|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
49-813 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 1642.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 49 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPP 128
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 129 RYGWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 208
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 209 YLLLSKPAKGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLV 288
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 289 ETYFADVPVEAYKTLTSLKSVTGFGFDLVRGTKTLELIK-GGFPSGKYLFAGVVDGRNIWANNLASSLDTLKAFEGIVGK 367
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 368 DKLVVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALATALAGQQDEAFFSANAAAQASRKSSPRVTNETVQ 447
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 448 KAAAALKGSDHRRATNVSARLDSQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQE 527
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 528 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLT 607
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 608 GPVTILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHSFYLNWAVHSFRITNCGVE 687
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 688 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKML 767
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 2015352226 768 AVLESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKLGSAQ 813
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASAK 766
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
54-808 |
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: 1282.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 54 VGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRYGWN 133
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 134 GGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLS 213
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 214 KpakGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVETYFA 293
Cdd:TIGR01371 161 K---AVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 294 DVPvEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKAFEGIVGKdkLVVS 373
Cdd:TIGR01371 238 SVG-DALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 374 TSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALATALAGQQDEAFFSANAAAQA--SRKSSPRVTNETVQKAAA 451
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAiaARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 452 ALKGSDHRRATNVSARLDSQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDI 531
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 532 DVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVT 611
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 612 ILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHSFYLNWAVHSFRITNCGVEDTTQ 691
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 692 IHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLE 771
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 2015352226 772 SNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTK 808
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
51-415 |
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: 591.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 51 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRY 130
Cdd:cd03312 2 THILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPERF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 131 GWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYL 210
Cdd:cd03312 82 GALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 211 LLSKPAKGvekSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVET 290
Cdd:cd03312 162 KLSKAKGG---GFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 291 YFADVpVEAYKTLTSLkSVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKAFEGIVGkDKL 370
Cdd:cd03312 239 YFGSL-GENLDLLASL-PVDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2015352226 371 VVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALATA 415
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
480-803 |
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: 557.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 480 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 559
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 560 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 639
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 640 EDLEKAGITVIQIDEAALREGLPLRKSEHSFYLNWAVHSFRITNCGVEDTTQIHTHMCYSNFNDIIHSIIDMDADVITIE 719
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 720 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTRKYAEVKPALSNMV 799
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 2015352226 800 AAAK 803
Cdd:pfam01717 320 DAAK 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
480-806 |
1.26e-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: 428.40 E-value: 1.26e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 480 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 559
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 560 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 639
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 640 EDLEKAGITVIQIDEAALREGLPlrksehSFYLNWAVHSFRITNCGVEDtTQIHTHMCYSNFNDIIHSIIDMDADVITIE 719
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 720 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTR----KYAEVKPAL 795
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKL 312
|
330
....*....|.
gi 2015352226 796 SNMVAAAKHLR 806
Cdd:COG0620 313 RNMVAFAREVR 323
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
49-813 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 1642.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 49 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPP 128
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 129 RYGWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 208
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 209 YLLLSKPAKGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLV 288
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 289 ETYFADVPVEAYKTLTSLKSVTGFGFDLVRGTKTLELIK-GGFPSGKYLFAGVVDGRNIWANNLASSLDTLKAFEGIVGK 367
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 368 DKLVVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALATALAGQQDEAFFSANAAAQASRKSSPRVTNETVQ 447
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 448 KAAAALKGSDHRRATNVSARLDSQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQE 527
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 528 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLT 607
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 608 GPVTILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHSFYLNWAVHSFRITNCGVE 687
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 688 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKML 767
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 2015352226 768 AVLESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKLGSAQ 813
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASAK 766
|
|
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
48-811 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1349.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 48 AMASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVP 127
Cdd:PRK05222 1 MIKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 128 PRYGWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPV 207
Cdd:PRK05222 81 ERFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDPDTQFKLTSNKLLDEFEEAKALGINTKPVLLGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 208 SYLLLSKpakGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVL 287
