain is thought to bind the substrate, in particular, the negatively charged polyglutamate chain. The N-terminal domain is also thought to stabilize a loop from the C-terminal domain.
Pssm-ID: 400526 [Multi-domain] Cd Length: 310 Bit Score: 504.81 E-value: 1.16e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 52 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQRVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRY 131
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 132 GWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYL 211
Cdd:pfam08267 81 GNDGGLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELDKDTEFKLNSNKLLDEYKEAKALGIETKPVLLGPVTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 212 LLSkpaKGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVET 291
Cdd:pfam08267 161 KLS---KGKGGSFDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLAT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743796608 292 YFADVpVEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKALEGIV 366
Cdd:pfam08267 238 YFGSV-ADALELLASLP-VAGLGLDLVRGPENLAALKKGFPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
482-804 |
1.45e-147 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the C-terminal barrel, and a few single-barrel sequences most similar to the C-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Sidechains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239427 [Multi-domain] Cd Length: 332 Bit Score: 436.27 E-value: 1.45e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 482 PTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTan 561
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 562 GWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTK-RPMKGMLTGPVTILNWSFVRN---DQPRFETCYQIALAIK 637
Cdd:cd03311 79 GWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 638 DEVEDLEKAGITVIQIDEAALREGLPLRK-SEHAFYLNWAVHSFRitncGVEDTTQIHTHMCYSNF----------NDII 706
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLEPdDLAADYLKWANEALA----DRPDDTQIHTHICYGNFrstwaaeggyEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 707 HSIIDMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKT 786
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKE-LPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFAT 313
|
330
....*....|....*...
gi 743796608 787 RKYAEVKPALSNMVAAAK 804
Cdd:cd03311 314 RERGNALTKLENMVKAAL 331
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
481-807 |
2.80e-144 |
|
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 427.63 E-value: 2.80e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 481 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 560
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 561 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 640
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 641 EDLEKAGITVIQIDEAALREGLPlrksehAFYLNWAVHSFRITNCGVEDtTQIHTHMCYSNFNDIIHSIIDMDADVITIE 720
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 721 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTR----KYAEVKPAL 796
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKL 312
|
330
....*....|.
gi 743796608 797 SNMVAAAKHLR 807
Cdd:COG0620 313 RNMVAFAREVR 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
51-406 |
1.98e-85 |
|
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 274.71 E-value: 1.98e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 51 ASHIVGYPRMgpkRELKFALESFWDGKSSAEDLQRVAADLRSSIWKQMSDAGIKFIPSNTFSCYDqvldttaMLGAVPPR 130
Cdd:COG0620 3 TTTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYD-------MVGYFPER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 131 ygWNGgeigfdvyFSMARgNASVpamemtKWFDTNYHYiVPELGPEVNFSyaSHKAVNEYKEAKAL-GVDTVPVLVGPVS 209
Cdd:COG0620 73 --LDG--------YAFAR-NGWV------EWFDTNYHY-VPEITGDVSFS--GPMTVEEFRFAKSLtGKPVKPVLPGPVT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 210 YLLLSKpakgVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLV 289
Cdd:COG0620 133 LLLLSK----VRDYKDREELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKIHL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 290 ETYFADVPvEAYKTLTSLKsVTGFGFDLVRGT-KTLELIKgGFPSGKYLFAGVVDGRNIWANNLASSLDTLKALEGIVGK 368
Cdd:COG0620 209 HTCYGGYE-DILEALAALP-VDGIHLEFVRSRaGLLEPLK-ELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPP 285
|
330 340 350
....*....|....*....|....*....|....*...
