|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
41-1053 |
0e+00 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 1841.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 41 ETVARAVKGLAQGSAGAPTADALRGNSLTPEFRIDpVTGALSAQPGQTVSPSSCLGCWTQCGVRLRVDTETNRILRVAGN 120
Cdd:PRK14991 27 DTAKRAAKGLLNGTSGKPTRDRIHGNSLTPEYRVD-AQGQLQPNPQQRVANTQCLGCWTQCGVRVRVDNATNKILRIAGN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 121 PYHPLATTQPAPMHAPVREVYARLGGDNGLEGRATSCARGSAMLEQLTSPYRVLQPLKRVGPRGAGQWRTISFEQLVEEV 200
Cdd:PRK14991 106 PYHPLSTDHHIDMSTPVKEAFESLSGESGLEGRSTACARGNAMLEQLDSPYRVLQPLKRVGKRGSGKWQRISFEQLVEEV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 201 CEGGDLFGEGHVDGLRAIYDPVTPLDPDNPEYGPRSNQLLFTDSANEGRTPLIQRFAAQSFGTVNVSNHGSYCGQSFRVG 280
Cdd:PRK14991 186 VEGGDLFGEGHVDGLRAIRDLDTPIDAKNPEYGPKANQLLVTNASDEGRDAFIKRFAFNSFGTRNFGNHGSYCGLAYRAG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 281 TGAAFGDLKGMPHGKPDWTRARFGLFIGTAPAQSGNPFQRQGRQLAEARVRDDgagFHYVVVSPVLPASASLAAGSGNEW 360
Cdd:PRK14991 266 SGALMGDLDKNPHVKPDWDNVEFALFIGTSPAQSGNPFKRQARQLANARTRGN---FEYVVVAPALPLSSSLAAGDNNRW 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 361 LAVDPAGDLALVMGMIRWILEHDRYDAAMLSQPGPAAMDAAGEAAWTNATHLVIDAPGHARHGSCLRGADLGWPRAGADP 440
Cdd:PRK14991 343 LPIRPGTDSALAMGMIRWIIDNQRYNADYLAQPGVAAMQAAGEASWTNATHLVIADPGHPRYGQFLRASDLGLPFEGEAR 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 441 -QAEDVYVVQRPDGTLAPHTHAGPAALFVERDLPAEGVAPglggVRASSALALLRREARRMTLDEYARHSGVPAARIAGL 519
Cdd:PRK14991 423 gDGEDTLVVDAADGELVPATQAQPARLFVEQYVTLADGQR----VRVKSSLQLLKEAARKLSLAEYSEQCGVPEAQIIAL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 520 AERFTSHGKQAVADAHGGTMSGAGFYTAYAIAMLNTLVGNLNVAGGLVLDGGPFAPYGKGPRYDIAGFAGRVAPRGVSLS 599
Cdd:PRK14991 499 AEEFTSHGRKAAVISHGGTMSGNGFYNAWAIMMLNALIGNLNLKGGVVVGGGKFPGFGDGPRYNLASFAGKVKPKGVSLS 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 600 RNRFPYEKSSEYRRKAEAGQSPYPARSPWYPATGALSSEMLASALAGYPYRAKVWLNHMSNPVYAIAGLKNVIADKLRDP 679
Cdd:PRK14991 579 RSKFPYEKSSEYRRKVEAGQSPYPAKAPWYPFVAGLLTEMLTAALEGYPYPLKAWINHMSNPIYGVPGLRAVIEEKLKDP 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 680 GLLPLSVSINAFINETNALADYIVPDTITYESWGVSAPWADVQAKASTVRWPAVAPRVARTADGEPVCLESFLIACAKRL 759
Cdd:PRK14991 659 KKLPLFISIDAFINETTALADYIVPDTHTYESWGFTAPWGGVPTKASTARWPVVEPRTAKTADGQPVCMESFLIAVAKRL 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 760 GMPGFGADAIAGRDGRRHALDTASDFFLRGMANMAYAGGAPVAEASEDDLALTGVDRHADLLRRTLHEDEWRRVALLMSR 839
Cdd:PRK14991 739 QLPGFGDNAIKDAQGNTHPLNRAEDFYLRGAANIAYLGKTPVADASDEDIALTGVSRILPALQATLKPDEVRRVAFIYAR 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 840 GGRFDAAEDVWRDGRVHPPYRKPLHVWSEDLARMRHAMTGEPYSGCPTWYPTRLADGRAMREQYPQADWPFLLSSFKSNL 919
Cdd:PRK14991 819 GGRFAPAESAYDEERMGNRWKKPLQIWNEDVAAARHSMTGERYSGCPTWYPPRLADGTPLREQFPESQWPLLLISFKSNL 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 920 MSSMSIGVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGYGHTELGARAHVV 999
Cdd:PRK14991 899 MSSMSIASPRLRQVKPANPVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHGYGHRELGARAHSI 978
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....
gi 33567827 1000 DGQPMPHDPALAAGVNLNDLGFGDATRAlRDNVWIDWVSGAAVRQGLPARLEKA 1053
Cdd:PRK14991 979 DGKPMPANPQIRAGVNLNDLGLADPTRE-ITNVWVDWVSGAAVRQGLPAKIEKI 1031
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
91-896 |
0e+00 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 1152.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 91 PSSCLGCWTQCGVRLRVDTETNRILRVAGNPYHPLATTQPAPMHAPVRE-VYARLGGDNGLEGRATSCARGSAMLEQLTS 169
Cdd:cd02758 1 YSSCLGCWTQCGIRVRVDKETGKVLRIAGNPYHPLNTAPSLPYNTPLKEsLYLSLVGENGLKARATACARGNAGLQYLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 170 PYRVLQPLKRVGPRGAGQWRTISFEQLVEEVCEGGDLFGEGHVDGLRAIYDPVTPLDPDNPEYGPRSNQLLFTDSANEGR 249
Cdd:cd02758 81 PYRVLQPLKRVGPRGSGKWKPISWEQLIEEVVEGGDLFGEGHVEGLKAIRDLDTPIDPDHPDLGPKANQLLYTFGRDEGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 250 TPLIQRFAAQSFGTVNVSNHGSYCGQSFRVGTGAAFGDLKGMPHGKPDWTRARFGLFIGTAPAQSGNPFQRQGRQLAEAR 329
Cdd:cd02758 161 TPFIKRFANQAFGTVNFGGHGSYCGLSYRAGNGALMNDLDGYPHVKPDFDNAEFALFIGTSPAQAGNPFKRQARRLAEAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 330 VRDdgaGFHYVVVSPVLPASASlAAGSGNEWLAVDPAGDLALVMGMIRWILEHDRYDAAMLSQPGPAAMDAAGEAAWTNA 409
Cdd:cd02758 241 TEG---NFKYVVVDPVLPNTTS-AAGENIRWVPIKPGGDGALAMAMIRWIIENERYNAEYLSIPSKEAAKAAGEPSWTNA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 410 THLVIDapgharhgsclrgadlgwpragadpqaedvyvvqrpdgtlaphthagpaalfverdlpaegvapglggVRASSA 489
Cdd:cd02758 317 THLVIT--------------------------------------------------------------------VRVKSA 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 490 LALLRREARRMTLDEYARHSGVPAARIAGLAERFTSHGKQAVADAHGGTMSGAGFYTAYAIAMLNTLVGNLNVAGGLVLD 569
Cdd:cd02758 329 LQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTMHSNGFYNAYAIRMLNALIGNLNWKGGLLMS 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 570 GGPFAPYGKGPRYDIAGFAGRVAPRGVSLSRNRFPYEKSSEYRRKAEAGQSPYPARSPWYPATGALSSEMLASALAGYPY 649
Cdd:cd02758 409 GGGFADNSAGPRYDFKKFFGEVKPWGVPIDRSKKAYEKTSEYKRKVAAGENPYPAKRPWYPLTPELYTEVIASAAEGYPY 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 650 RAKVWLNHMSNPVYAIAGLKNVIADKLRDPGLLPLSVSINAFINETNALADYIVPDTITYESWGVSAPWADVQAKASTVR 729
Cdd:cd02758 489 KLKALILWMANPVYGAPGLVKQVEEKLKDPKKLPLFIAIDAFINETSAYADYIVPDTTYYESWGFSTPWGGVPTKASTAR 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 730 WPAVAPRVARTADGEPVCLESFLIACAKRLGMPGFGADAIAGRDGRRHALDTASDFFLRGMANMAYAGGAPVAEASEDDL 809
Cdd:cd02758 569 WPVIAPLTEKTANGHPVSMESFLIDLAKALGLPGFGPNAIKDGQGNKFPLNRAEDYYLRVAANIAYDGKAPVPDASEEEL 648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 810 ALTGVDRHADLLRRTLHEDEWRRVALLMSRGGRFDAAEDVWRDGRVHPPYRKPLHVWSEDLARMRHAMTGEPYSGCPTWY 889
Cdd:cd02758 649 KLTGVNRPIPALKRTLKPEEWRKVAYILARGGRFAPYEESYDGDNLRNRWGKTLQIWNEKLAKSRNSVTGEYFSGCPTYY 728
|
....*..