Cdd:PRK05222 161 TFLWLSK---SKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 288 VETYFADVpVEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKAFEGIVgk 367
Cdd:PRK05222 238 LATYFGSL-NDALDLLASLP-VDGLHLDLVRGPEQLAALLKYFPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKV-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 368 DKLVVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALATALAGQQD--EAFFSANAAAQASRKSSPRVTNET 445
Cdd:PRK05222 314 DRLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGavAEALAANRAAIAARRTSPRVHNPA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 446 VQKAAAALKGSDHRRATNVSARLDSQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKI 525
Cdd:PRK05222 394 VRARLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 526 QEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGM 605
Cdd:PRK05222 474 QEELGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGM 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 606 LTGPVTILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHSFYLNWAVHSFRITNCG 685
Cdd:PRK05222 554 LTGPVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSG 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 686 VEDTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEK 765
Cdd:PRK05222 634 VKDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFED-FGYPNEIGPGVYDIHSPRVPSVEEIEELLRK 712
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 2015352226 766 MLAVLESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKLGS 811
Cdd:PRK05222 713 ALEVIPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELAA 758
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
54-808 |
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: 1282.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 54 VGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRYGWN 133
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 134 GGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLS 213
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 214 KpakGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVETYFA 293
Cdd:TIGR01371 161 K---AVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 294 DVPvEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKAFEGIVGKdkLVVS 373
Cdd:TIGR01371 238 SVG-DALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 374 TSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALATALAGQQDEAFFSANAAAQA--SRKSSPRVTNETVQKAAA 451
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAiaARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 452 ALKGSDHRRATNVSARLDSQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDI 531
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 532 DVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVT 611
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 612 ILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHSFYLNWAVHSFRITNCGVEDTTQ 691
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 692 IHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLE 771
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 2015352226 772 SNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTK 808
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
51-415 |
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: 591.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 51 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRY 130
Cdd:cd03312 2 THILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPERF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 131 GWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYL 210
Cdd:cd03312 82 GALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 211 LLSKPAKGvekSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVET 290
Cdd:cd03312 162 KLSKAKGG---GFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 291 YFADVpVEAYKTLTSLkSVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKAFEGIVGkDKL 370
Cdd:cd03312 239 YFGSL-GENLDLLASL-PVDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2015352226 371 VVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALATA 415
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
480-803 |
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: 557.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 480 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 559
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 560 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 639
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 640 EDLEKAGITVIQIDEAALREGLPLRKSEHSFYLNWAVHSFRITNCGVEDTTQIHTHMCYSNFNDIIHSIIDMDADVITIE 719
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 720 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTRKYAEVKPALSNMV 799
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 2015352226 800 AAAK 803
Cdd:pfam01717 320 DAAK 323
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
51-365 |
6.28e-175 |
|
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: 505.58 E-value: 6.28e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 51 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRY 130
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 131 GWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYL 210
Cdd:pfam08267 81 GNDGGLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELDKDTEFKLNSNKLLDEYKEAKALGIETKPVLLGPVTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 211 LLSkpaKGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVET 290
Cdd:pfam08267 161 KLS---KGKGGSFDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLAT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015352226 291 YFADVpVEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLASSLDTLKAFEGIV 365
Cdd:pfam08267 238 YFGSV-ADALELLASLP-VAGLGLDLVRGPENLAALKKGFPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
481-803 |
3.26e-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: 435.50 E-value: 3.26e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 481 PTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTan 560
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 561 GWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTK-RPMKGMLTGPVTILNWSFVRN---DQPRFETCYQIALAIK 636
Cdd:cd03311 79 GWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 637 DEVEDLEKAGITVIQIDEAALREGLPLRK-SEHSFYLNWAVHSFRitncGVEDTTQIHTHMCYSNF----------NDII 705
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLEPdDLAADYLKWANEALA----DRPDDTQIHTHICYGNFrstwaaeggyEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 706 HSIIDMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKT 785
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKE-LPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFAT 313
|
330
....*....|....*...
gi 2015352226 786 RKYAEVKPALSNMVAAAK 803
Cdd:cd03311 314 RERGNALTKLENMVKAAL 331
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
480-806 |
1.26e-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: 428.40 E-value: 1.26e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 480 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 559
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 560 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 639
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 640 EDLEKAGITVIQIDEAALREGLPlrksehSFYLNWAVHSFRITNCGVEDtTQIHTHMCYSNFNDIIHSIIDMDADVITIE 719
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 720 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTR----KYAEVKPAL 795
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKL 312
|
330
....*....|.