gi 743796608 369 DKLVVSTSCSLLHTAVDLvNEPKLDKEIKSWLAFAAQK 406
Cdd:COG0620 286 ERLWVSPDCGLKHRPVDL-TREEAWAKLRNMVAFAREV 322
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
477-811 |
3.98e-80 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 260.68 E-value: 3.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 477 NLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGF 556
Cdd:PRK04326 5 KLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 557 AFtaNGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMT-KRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALA 635
Cdd:PRK04326 85 KF--YGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFNEYYKDKEELVFDLAKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 636 IKDEVEDLEKAGITVIQIDEAAlregLPLRKSEHAfylnWAVHSFRITNCGVEdtTQIHTHMCYSNFNDIIHSIIDMDAD 715
Cdd:PRK04326 163 INEEIKNLVEAGAKYIQIDEPA----LATHPEDVE----IAVEALNRIVKGIN--AKLGLHVCYGDYSRIAPYILEFPVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 716 VITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTRKYAEVKPA 795
Cdd:PRK04326 233 QFDLEFANGNYKLLDLLKE-YGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPREIAYQK 311
|
330
....*....|....*.
gi 743796608 796 LSNMVAAAKHLRTKLG 811
Cdd:PRK04326 312 LVNMVKATREVREELD 327
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
482-804 |
5.70e-36 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers both the N-and C-terminal barrel, and some single-barrel sequences, mostly from Archaea. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239426 [Multi-domain] Cd Length: 321 Bit Score: 138.71 E-value: 5.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 482 PTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERnDMVEYFGEQLSGFAFtan 561
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DMIGRFLEVLVDLET--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 562 GWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQP--RFETCYQIALAIKDE 639
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPdaYEDLAKSLAEFLREQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 640 VEDLEKAGITVIQIDEAALREGLPLRKSEHAfYLNWAVHSFRITNCGvedttQIHTHMCYsnfNDIIHSIIDMDADVITI 719
Cdd:cd03310 157 VKELKNRGIVVVQIDEPSLGAVGAGAFEDLE-IVDAALEEVSLKSGG-----DVEVHLCA---PLDYEALLELGVDVIGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 720 ENSRSD-------EKLLSVFREGVKYGAGIGPGVYDIHSPR--IPSEEEIADRIEKMLAVLESnILWVNPDCGLKTRKYA 790
Cdd:cd03310 228 DAAALPskyledlKKLLRIGVRTLILGLVVTDNEAKGRNAWkeIERLEKLVRRLEEPGEVLDE-ILYLTPDCGLAFLPPQ 306
|
330
....*....|....
gi 743796608 791 EVKPALSNMVAAAK 804
Cdd:cd03310 307 EARRKLALLAEAAR 320
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
482-804 |
6.12e-31 |
|
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases, as well as cobalamine (B12) independent methionine synthases. Despite their sequence similarities, members of this family have clearly different functions. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane, and methionine synthases transfer a methyl group from a folate cofactor to L-homocysteine in a reaction requiring zinc.
Pssm-ID: 238261 [Multi-domain] Cd Length: 306 Bit Score: 123.76 E-value: 6.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 482 PTTTIGSFPQTMDLRRvrreykaKKISEQNYVEAIKEEINKVVKiQEELDIDVLVHGEpernDMVEYFGEQLsgfaftaN 561
Cdd:cd00465 1 PVQCEGQTGIMEASET-------MAISEEPGETSKAEWGITLVE-PEEIPLDVIPVHE----DDVLKVAQAL-------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 562 GWVQSYGSRCVKPPIIYGDV-SRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRND---------QPRFETCYQ 631
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEEdPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSMGDalmalyerpEAMHELIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 632 IALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEhaFYLNWAVHSFR-ITNCGVEDTTQIHTHMCYSNfNDIIHSII 710
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGPK--MFKKFALPAYKkVAEYKAAGEVPIVHHSCYDA-ADLLEEMI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 711 DMDADVITIENSRSDEKLLsvfREGVKYGAGIGPGVYDIHSPRipSEEEIADRIEKMLAVLESNIlWVNPDCGLKTRKYA 790
Cdd:cd00465 219 QLGVDVISFDMTVNEPKEA---IEKVGEKKTLVGGVDPGYLPA--TDEECIAKVEELVERLGPHY-IINPDCGLGPDSDY 292
|
330
....*....|....