gi 33567827 890 PTRLADG 896
Cdd:cd02758 729 PPRFADG 735
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
72-1053 |
5.55e-79 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 272.49 E-value: 5.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 72 FRIDPVTGALSAQPGQTVSPSSCLGCWTQCGvrLRVDTETNRILRVAGNPYHPLAttqpapmhapvrevyarlggdnglE 151
Cdd:COG0243 6 FKAAGAGAAALEAAGTKTVKTTCPGCGVGCG--LGVKVEDGRVVRVRGDPDHPVN------------------------R 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 152 GRAtsCARGSAMLEQLTSPYRVLQPLKRVGPRGAGQWRTISFEQLVEEVceggdlfgeghVDGLRAIYDpvtpldpdnpE 231
Cdd:COG0243 60 GRL--CAKGAALDERLYSPDRLTYPMKRVGPRGSGKFERISWDEALDLI-----------AEKLKAIID----------E 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 232 YGPRSNqLLFTDSANEGRT-----PLIQRFAAQsFGTVNVSNHGSYCGQSFRVGTGAAFGDLKGmPHGKPDWTRARFGLF 306
Cdd:COG0243 117 YGPEAV-AFYTSGGSAGRLsneaaYLAQRFARA-LGTNNLDDNSRLCHESAVAGLPRTFGSDKG-TVSYEDLEHADLIVL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 307 IGTAPAQSGNpfqRQGRQLAEARvRDDGAGFhyVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILEHDRYD 386
Cdd:COG0243 194 WGSNPAENHP---RLLRRLREAA-KKRGAKI--VVIDPRRTETAAIA----DEWLPIRPGTDAALLLALAHVLIEEGLYD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 387 AAMlsqpgpaamdaageaawtnathlvidapgharhgsclrgadlgwpragadpqaedvyvvqrpdgtLAPHTHagpaal 466
Cdd:COG0243 264 RDF-----------------------------------------------------------------LARHTV------ 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 467 fverdlpaegvapglggvrassALALLRREARRMTLDEYARHSGVPAARIAGLAERFTSHGKQAVADAHGGTMSGAGFYT 546
Cdd:COG0243 273 ----------------------GFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQT 330
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 547 AYAIAMLNTLVGNLNVAGglvldGGPFAPYGkgprydiagfagrvaprgvslsrnrfpyeksseyrrkaeagqspypars 626
Cdd:COG0243 331 VRAIANLALLTGNIGKPG-----GGPFSLTG------------------------------------------------- 356
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 627 pwypatgalssEMLasaLAGYPYRAKVWLNHMSNPVYAIAGLkNVIADKLRDpglLPLSVSINAFINETNALADYIVPDT 706
Cdd:COG0243 357 -----------EAI---LDGKPYPIKALWVYGGNPAVSAPDT-NRVREALRK---LDFVVVIDTFLTETARYADIVLPAT 418
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 707 ITYESWGVSAPWAD--VQAkastvRWPAVAPRvartadGEpvCLESFLIAC--AKRLGMPgfgadaiagrdgrrhaldta 782
Cdd:COG0243 419 TWLERDDIVTNSEDrrVHL-----SRPAVEPP------GE--ARSDWEIFAelAKRLGFE-------------------- 465
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 783 sDFFLRGMAnmayaggapvaeaseddlaltgvdrhadllrrtlhEDEWRRVALLMSRGGRFDaAEDVWRDGRVHPPyRKP 862
Cdd:COG0243 466 -EAFPWGRT-----------------------------------EEDYLRELLEATRGRGIT-FEELREKGPVQLP-VPP 507
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 863 LHVWSEDLA------RMRHAMTGEPYSGCPTWYPTrladgrAMREQYPQADWPFLLSSFKSNLMS-SMSIGVSRLRQVHP 935
Cdd:COG0243 508 EPAFRNDGPfptpsgKAEFYSETLALPPLPRYAPP------YEGAEPLDAEYPLRLITGRSRDQWhSTTYNNPRLREIGP 581
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 936 HNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGYGhtelgarahvvdgqpmpHDPALAAGVN 1015
Cdd:COG0243 582 RPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWW-----------------YEPADDKGGN 644
|
970 980 990
....*....|....*....|....*....|....*...