gi 2015352226 796 SNMVAAAKHLR 806
Cdd:COG0620 313 RNMVAFAREVR 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
50-405 |
1.07e-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: 275.48 E-value: 1.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 50 ASHIVGYPRMgpkRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDqvldttaMLGAVPPR 129
Cdd:COG0620 3 TTTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYD-------MVGYFPER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 130 ygWNGgeigfdvyFSMARgNASVpamemtKWFDTNYHYiVPELGPEVNFSyaSHKAVNEYKEAKAL-GVDTVPVLVGPVS 208
Cdd:COG0620 73 --LDG--------YAFAR-NGWV------EWFDTNYHY-VPEITGDVSFS--GPMTVEEFRFAKSLtGKPVKPVLPGPVT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 209 YLLLSKpakgVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLV 288
Cdd:COG0620 133 LLLLSK----VRDYKDREELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKIHL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 289 ETYFADVPvEAYKTLTSLKsVTGFGFDLVRGT-KTLELIKgGFPSGKYLFAGVVDGRNIWANNLASSLDTLKAFEGIVGK 367
Cdd:COG0620 209 HTCYGGYE-DILEALAALP-VDGIHLEFVRSRaGLLEPLK-ELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPP 285
|
330 340 350
....*....|....*....|....*....|....*...
gi 2015352226 368 DKLVVSTSCSLLHTAVDLvNEPKLDKEIKSWLAFAAQK 405
Cdd:COG0620 286 ERLWVSPDCGLKHRPVDL-TREEAWAKLRNMVAFAREV 322
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
476-810 |
5.99e-80 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 260.29 E-value: 5.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 476 NLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGF 555
Cdd:PRK04326 5 KLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 556 AFtaNGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMT-KRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALA 634
Cdd:PRK04326 85 KF--YGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFNEYYKDKEELVFDLAKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 635 IKDEVEDLEKAGITVIQIDEAAlregLPLRKSEHSfylnWAVHSFRITNCGVEdtTQIHTHMCYSNFNDIIHSIIDMDAD 714
Cdd:PRK04326 163 INEEIKNLVEAGAKYIQIDEPA----LATHPEDVE----IAVEALNRIVKGIN--AKLGLHVCYGDYSRIAPYILEFPVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 715 VITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTRKYAEVKPA 794
Cdd:PRK04326 233 QFDLEFANGNYKLLDLLKE-YGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPREIAYQK 311
|
330
....*....|....*.
gi 2015352226 795 LSNMVAAAKHLRTKLG 810
Cdd:PRK04326 312 LVNMVKATREVREELD 327
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
481-803 |
9.81e-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: 137.94 E-value: 9.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 481 PTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERnDMVEYFGEQLSGFAFtan 560
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DMIGRFLEVLVDLET--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 561 GWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQP--RFETCYQIALAIKDE 638
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPdaYEDLAKSLAEFLREQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 639 VEDLEKAGITVIQIDEAALREGLPLRKSEHSfYLNWAVHSFRITNCGvedttQIHTHMCYsnfNDIIHSIIDMDADVITI 718
Cdd:cd03310 157 VKELKNRGIVVVQIDEPSLGAVGAGAFEDLE-IVDAALEEVSLKSGG-----DVEVHLCA---PLDYEALLELGVDVIGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 719 ENSRSD-------EKLLSVFREGVKYGAGIGPGVYDIHSPR--IPSEEEIADRIEKMLAVLESnILWVNPDCGLKTRKYA 789
Cdd:cd03310 228 DAAALPskyledlKKLLRIGVRTLILGLVVTDNEAKGRNAWkeIERLEKLVRRLEEPGEVLDE-ILYLTPDCGLAFLPPQ 306
|
330
....*....|....