gi 743796608 791 EvKPALSNMVAAAK 804
Cdd:cd00465 293 K-PEHLRAVVQLVD 305
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
480-807 |
6.20e-31 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 123.56 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 480 ILPTTTIGSFPQTmdlRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPeRNDMVEYFGEQLSGFAft 559
Cdd:PRK00957 1 IMITTVVGSYPVV---KGEPETLKDKIKGFFGLYDPYKPAIEEAVADQVKAGIDIISDGQV-RGDMVEIFASNMPGFD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 560 angwvqsyGSRCVkppiiyGDVSRP-KAMTV----FWSSMAQSMT-KRPMKGMLTGPVTILNWSFVRN---DQPRFETCY 630
Cdd:PRK00957 75 --------GKRVI------GRVEPPaKPITLkdlkYAKKVAKKKDpNKGVKGIITGPSTLAYSLRVEPfysDNKDEELIY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 631 QIALAIKDEVEDLEKAGITVIQIDEAALREGLP-LRKSEHAfyLNWAVHSFRITNCgvedttqihTHMCySNFNDIIHSI 709
Cdd:PRK00957 141 DLARALRKEAEALEKAGVAMIQIDEPILSTGAYdLEVAKKA--IDIITKGLNVPVA---------MHVC-GDVSNIIDDL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 710 IDMDADVITIENSRSDEKlLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLK--TR 787
Cdd:PRK00957 209 LKFNVDILDHEFASNKKN-LEILEEKDLIGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDCGMRmlPR 287
|
330 340
....*....|....*....|
gi 743796608 788 KYAEVKpaLSNMVAAAKHLR 807
Cdd:PRK00957 288 DVAFEK--LKNMVEAAREIR 305
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
478-810 |
1.49e-24 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 105.77 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 478 LPILPTTTIGSF--PQ--TMDLRRVRREYKAKKISEQNYVEAIKeeinkvVKIQEELDiDVLVHGEPERNDMVEYFGEQL 553
Cdd:PRK01207 1 MAALITQEIGSFrkPEylSREFHKIEGTDKFYELAERATLETLD------VFENAGLD-NIGIGGEMFRWEMYEHPAERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 554 SGFAFTanGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIA 633
Cdd:PRK01207 74 KGIIFY--GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEFA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 634 LAIKDEVEDLEKAGITV-------IQIDEAAlreglplrKSEHAFYLNWAVHSFRITNCGVEDttQIHTHMCYSNFNDII 706
Cdd:PRK01207 152 RIINEELKDIKSAWDRKspgrkleIQIDEPA--------TTTHPDEMDIVVDSINKSVYGIDN--EFSIHVCYSSDYRLL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 707 HSII-DMDADVITIENSRSDE----------------KLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLA 769
Cdd:PRK01207 222 YDRIpELNIDGYNLEYSNRDTlepgtsdekrpgfqdlKYFAEHNESLQRKKFIGLGVTDVHIDYVEPVKLIEDRIRYALK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 743796608 770 VL-ESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKL 810
Cdd:PRK01207 302 IIkDPELVRLNPDCGLRTRSREIGEQKLRNMVAAKNNILKEL 343
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
479-811 |
2.14e-20 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 93.21 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 479 PILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAF 558
Cdd:PRK09121 1 TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 559 TANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKD 638
Cdd:PRK09121 81 EKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 639 EVEDLEKAGITVIQIDEAALreglplrkseHAFY---LNWAVHSFRITNCGVEDTTQIhtHMCYS--------------- 700
Cdd:PRK09121 161 EAKELEAAGVDIIQFDEPAF----------NVFFdevNDWGVAALERAIEGLKCETAV--HICYGygikantdwkktlgs 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 701 ---NFNDIIHSIIDMDADVITIE--NSRSDEKLLSVFRegvkyGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNI 775
Cdd:PRK09121 229 ewrQYEEAFPKLQKSNIDIISLEchNSRVPMDLLELIR-----GKKVMVGAIDVASDTIETPEEVADTLRKALQFVDADK 303
|
330 340 350
....*....|....*....|....*....|....*...