gi 33567827 1016 LNDLgFGDATralrdnvwiDWVSGAAVRQGLPARLEKA 1053
Cdd:COG0243 645 VNVL-TPDAT---------DPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
908-1052 |
2.41e-58 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 196.75 E-value: 2.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 908 WPFLLSSFKSNLMSSMSIGVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGY 987
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIEHGY 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33567827 988 GHTELGARAHVVDGQPMPHDPALAAGVNLNDLGFGDATRALRDNVwiDWVSGAAVRQGLPARLEK 1052
Cdd:cd02780 81 GHWAYGAVASTIDGKDLPGDAWRGAGVNINDIGLVDPSRGGWSLV--DWVGGAAARYDTPVKIEK 143
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
91-735 |
8.58e-38 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 147.83 E-value: 8.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 91 PSSCLGCWTQCGVRLRVdtETNRILRVAGNPYHPLAttqpapmhapvrevyarlggdnglEGRAtsCARGSAMLEQLTSP 170
Cdd:cd02755 2 PSICEMCSSRCGILARV--EDGRVVKIDGNPLSPLS------------------------RGKL--CARGNAGIQLLYDP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 171 YRVLQPLKRVGPRGAGQWRTISFEQLVEEVceggdlfgeghVDGLRAIydpvtpldpdNPEYGPRSnqLLFTdSANEGRT 250
Cdd:cd02755 54 DRLKKPLIRVGERGEGKFREASWDEALQYI-----------ASKLKEI----------KEQHGPES--VLFG-GHGGCYS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 251 PLIQRFaAQSFGTVNVSNHGSYCGQSFRVGTGAAFGDLKGMPhgKPDWTRARFGLFIGTAPAQSGNPfqRQGRQLAEARV 330
Cdd:cd02755 110 PFFKHF-AAAFGSPNIFSHESTCLASKNLAWKLVIDSFGGEV--NPDFENARYIILFGRNLAEAIIV--VDARRLMKALE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 331 RddgaGFHYVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILEHDRYDAAmlsqpgpaamdaageaawtnat 410
Cdd:cd02755 185 N----GAKVVVVDPRFSELASKA----DEWIPIKPGTDLAFVLALIHVLISENLYDAA---------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 411 hlvidapgharhgsclrgadlgwpragadpqaedvyvvqrpdgtlaphthagpaalFVErdlpaegvapglggvRASSAL 490
Cdd:cd02755 235 --------------------------------------------------------FVE---------------KYTNGF 243
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 491 ALLRREARRMTLDEYARHSGVPAARIAGLAERFTSHGKQAVAD-AHGGTMSGAGFYTAYAIAMLNTLVGNLNVAGGLvld 569
Cdd:cd02755 244 ELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDpGWRGTFYSNSFQTRRAIAIINALLGNIDKRGGL--- 320
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 570 ggpfapygkgprydiagfagrvaprgvslsrnrfpyeksseyrrkaeagqspYPARSPwypatgalssemlasalagYPY 649
Cdd:cd02755 321 ----------------------------------------------------YYAGSA-------------------KPY 329
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 650 RAKVW-------LNHMSNPVYAIAGLKNviadklrdpglLPLSVSINAFINETNALADYIVPDTiTY-----ESWGVSAP 717
Cdd:cd02755 330 PIKALfiyrtnpFHSMPDRARLIKALKN-----------LDLVVAIDILPSDTALYADVILPEA-TYlerdePFSDKGGP 397
|
650
....*....|....*...
gi 33567827 718 wadvqAKASTVRWPAVAP 735
Cdd:cd02755 398 -----APAVATRQRAIEP 410
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
91-759 |
1.82e-37 |
|
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.
Pssm-ID: 238218 [Multi-domain] Cd Length: 374 Bit Score: 145.16 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 91 PSSCLGCWTQCGvrLRVDTETNRILRVAGNPYHPLAttqpapmhapvrevyarlggdnglEGRAtsCARGSAMLEQLTSP 170
Cdd:cd00368 1 PSVCPFCGVGCG--ILVYVKDGKVVRIEGDPNHPVN------------------------EGRL--CDKGRAGLDGLYSP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 171 YRVLQPLKRVGPRgaGQWRTISFEQLVEEVceggdlfgeghVDGLRAIYDpvtpldpdnpEYGPRSNQLLFTDSANEGRT 250
Cdd:cd00368 53 DRLKYPLIRVGGR--GKFVPISWDEALDEI-----------AEKLKEIRE----------KYGPDAIAFYGGGGASNEEA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 251 PLIQRFAAqSFGTVNVSNHGSYCGQSFRVGTGAAFGDlkGMPHGKPDWTRARFGLFIGTAPAQSGnpfQRQGRQLAEARV 330
Cdd:cd00368 110 YLLQKLLR-ALGSNNVDSHARLCHASAVAALKAFGGG--APTNTLADIENADLILLWGSNPAETH---PVLAARLRRAKK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 331 RddgaGFHYVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGmirwilehdrydaamlsqpgpaamdaageaawtnat 410
Cdd:cd00368 184 R----GAKLIVIDPRRTETAAKA----DEWLPIRPGTDAALALA------------------------------------ 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 411 hlvidapgharhgsclrgadlgwpragadpqaedvyvvqrpdgtlaphthagpaalfverdlpaegvapglggvrassal 490
Cdd:cd00368 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 491 allrrearrmtlDEYARHSGVPAARIAGLAERFTSHGKQAVADAHGGTMSGAGFYTAYAIAMLNTLVGNLNVAGGlvldg 570
Cdd:cd00368 220 ------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGG----- 282
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 571 gpfapygkgprydiagfagrvaprgvslsrnrfpyeksseyrrkaeagqspyparspwypatgalssemlasalagypyr 650
Cdd:cd00368 --------------------------------------------------------------------------------
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 651 akvWLNHMSNPVYAIAGLKNVIADKLRdpglLPLSVSINAFINETNALADYIVPDTITYESWGVSAPWAdvqakastvrW 730
Cdd:cd00368 283 ---GLGPGGNPLVSAPDANRVRAALKK----LDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTE----------G 345
|
650 660
....*....|....*....|....*....