gi 2015352226 790 EVKPALSNMVAAAK 803
Cdd:cd03310 307 EARRKLALLAEAAR 320
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
481-803 |
6.11e-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: 6.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 481 PTTTIGSFPQTMDLRRvrreykaKKISEQNYVEAIKEEINKVVKiQEELDIDVLVHGEpernDMVEYFGEQLsgfaftaN 560
Cdd:cd00465 1 PVQCEGQTGIMEASET-------MAISEEPGETSKAEWGITLVE-PEEIPLDVIPVHE----DDVLKVAQAL-------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 561 GWVQSYGSRCVKPPIIYGDV-SRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRND---------QPRFETCYQ 630
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEEdPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSMGDalmalyerpEAMHELIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 631 IALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEhsFYLNWAVHSFR-ITNCGVEDTTQIHTHMCYSNfNDIIHSII 709
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGPK--MFKKFALPAYKkVAEYKAAGEVPIVHHSCYDA-ADLLEEMI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 710 DMDADVITIENSRSDEKLLsvfREGVKYGAGIGPGVYDIHSPRipSEEEIADRIEKMLAVLESNIlWVNPDCGLKTRKYA 789
Cdd:cd00465 219 QLGVDVISFDMTVNEPKEA---IEKVGEKKTLVGGVDPGYLPA--TDEECIAKVEELVERLGPHY-IINPDCGLGPDSDY 292
|
330
....*....|....
gi 2015352226 790 EvKPALSNMVAAAK 803
Cdd:cd00465 293 K-PEHLRAVVQLVD 305
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
479-806 |
1.50e-30 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 122.41 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 479 ILPTTTIGSFPQTmdlRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPeRNDMVEYFGEQLSGFAft 558
Cdd:PRK00957 1 IMITTVVGSYPVV---KGEPETLKDKIKGFFGLYDPYKPAIEEAVADQVKAGIDIISDGQV-RGDMVEIFASNMPGFD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 559 angwvqsyGSRCVkppiiyGDVSRP-KAMTV----FWSSMAQSMT-KRPMKGMLTGPVTILNWSFVRN---DQPRFETCY 629
Cdd:PRK00957 75 --------GKRVI------GRVEPPaKPITLkdlkYAKKVAKKKDpNKGVKGIITGPSTLAYSLRVEPfysDNKDEELIY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 630 QIALAIKDEVEDLEKAGITVIQIDEAALREGLPlrksehsfYLNWAVHSFRITNCGVEDTTQIHThmCySNFNDIIHSII 709
Cdd:PRK00957 141 DLARALRKEAEALEKAGVAMIQIDEPILSTGAY--------DLEVAKKAIDIITKGLNVPVAMHV--C-GDVSNIIDDLL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 710 DMDADVITIENSRSDEKlLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLK--TRK 787
Cdd:PRK00957 210 KFNVDILDHEFASNKKN-LEILEEKDLIGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDCGMRmlPRD 288
|
330
....*....|....*....
gi 2015352226 788 YAEVKpaLSNMVAAAKHLR 806
Cdd:PRK00957 289 VAFEK--LKNMVEAAREIR 305
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
477-809 |
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 2015352226 477 LPILPTTTIGSF--PQ--TMDLRRVRREYKAKKISEQNYVEAIKeeinkvVKIQEELDiDVLVHGEPERNDMVEYFGEQL 552
Cdd:PRK01207 1 MAALITQEIGSFrkPEylSREFHKIEGTDKFYELAERATLETLD------VFENAGLD-NIGIGGEMFRWEMYEHPAERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 553 SGFAFTanGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIA 632
Cdd:PRK01207 74 KGIIFY--GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEFA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 633 LAIKDEVEDLEKAGITV-------IQIDEAAlreglplrKSEHSFYLNWAVHSFRITNCGVEDttQIHTHMCYSNFNDII 705
Cdd:PRK01207 152 RIINEELKDIKSAWDRKspgrkleIQIDEPA--------TTTHPDEMDIVVDSINKSVYGIDN--EFSIHVCYSSDYRLL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 706 HSII-DMDADVITIENSRSDE----------------KLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLA 768
Cdd:PRK01207 222 YDRIpELNIDGYNLEYSNRDTlepgtsdekrpgfqdlKYFAEHNESLQRKKFIGLGVTDVHIDYVEPVKLIEDRIRYALK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2015352226 769 VL-ESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKL 809
Cdd:PRK01207 302 IIkDPELVRLNPDCGLRTRSREIGEQKLRNMVAAKNNILKEL 343
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
478-810 |
3.01e-20 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 92.82 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 478 PILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAF 557
Cdd:PRK09121 1 TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 558 TANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKD 637
Cdd:PRK09121 81 EKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 638 EVEDLEKAGITVIQIDEAALreglplrksehSFYL----NWAVHSFRITNCGVEDTTQIhtHMCYS-------------- 699
Cdd:PRK09121 161 EAKELEAAGVDIIQFDEPAF-----------NVFFdevnDWGVAALERAIEGLKCETAV--HICYGygikantdwkktlg 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 700 ----NFNDIIHSIIDMDADVITIE--NSRSDEKLLSVFRegvkyGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESN 773
Cdd:PRK09121 228 sewrQYEEAFPKLQKSNIDIISLEchNSRVPMDLLELIR-----GKKVMVGAIDVASDTIETPEEVADTLRKALQFVDAD 302
|
330 340 350
....*....|....*....|....*....|....*....