gi 743796608 776 LWVNPDCGLK--TRKYAEVKpaLSNMVAAAKHLRTKLG 811
Cdd:PRK09121 304 LYPCTNCGMAplSRDVARGK--LNALSAGAEIVRRELA 339
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
54-346 |
2.50e-08 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 56.67 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 54 IVG-YPRmgPKRELKfALESFWDGKSSAEDLQRVAADLRSSIWKQMSDAGIKFIpsntfscydqvldTTAMlgavpprYG 132
Cdd:PRK08575 7 LVGsYPR--PVKLAK-VISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYT-------------TDGL-------FR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 133 WNggEIgFDVYFSMARGnasVPAMEMTKWFDTNYHYIVPELGPEVNFsyashKAVNEY----KEAKALGVDTVP------ 202
Cdd:PRK08575 64 WD--DI-FDPTISFISG---VEKGGLQRFYDNNFYYRQPVIKEKINL-----KEENPYlqwlESAREIKEEVSLesklka 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 203 VLVGPVSYLLLSKPakgvEKSFSLLSLIDKILPVYQEVLAELKaAGASWIQFDEPKLVM-DLGAHELQAFTHAYSALEAS 281
Cdd:PRK08575 133 VLPGPLTYAVLSDN----EYYKNLIELMEDYASVVNSLIKELS-SVVDAVEIHEPSIFAkGIKRDTLEKLPEVYKTMAKN 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743796608 282 LSGLNVLVeTYFADVPVEAYKTLTSLkSVTGFGFDLVRGTKTLELIKGGFpSGKYLFAGVVDGRN 346
Cdd:PRK08575 208 VNIEKHLM-TYFEINNLKRLDILFSL-PVTYFGIDVIENLKKLGRVYTYL-KGRKVYLGILNARN 269
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
486-775 |
1.84e-03 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 41.26 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 486 IGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSG------FAFT 559
Cdd:PRK08575 8 VGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISGvekgglQRFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 560 ANGWVqsYGSrcvkpPIIYGDVS-RPKAMTVFWSSMAQSMTKR-----PMKGMLTGPVTILNWSfvrnDQPRFETCYQIA 633
Cdd:PRK08575 88 DNNFY--YRQ-----PVIKEKINlKEENPYLQWLESAREIKEEvslesKLKAVLPGPLTYAVLS----DNEYYKNLIELM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 634 LAIKDEVEDLEKA---GITVIQIDEAALREglplrKSEHAFYLNWAVHSFRITNCGVEDTTQIHTHMCYSNFnDIIHSII 710
Cdd:PRK08575 157 EDYASVVNSLIKElssVVDAVEIHEPSIFA-----KGIKRDTLEKLPEVYKTMAKNVNIEKHLMTYFEINNL-KRLDILF 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743796608 711 DMDADVITIENSRSDEKLLSVFrEGVKyGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNI 775
Cdd:PRK08575 231 SLPVTYFGIDVIENLKKLGRVY-TYLK-GRKVYLGILNARNTKMEKISTIRRIVNKVKRKGVSDI 293
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
236-379 |
5.81e-03 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 39.58 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743796608 236 VYQEVLaELKAAGASWIQFDEPKLVMDLGAHEL--QAFTHAYSALEASLsGLNV------LVETYFADVPveayktltsl 307
Cdd:PRK04326 163 INEEIK-NLVEAGAKYIQIDEPALATHPEDVEIavEALNRIVKGINAKL-GLHVcygdysRIAPYILEFP---------- 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743796608 308 ksVTGFGFDLV-RGTKTLELIKG-GFpsGKYLFAGVVDGRNIWANNLASSLDTLKALEGIVGKDKLVVSTSCSL 379
Cdd:PRK04326 231 --VDQFDLEFAnGNYKLLDLLKEyGF--DKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGL 300
|
|
| |