gi 33567827 731 PAVAPRVARTADGEPVCLESFLIACAKRL 759
Cdd:cd00368 346 RVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
48-1020 |
7.10e-33 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 137.11 E-value: 7.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 48 KGLAQGSAGAPTAdalrgnSLTPefridpvtGALSAQPGQTVS------PSSCLGCWTQCGVRLRVdtETNRILRVAGNP 121
Cdd:PRK15488 10 KGAGAGCAACALG------SLLP--------GALAANEIAQLKgktkltPSICEMCSTRCPIEARV--VNGKNVFIQGNP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 122 YHPlattqpapmhapvrevyarlggdngleGRATS-CARGSAMLEQLTSPYRVLQPLKRVGPRGAGQWRTISFEQLVEEV 200
Cdd:PRK15488 74 KAK---------------------------SFGTKvCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 201 CEggdlfgeghvdGLRAIYDpvtpldpdnpEYGPRSnqllFTDSANEGRTPLIQRFAAQSFGTVNVSNHGSYCGQSFRVG 280
Cdd:PRK15488 127 AA-----------KLNAIKQ----------QHGPES----VAFSSKSGSLSSHLFHLATAFGSPNTFTHASTCPAGYAIA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 281 TGAAFG-DLkgmphgKPDWTRAR----FG--LFIGTAPAQSgnpfqrqgRQLAEARVrDDGAGFhyVVVSPVLpasaSLA 353
Cdd:PRK15488 182 AKVMFGgKL------KRDLANSKyiinFGhnLYEGINMSDT--------RGLMTAQM-EKGAKL--VVFEPRF----SVV 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 354 AGSGNEWLAVDPAGDLALVMGMIRWILEHDRYDAAmlsqpgpaamdaageaawtnathlvidapgharhgsclrgadlgw 433
Cdd:PRK15488 241 ASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKA--------------------------------------------- 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 434 pragadpqaedvyvvqrpdgtlaphthagpaalFVErdlpaegvapglggvRASSALALLRREARRMTLDEYARHSGVPA 513
Cdd:PRK15488 276 ---------------------------------FVE---------------RYTSGFEELAASVKEYTPEWAEAISDVPA 307
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 514 ARIAGLAERFTSHGKQAVAD-AHGGTMSGAGFYTAYAIAMLNTLVGNLNVAGGLVLdggpfapyGKG-PRYDiaGFAG-R 590
Cdd:PRK15488 308 DDIRRIARELAAAAPHAIVDfGHRATFTPEEFDMRRAIFAANVLLGNIERKGGLYF--------GKNaSVYN--KLAGeK 377
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 591 VAPRGVSLSRNRFPyeKSSEYRRKAEAGQSPYPARSpwypatGALSSEMLASALAGYPYRAKVWLNHMSNPVYAIAGLKN 670
Cdd:PRK15488 378 VAPTLAKPGVKGMP--KPTAKRIDLVGEQFKYIAAG------GGVVQSIIDATLTQKPYQIKGWVMSRHNPMQTVTDRAD 449
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 671 VIADKLRdpglLPLSVSINAFINETNALADYIVPDTiTY--ESWGVSapwaDVQAK--ASTVRWPAVAPrvarTADGEPv 746
Cdd:PRK15488 450 VVKALKK----LDLVVVCDVYLSESAAYADVVLPES-TYleRDEEIS----DKSGKnpAYALRQRVVEP----IGDTKP- 515
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 747 cleSFLIA--CAKRLGMPGFgadaiagrdgrrhaldtasdFFLRGMAnmayaggapvaeasedDLALTGVDRHADLLRRt 824
Cdd:PRK15488 516 ---SWQIFkeLGEKMGLGQY--------------------YPWQDME----------------TLQLYQVNGDHALLKE- 555
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 825 LHED---EWrRVALLMSRGG-------RFDAAEDVWRDG------RVHPPYRKpLHVWSEDLARMrhamtgEPYSGCPTW 888
Cdd:PRK15488 556 LKKKgyvSF-GVPLLLREPKmvakfvaRYPNAKAVDEDGtygsqlKFKTPSGK-IELFSAKLEAL------APGYGVPRY 627
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 889 YPTRLADGR---------AMREQYPQADWPFLlssfkSNLMSSmsigvsrlrqvhphNPVSISRADASRLGIGNGDAVRI 959
Cdd:PRK15488 628 RDVALKKEDelyfiqgkvAVHTNGATQNVPLL-----ANLMSD--------------NAVWIHPQTAGKLGIKNGDEIRL 688
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33567827 960 VTPGGAVTGLALVRDGVQPGAIAIEHGYGHT--ELgARAH---VVDGQPMPHDPALAAGVNLNDLG 1020
Cdd:PRK15488 689 ENSVGKEKGKALVTPGIRPDTLFAYMGFGSKnkEL-TRATgkgIHCGNLLPHVTSPVSGTNVHTTG 753
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
92-785 |
1.30e-28 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 123.02 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 92 SSCLGCWTQCGVRLRVdtETNRILRVAGNPYHPLattqpapmhapvrevyarlggdngleGRATSCARGSAMLEQLTSPY 171
Cdd:cd02763 2 TTCYMCACRCGIRVHL--RDGKVRYIKGNPDHPL--------------------------NKGVICAKGSSGIMKQYSPA 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 172 RVLQPLKRVGPRGAGQWRTISFEQLVEEVCEggdlfgegHVDGLRAIydpvtplDPdnpeygprSNQLLFTdsaneGR-- 249
Cdd:cd02763 54 RLTKPLLRKGPRGSGQFEEIEWEEAFSIATK--------RLKAARAT-------DP--------KKFAFFT-----GRdq 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 250 -TPLIQRFAAQsFGTVNVSNHGSYCGQSFRVG----TGAAFGDLkgmphGKPDWTRARFGLFIGTAPAQSGNPFQRQGRQ 324
Cdd:cd02763 106 mQALTGWFAGQ-FGTPNYAAHGGFCSVNMAAGglysIGGSFWEF-----GGPDLEHTKYFMMIGVAEDHHSNPFKIGIQK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 325 LAEarvrddgAGFHYVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILEHDRYDAAMLSQpgpaamdaagea 404
Cdd:cd02763 180 LKR-------RGGKFVAVNPVRTGYAAIA----DEWVPIKPGTDGAFILALAHELLKAGLIDWEFLKR------------ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 405 aWTNATHLVIDAPGHARHgsclrgadlgwpRAGadpqaedvyvvqrpdgtlaphthagpaalfverdLPAEGVApglggv 484
Cdd:cd02763 237 -YTNAAELVDYTPEWVEK------------ITG----------------------------------IPADTIR------ 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 485 RASSALALLRREARRMTLDEYARHSGVPAARIAGLAERFtsHGKQAVAdAHGGtmsgaGFYTAYAIAMLNTLVGNLNVAG 564
Cdd:cd02763 264 RIAKELGVTARDQPIELPIAWTDVWGRKHEKITGRPVSF--HAMRGIA-AHSN-----GFQTIRALFVLMMLLGTIDRPG 335
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 565 GLvLDGGPF---APYG----KGPRYDIAGFAGRVAPRGVSLSRNRFPYEKSSEYRRKAEAGQSPYPArspwypATGALSS 637
Cdd:cd02763 336 GF-RHKPPYprhIPPLpkppKIPSADKPFTPLYGPPLGWPASPDDLLVDEDGNPLRIDKAYSWEYPL------AAHGCMQ 408
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 638 EMLASALAGYPYRAKVWLNHMSNPVY----AIAGLKNVIADKLRDPG-LLPLSVSINAFINETNALADYIVPDTITYESW 712
Cdd:cd02763 409 NVITNAWRGDPYPIDTLMIYMANMAWnssmNTPEVREMLTDKDASGNyKIPFIIVCDAFYSEMVAFADLVLPDTTYLERH 488
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33567827 713 GVSA----PWADVQAKASTVRWPAVAPrvartaDGEPVCLESFLIACAKRLGMPGFGADaiagrDGRRHALDTAsDF 785
Cdd:cd02763 489 DAMSlldrPISEADGPVDAIRVPIVEP------KGDVKPFQEVLIELGTRLGLPGFTNE-----DGTRKYRDYP-DF 553
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
91-761 |
2.01e-27 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 117.41 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 91 PSSCLGCWTQCGVRLRVdtETNRILRVAGNPYHPLattqpapmhapvrevyarlggdngleGRATSCARGSAMLEQLTSP 170
Cdd:cd02759 1 KGTCPGCHSGCGVLVYV--KDGKLVKVEGDPNHPT--------------------------NKGRLCMRGLAAPEIVYHP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 171 YRVLQPLKRVGPRGAGQWRTISFEQLVEEVCEggdlfgegHVDGLRAiydpvtpldpdnpEYGPRSNQLLFTDSANEGR- 249
Cdd:cd02759 53 DRLLYPLKRVGERGENKWERISWDEALDEIAE--------KLAEIKA-------------EYGPESIATAVGTGRGTMWq 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 250 TPLIQRFAAQSFGTVNVSNHGSYCGQSFRVGTGAAFGDLKGMPHgkPDWTRARFGLFIGTAPAQSGNPFqrQGRQLAEAR 329
Cdd:cd02759 112 DSLFWIRFVRLFGSPNLFLSGESCYWPRDMAHALTTGFGLGYDE--PDWENPECIVLWGKNPLNSNLDL--QGHWLVAAM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 330 VRddgaGFHYVVVSPVLPASASLAAgsgnEWLAVDPAGDLALVMGMIRWILEHDRYDAAMLSQpgpaamdaageaaWTNA 409
Cdd:cd02759 188 KR----GAKLIVVDPRLTWLAARAD----LWLPIRPGTDAALALGMLNVIINEGLYDKDFVEN-------------WCYG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 410 thlvidapgharhgsclrgadlgwpragadpqaedvyvvqrpdgtlaphthagpaalFVErdlpaegvapglggvrassa 489
Cdd:cd02759 247 ---------------------------------------------------------FEE-------------------- 249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 490 lalLRREARRMTLDEYARHSGVPAARIAGLAERFTSHGKQAVADAHGGTMSGAGFYTAYAIAMLNTLVGNLNVAGGLVLd 569
Cdd:cd02759 250 ---LAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNLL- 325
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 570 ggpfapygkgprydiagfagrvaprgvslsrnrfpyeksseyrrkaeagqSPYPARSPWypatgALSSEMLASalagypy 649
Cdd:cd02759 326 --------------------------------------------------IPYPVKMLI-----VFGTNPLAS------- 343
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 650 rakvwlnhMSNPVYAIAGLKNviadklrdpglLPLSVSINAFINETNALADYIVPDTITYESWGVSAPWADVQAKASTVR 729
Cdd:cd02759 344 --------YADTAPVLEALKA-----------LDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAENFVQLRQK 404
|
650 660 670
....*....|....*....|....*....|..