gi 2015352226 774 ILWVNPDCGLK--TRKYAEVKpaLSNMVAAAKHLRTKLG 810
Cdd:PRK09121 303 KLYPCTNCGMAplSRDVARGK--LNALSAGAEIVRRELA 339
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
53-345 |
8.30e-09 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 58.21 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 53 IVG-YPRmgPKRELKfALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIpsntfscydqvldTTAMlgavpprYG 131
Cdd:PRK08575 7 LVGsYPR--PVKLAK-VISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYT-------------TDGL-------FR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 132 WNggEIgFDVYFSMARGnasVPAMEMTKWFDTNYHYIVPELGPEVNFsyashKAVNEY----KEAKALGVDTVP------ 201
Cdd:PRK08575 64 WD--DI-FDPTISFISG---VEKGGLQRFYDNNFYYRQPVIKEKINL-----KEENPYlqwlESAREIKEEVSLesklka 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 202 VLVGPVSYLLLSKPakgvEKSFSLLSLIDKILPVYQEVLAELKaAGASWIQFDEPKLVM-DLGAHELQAFTHAYSALEAS 280
Cdd:PRK08575 133 VLPGPLTYAVLSDN----EYYKNLIELMEDYASVVNSLIKELS-SVVDAVEIHEPSIFAkGIKRDTLEKLPEVYKTMAKN 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015352226 281 LSGLNVLVeTYFADVPVEAYKTLTSLkSVTGFGFDLVRGTKTLELIKGGFpSGKYLFAGVVDGRN 345
Cdd:PRK08575 208 VNIEKHLM-TYFEINNLKRLDILFSL-PVTYFGIDVIENLKKLGRVYTYL-KGRKVYLGILNARN 269
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
485-774 |
1.72e-03 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 41.26 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 485 IGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSG------FAFT 558
Cdd:PRK08575 8 VGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISGvekgglQRFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 559 ANGWVqsYGSrcvkpPIIYGDVS-RPKAMTVFWSSMAQSMTKR-----PMKGMLTGPVTILNWSfvrnDQPRFETCYQIA 632
Cdd:PRK08575 88 DNNFY--YRQ-----PVIKEKINlKEENPYLQWLESAREIKEEvslesKLKAVLPGPLTYAVLS----DNEYYKNLIELM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015352226 633 LAIKDEVEDLEKA---GITVIQIDEAALREglplrKSEHSFYLNWAVHSFRITNCGVEDTTQIHTHMCYSNFnDIIHSII 709
Cdd:PRK08575 157 EDYASVVNSLIKElssVVDAVEIHEPSIFA-----KGIKRDTLEKLPEVYKTMAKNVNIEKHLMTYFEINNL-KRLDILF 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015352226 710 DMDADVITIENSRSDEKLLSVFrEGVKyGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNI 774
Cdd:PRK08575 231 SLPVTYFGIDVIENLKKLGRVY-TYLK-GRKVYLGILNARNTKMEKISTIRRIVNKVKRKGVSDI 293
|
|
| |