gi 33567827 730 wpAVAPRVARTADGEpvclesFLIACAKRLGM 761
Cdd:cd02759 405 --AVEPYGEAKSDYE------IVLELGKRLGP 428
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
91-716 |
1.91e-25 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 111.76 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 91 PSSCLGCWTQCGVRLRVDTetNRILRVAGNPYHPlattqpapmhapvrevyarlgGDNGlegraTSCARGSAMLEQLTSP 170
Cdd:cd02757 3 PSTCQGCTAWCGLQAYVED--GRVTKVEGNPLHP---------------------GSRG-----RLCAKGHLGLQQVYDP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 171 YRVLQPLKRVGPRGA----GQWRTISFEQLVEEVCEggdlfgegHVDGLRaiydpvtpldpdnpEYGPRSNQLLFTDSAN 246
Cdd:cd02757 55 DRILYPMKRTNPRKGrdvdPKFVPISWDEALDTIAD--------KIRALR--------------KENEPHKIMLHRGRYG 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 247 EGRTPLIQRFAAqSFGTVNVSNHGSYCGQSFRVGTGAAFGdlkGMPHGKPDWTRARFGLFIGTAPAQSG--NPFQRQ--G 322
Cdd:cd02757 113 HNNSILYGRFTK-MIGSPNNISHSSVCAESEKFGRYYTEG---GWDYNSYDYANAKYILFFGADPLESNrqNPHAQRiwG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 323 RQLAEARVrddgagfhyVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILEHDRYDAAMLSQpgpaamdaag 402
Cdd:cd02757 189 GKMDQAKV---------VVVDPRLSNTAAKA----DEWLPIKPGEDGALALAIAHVILTEGLWDKDFVGD---------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 403 eaaWTNATHLVidapgharhgsclrgadlgwpRAGADPQAEDVYVVqrpdgtlapHTHagpaalfverdlpaegvapglg 482
Cdd:cd02757 246 ---FVDGKNYF---------------------KAGETVDEESFKEK---------STE---------------------- 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 483 gvrasSALALLRREARRMTLDEYARHSGVPAARIAGLAERF-TSHGKQAVADAHGGTMSGAGFYTAYAIAMLNTLVGNLN 561
Cdd:cd02757 271 -----GLVKWWNLELKDYTPEWAAKISGIPAETIERVAREFaTAAPAAAAFTWRGATMQNRGSYNSMACHALNGLVGSID 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 562 VAGGLVLDGGpfapygkgprydiagfagrvaprgvslsrnrfpyeksseyrrkaeagqSPyparspwypatgalssemla 641
Cdd:cd02757 346 SKGGLCPNMG------------------------------------------------VP-------------------- 357
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33567827 642 salagypyRAKVWLNHMSNPVYAIAGLKNVIaDKLRDpglLPLSVSINAFINETNALADYIVPDTITYESWGVSA 716
Cdd:cd02757 358 --------KIKVYFTYLDNPVFSNPDGMSWE-EALAK---IPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMS 420
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
157-567 |
3.47e-23 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 105.25 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 157 CARGSAMLEQLTSPYRVLQPLKRVGPRGAGQWRTISFEQLVEEVceggdlfgeghVDGLRAIYDpvtpldpdnpEYGPRS 236
Cdd:cd02765 40 CTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITWDEALDTI-----------ADKLTEAKR----------EYGGKS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 237 nQLLFTDSANEGRTPLIQR--FAAQSFGTVNVS-NHGSycGQSFRVGTGAAFGdlKGMpHGKPDWTRARFGLFIGTAPAQ 313
Cdd:cd02765 99 -ILWMSSSGDGAILSYLRLalLGGGLQDALTYGiDTGV--GQGFNRVTGGGFM--PPT-NEITDWVNAKTIIIWGSNILE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 314 SgnpfqrqgrQLAEAR----VRDDGAGFhyVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILEHDRYDAAM 389
Cdd:cd02765 173 T---------QFQDAEffldARENGAKI--VVIDPVYSTTAAKA----DQWVPIRPGTDPALALGMINYILEHNWYDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 390 LSQpgpaamdaageaaWTNATHLVidapgHARHGSCLRGADLGwpragaDPQAEDVYVVQRPD-GTLAPH-THAGPAALF 467
Cdd:cd02765 238 LKS-------------NTSAPFLV-----REDNGTLLRQADVT------ATPAEDGYVVWDTNsDSPEPVaATNINPALE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 468 VERDlpaegvapgLGGVRASSALALLRREARRMTLDEYARHSGVPAARIAGLAERFTSHGKQAVADAHGGTMSGAGFYTA 547
Cdd:cd02765 294 GEYT---------INGVKVHTVLTALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFG 364
|
410 420
....*....|....*....|
gi 33567827 548 YAIAMLNTLVGNLNVAGGLV 567
Cdd:cd02765 365 RTAAILAALTGNIGRVGGGV 384
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
91-983 |
3.97e-23 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 105.74 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 91 PSSCLGCWTQCGVRLRVDTetNRILRVAGNPYHPLattqpapmhapvrevyarlggdNglEGRAtsCARGSAMLEQLTSP 170
Cdd:COG3383 8 KTVCPYCGVGCGIDLEVKD--GKIVKVEGDPDHPV----------------------N--RGRL--CVKGRFGFEFVNSP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 171 YRVLQPLKRVGprgaGQWRTISFEQLVEEVceggdlfgeghVDGLRAIYDpvtpldpdnpEYGPRSNQLLFTdsaneGRT 250
Cdd:COG3383 60 DRLTTPLIRRG----GEFREVSWDEALDLV-----------AERLREIQA----------EHGPDAVAFYGS-----GQL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 251 P-----LIQRFAAQSFGTVNVSNHGSYCGQSFRVGTGAAFGdLKGMPHGKPDWTRARFGLFIGTAPAQSGNPFqrqGRQL 325
Cdd:COG3383 110 TneenyLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFG-SDAPPNSYDDIEEADVILVIGSNPAEAHPVL---ARRI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 326 AEARVRddgaGFHYVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILEHDRYDAAmlsqpgpaamdaageaa 405
Cdd:COG3383 186 KKAKKN----GAKLIVVDPRRTETARLA----DLHLQIKPGTDLALLNGLLHVIIEEGLVDED----------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 406 wtnathlvidapgharhgsclrgadlgwpragadpqaedvYVVQRPDGtlaphthagpaalFVErdlpaegvapglggvr 485
Cdd:COG3383 241 ----------------------------------------FIAERTEG-------------FEE---------------- 251
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 486 assalalLRREARRMTLDEYARHSGVPAARIAGLAERFTSHGKQAVADAHGGTMSGAGFYTAYAIAMLNTLVGNLNVAGG 565
Cdd:COG3383 252 -------LKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGT 324
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 566 lvldgGPFAPYGK----GPRyDIAGFAgrvaprgvslsrNRFP-YEK--SSEYRRK-AEAGQSPYPARSPWYPATgalss 637
Cdd:COG3383 325 -----GPFPLTGQnnvqGGR-DMGALP------------NVLPgYRDvtDPEHRAKvADAWGVPPLPDKPGLTAV----- 381
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 638 EMLASALAGypyRAKVWLNHMSNPV-------YAIAGLKNviadklrdpglLPLSVSINAFINETNALADYIVPdtitye 710
Cdd:COG3383 382 EMFDAIADG---EIKALWIIGENPAvsdpdanHVREALEK-----------LEFLVVQDIFLTETAEYADVVLP------ 441
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 711 swgvSAPWADvqaKASTV--------RWpavapRVARTADGEpvCLESFLIAC--AKRLGMPgfgadaiagrdgrrhald 780
Cdd:COG3383 442 ----AASWAE---KDGTFtnterrvqRV-----RKAVEPPGE--ARPDWEIIAelARRLGYG------------------ 489
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 781 tasdfflrgmanMAYAGGAPVAeaseddlaltgvdrhadllrrtlheDEWRRVALLMSrGGRFDAAEdvwRDGRVHPPYR 860
Cdd:COG3383 490 ------------FDYDSPEEVF-------------------------DEIARLTPDYS-GISYERLE---ALGGVQWPCP 528
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 861 KPLHvwsedlarmrhamTGEPY---SGCPTwyptrlADGRA--MREQY------PQADWPFLLSSFKS----NLMsSMSI 925
Cdd:COG3383 529 SEDH-------------PGTPRlftGRFPT------PDGKArfVPVEYrppaelPDEEYPLVLTTGRLldqwHTG-TRTR 588
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 33567827 926 GVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAI 983
Cdd:COG3383 589 RSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFM 646
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
152-780 |
4.38e-22 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 102.74 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 152 GRATSCARGSAMLEQLTSPYRVLQPLKRVGPRGAGQ----WRTISFEQLVEEVCEggdlfgegHVDGLRAiydpvtplDP 227
Cdd:cd02760 38 ARGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKKGRNedpgFVPISWDEALDLVAA--------KLRRVRE--------KG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 228 DNPEYG-PRsnqllFTDSANEGRTPLIQR-----FAAqSFGTVNVS---NHGSYCGQSFRVGTG---AAFGDLkgmphgk 295
Cdd:cd02760 102 LLDEKGlPR-----LAATFGHGGTPAMYMgtfpaFLA-AWGPIDFSfgsGQGVKCVHSEHLYGEfwhRAFTVA------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 296 PDWTRARFGLFIGTAPAQSGNPFQRqgRQLAEARVRddgaGFHYVVVSPVLPASASLAAgsgnEWLAVDPAGDLALVMGM 375
Cdd:cd02760 169 ADTPLANYVISFGSNVEASGGPCAV--TRHADARVR----GYKRVQVEPHLSVTGACSA----EWVPIRPKTDPAFMFAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 376 IRWILEH---DRYDAAMLSQPgpaamdaageaawTNATHLVIDapgharHGSCLRGADLGWPragadpqaedvYVVQRPD 452
Cdd:cd02760 239 IHVMVHEqglGKLDVPFLRDR-------------TSSPYLVGP------DGLYLRDAATGKP-----------LVWDERS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 453 GTLAPHTH--AGPA-----ALFVERDLPAEGVAPGLGGVRASSALALLRREARRMTLDEYARHSGVPAARIAGLAERF-- 523
Cdd:cd02760 289 GRAVPFDTrgAVPAvagdfAVDGAVSVDADDETAIHQGVEGTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIAREFle 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 524 -TSHGKQAVADAHG------------GTMSGAG-FYTAYAIAMLNTLVGNLNVAGGLVldggPFAPYGKGPRYD-----I 584
Cdd:cd02760 369 nASIGSTIEVDGVTlpyrpvavtlgkSVNNGWGaFECCWARTLLATLVGALEVPGGTL----GTTVRLNRPHDDrlasvK 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 585 AGFAGRVAPRGVSLSRNRFPyekSSEYRRKAEAGQSPYPARSPWYPATG----ALSSEMLASALAGY--PYRAKVWLNHM 658
Cdd:cd02760 445 PGEDGFMAQGFNPTDKEHWV---VKPTGRNAHRTLVPIVGNSAWSQALGptqlAWMFLREVPLDWKFelPTLPDVWFNYR 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 659 SNPVYAIAGLKNVIADKLRdpglLPLSVSINAFINETNALADYIVPDTITYESWG---------VSAPWADvqaKASTVR 729
Cdd:cd02760 522 TNPAISFWDTATLVDNIAK----FPFTVSFAYTEDETNWMADVLLPEATDLESLQmikvggtkfVEQFWEH---RGVVLR 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 730 WPAVAPrVARTADGEPVCLEsfliaCAKRLGM---------PGFGADAIAGrDGRRHALD 780
Cdd:cd02760 595 QPAVEP-QGEARDFTWISTE-----LAKRTGLladynaalnRGAGGAPLKG-EGYDQSLD 647
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
91-744 |
1.25e-16 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 84.37 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 91 PSSCLGCWTQCGvrLRVDTETNRILRVAGNPYHPLAttqpapmhapvrevyarlggdnglegRATSCARGSAMLEQLTSP 170
Cdd:cd02762 1 KRACILCEANCG--LVVTVEDGRVASIRGDPDDPLS--------------------------KGYICPKAAALGDYQNDP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 171 YRVLQPLKRVGprgaGQWRTISFEQLVEEVCEGgdlfgeghvdgLRAIYDPvtpLDPDNPEY---GPRSNqllftDSANE 247
Cdd:cd02762 53 DRLRTPMRRRG----GSFEEIDWDEAFDEIAER-----------LRAIRAR---HGGDAVGVyggNPQAH-----THAGG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 248 GRTPLIQRfaaqSFGTVNVSNHGSYCGQSFRVGTGAAFGDLKGMPHgkPDWTRARFGLFIGTAPAQS-GNPFQRQGRQLA 326
Cdd:cd02762 110 AYSPALLK----ALGTSNYFSAATADQKPGHFWSGLMFGHPGLHPV--PDIDRTDYLLILGANPLQSnGSLRTAPDRVLR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 327 EARVRDDGAGFhyVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILEHdrydaamlsqpgpaamdaageaaw 406
Cdd:cd02762 184 LKAAKDRGGSL--VVIDPRRTETAKLA----DEHLFVRPGTDAWLLAAMLAVLLAE------------------------ 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 407 tnathlvidapgharhGSCLRGAdlgwpragadpqaedvyvvqrpdgtLAPHTHAgpaalfverdlpaegvapglggvra 486
Cdd:cd02762 234 ----------------GLTDRRF-------------------------LAEHCDG------------------------- 247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 487 ssaLALLRREARRMTLDEYARHSGVPAARIAGLAERFTSHGKQAVADAHGGTMSGAGFYTAYAIAMLNTLVGNLNVAGGL 566
Cdd:cd02762 248 ---LDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGA 324
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 567 VLDGgPFAPYgkgprydiagfAGRVAPRGVSLSRnrfpyeksseyRRKAEAGQSPYPARSPwypaTGALSSEMLASAlag 646
Cdd:cd02762 325 MFTT-PALDL-----------VGQTSGRTIGRGE-----------WRSRVSGLPEIAGELP----VNVLAEEILTDG--- 374
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 647 yPYRAKVWLNHMSNPVYAIAGlknviADKLRDP-GLLPLSVSINAFINETNALADYIVPDTITYESWgvSAPWADVQAKA 725
Cdd:cd02762 375 -PGRIRAMIVVAGNPVLSAPD-----GARLEAAlGGLEFMVSVDVYMTETTRHADYILPPASQLEKP--HATFFNLEFPR 446
|
650 660
....*....|....*....|.
gi 33567827 726 STVRW--PAVAPRVARTADGE 744
Cdd:cd02762 447 NAFRYrrPLFPPPPGTLPEWE 467
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
921-990 |
5.47e-16 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 74.28 E-value: 5.47e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 921 SSMSIGVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGYGHT 990
Cdd:cd02775 7 SGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHR 76
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
92-392 |
7.32e-16 |
|
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 81.91 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 92 SSC-LGCWTQCGvrLRVDTETNRILRVAGNPYHPlaTTqpapmhapvrevyarlggdnglegRATSCARGSAMLEQLTSP 170
Cdd:cd02766 2 SVCpLDCPDTCS--LLVTVEDGRIVRVEGDPAHP--YT------------------------RGFICAKGARYVERVYSP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 171 YRVLQPLKRVGPRGaGQWRTISFEQLVEEVceggdlfgeghVDGLRAIYDpvtpldpdnpEYGPRS--------NQLLFT 242
Cdd:cd02766 54 DRLLTPLKRVGRKG-GQWERISWDEALDTI-----------AAKLKEIKA----------EYGPESilpysyagTMGLLQ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 243 DSAnegrtplIQRFaaqsFGTVNVSN-HGSYCGqsfrvGTGAA-----FGDLKGMPhgKPDWTRARFGLFIGTAPAQSgn 316
Cdd:cd02766 112 RAA-------RGRF----FHALGASElRGTICS-----GAGIEaqkydFGASLGND--PEDMVNADLIVIWGINPAAT-- 171
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33567827 317 pFQRQGRQLAEARVRddgaGFHYVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILEHDRYDAAMLSQ 392
Cdd:cd02766 172 -NIHLMRIIQEARKR----GAKVVVIDPYRTATAARA----DLHIQIRPGTDGALALGVAKVLFREGLYDRDFLAR 238
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
907-1053 |
3.90e-14 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 70.11 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 907 DWPFLLSSFKSNLMS--SMSIGVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIE 984
Cdd:cd02782 1 DYPFLLLIGRRHLRSnnSWLHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33567827 985 HGYGHTELGARAHVVDgqpmphdpalaAGVNLNDlgfgdatraLRDNVWIDWVSGAAVRQGLPARLEKA 1053
Cdd:cd02782 81 HGWGHDYPGVSGAGSR-----------PGVNVND---------LTDDTQRDPLSGNAAHNGVPVRLARV 129
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
923-999 |
3.59e-12 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 63.83 E-value: 3.59e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33567827 923 MSIGVSRLRQVHPhNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGYGHTELGARAHVV 999
Cdd:pfam01568 17 RTRRVLRLAKPEP-EVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGWWYEPRGGNANAL 92
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
96-392 |
4.97e-11 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 66.58 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 96 GCWTQCGVR--LRVDTETNRILRVAGNPYHPLAttqpaPMHAPVRevyarlggdnglegratSCARGSAMLEQLTSPYRV 173
Cdd:cd02770 3 ACTVNCGGRcpLKAHVKDGVITRIETDDTGDDD-----PGFHQIR-----------------ACLRGRSQRKRVYNPDRL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 174 LQPLKRVGPRGAGQWRTISFEQLVEEVceggdlfgeghVDGLRAIYDpvtpldpdnpEYGPRS---NQLLFTDSANEGRT 250
Cdd:cd02770 61 KYPMKRVGKRGEGKFVRISWDEALDTI-----------ASELKRIIE----------KYGNEAiyvNYGTGTYGGVPAGR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 251 PLIQRFAAQSFGTVNvsNHGSYCGQSFRVGTGAAFGDlkgmPHGKPDWT-RARFGLFI--GTAPAQSGNPFQRQGRQLAE 327
Cdd:cd02770 120 GAIARLLNLTGGYLN--YYGTYSWAQITTATPYTYGA----AASGSSLDdLKDSKLVVlfGHNPAETRMGGGGSTYYYLQ 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33567827 328 ARvrddGAGFHYVVVSPVLPASASLAAGsgnEWLAVDPAGDLALVMGMIRWILEHDRYDAAMLSQ 392
Cdd:cd02770 194 AK----KAGAKFIVIDPRYTDTAVTLAD---EWIPIRPGTDAALVAAMAYVMITENLHDQAFLDR 251
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
157-390 |
1.56e-10 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 64.65 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 157 CARGSAMLEQLTSPYRVLQPLKRVGPRGAGQWRTISFEQLVEEVCEggdlfgeghvdglRAIYDPVTpldpdnpeYGPRS 236
Cdd:cd02750 51 CQRGASFSWYLYSPDRVKYPLKRVGARGEGKWKRISWDEALELIAD-------------AIIDTIKK--------YGPDR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 237 NqllFTDSANEGRTPLiqRFAAQS-----FGTVNVSNHGSYCgqSFRVGTGAAFGDlKGMPHGKPDWTRARFGLFIGTAP 311
Cdd:cd02750 110 V---IGFSPIPAMSMV--SYAAGSrfaslIGGVSLSFYDWYG--DLPPGSPQTWGE-QTDVPESADWYNADYIIMWGSNV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 312 AQSGNP---FqrqgrqLAEARVRddgaGFHYVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILEHDRYDAA 388
Cdd:cd02750 182 PVTRTPdahF------LTEARYN----GAKVVVVSPDYSPSAKHA----DLWVPIKPGTDAALALAMAHVIIKEKLYDED 247
|
..
gi 33567827 389 ML 390
Cdd:cd02750 248 YL 249
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
91-392 |
1.60e-10 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 65.11 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 91 PSSCLGCWTQCGVRLRVDTEtnRILRVAGNPYHPLAttqpapmhapvrevyarlggdnglegRATSCARGSAMLEQLTSP 170
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNG--VWVHQEGDPDHPVN--------------------------RGSLCPKGAALRDFVHSP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 171 YRVLQPLKRVGprGAGQWRTISFEQLVEEVceggdlfgeghVDGLRAIYDPVTPLDPDNPEYGPRSNQLLFTDSA---NE 247
Cdd:cd02752 53 KRLKYPMYRAP--GSGKWEEISWDEALDEI-----------ARKMKDIRDASFVEKNAAGVVVNRPDSIAFLGSAklsNE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 248 GrTPLIQRFAAqSFGTVNVSNHGSYCGQSFRVGTGAAFGdlKG-MPHGKPDWTRARFGLFIGTAPAQSgNP--FQrqgrQ 324
Cdd:cd02752 120 E-CYLIRKFAR-ALGTNNLDHQARIUHSPTVAGLANTFG--RGaMTNSWNDIKNADVILVMGGNPAEA-HPvsFK----W 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33567827 325 LAEARvrdDGAGFHYVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILehdRYDAAMLSQ 392
Cdd:cd02752 191 ILEAK---EKNGAKLIVVDPRFTRTAAKA----DLYVPIRSGTDIAFLGGMINYII---RYTPEEVED 248
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
101-386 |
3.48e-10 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 63.77 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 101 CGV--RLRVDTETNRILRVAGNPYHPlattqpapmhapvrevyarlgGDNGLegratSCARGSAMLEQLTSPYRVLQPLK 178
Cdd:cd02753 7 CGVgcGLELWVKDNKIVGVEPVKGHP---------------------VNRGK-----LCVKGRFGFDFVNSKDRLTKPLI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 179 RVGprgaGQWRTISFEQLVEEVceggdlfgeghVDGLRAIYDpvtpldpdnpEYGPRSnqLLFTDSA---NEgRTPLIQR 255
Cdd:cd02753 61 RKN----GKFVEASWDEALSLV-----------ASRLKEIKD----------KYGPDA--IAFFGSAkctNE-ENYLFQK 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 256 FAAQSFGTVNVSNHGSYC------GQSFRVGTGAAFGDLkgmphgkPDWTRARFGLFIGTAPAQSgNPFqrQGRQLAEAR 329
Cdd:cd02753 113 LARAVGGTNNVDHCARLChsptvaGLAETLGSGAMTNSI-------ADIEEADVILVIGSNTTEA-HPV--IARRIKRAK 182
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 330 VRddGAGFhyVVVSP---VLPASASLaagsgneWLAVDPAGDLALVMGMIRWILEHDRYD 386
Cdd:cd02753 183 RN--GAKL--IVADPrrtELARFADL-------HLQLRPGTDVALLNAMAHVIIEEGLYD 231
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
889-999 |
6.19e-10 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 57.90 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 889 YPTRLADGRaMREQYpqadwpfllssfksNLMSsMSIGVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTG 968
Cdd:cd00508 3 YPLVLTTGR-LLEHW--------------HTGT-MTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVV 66
|
90 100 110
....*....|....*....|....*....|.
gi 33567827 969 LALVRDGVQPGAIAIEHGYGHTELGARAHVV 999
Cdd:cd00508 67 RARVTDRVRPGTVFMPFHWGGEVSGGAANAL 97
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
62-565 |
6.55e-10 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 63.51 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 62 ALRGNSLTPEF-RIDPVTGALS-AQPGQTVSPSSC-LGCWTQCGVRLRVdtetnrilrvagnpyhplattqpapMHAPVR 138
Cdd:PRK14990 29 AMASSALTLPFsRIAHAVDSAIpTKSDEKVIWSACtVNCGSRCPLRMHV-------------------------VDGEIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 139 EVYARLGGDNGLEG--RATSCARGSAMLEQLTSPYRVLQPLKRVGPRGAGQWRTISFEQLVEEVCEGGDLFGEGHvdGLR 216
Cdd:PRK14990 84 YVETDNTGDDNYDGlhQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEY--GNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 217 AIYdpvtpldpdnPEYGPRSNQLLFTDSANEGRTpLIQRFAAQSFGTVNvsNHGSYCGQSFRVGTGAAFGdlkGMPHGK- 295
Cdd:PRK14990 162 SIY----------LNYGTGTLGGTMTRSWPPGNT-LVARLMNCCGGYLN--HYGDYSSAQIAEGLNYTYG---GWADGNs 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 296 -PDWTRARFGLFIGTAPAQ---SGNP---FQRQGRQLAEARVrddgagfhyVVVSpvlPASASLAAGSGNEWLAVDPAGD 368
Cdd:PRK14990 226 pSDIENSKLVVLFGNNPGEtrmSGGGvtyYLEQARQKSNARM---------IIID---PRYTDTGAGREDEWIPIRPGTD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 369 LALVMGMirwilehdrydaamlsqpgpaamdaageaAWTNATHLVIDAPgharhgsclrgadlgwpragadpqAEDVYVV 448
Cdd:PRK14990 294 AALVNGL-----------------------------AYVMITENLVDQP------------------------FLDKYCV 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 449 QrpdgtlaphthagpaalFVERDLPAEgvAPGLGGVRA------SSALALLRREARRMTldeyarhsGVPAARIAGLAER 522
Cdd:PRK14990 321 G-----------------YDEKTLPAS--APKNGHYKAyilgegPDGVAKTPEWASQIT--------GVPADKIIKLARE 373
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 33567827 523 FTSHGKQAVADAHGGTMSGAGFYTAYAIAMLNTLVGNLNVAGG 565
Cdd:PRK14990 374 IGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGG 416
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
909-990 |
7.07e-10 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 57.67 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 909 PFLLSSFKSNLMS-SMSIGVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGY 987
Cdd:cd02778 1 EFRLIYGKSPVHThGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGF 80
|
...
gi 33567827 988 GHT 990
Cdd:cd02778 81 GHW 83
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
91-390 |
1.40e-08 |
|
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 58.78 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 91 PSSCLGCwtqcgvRLRVDTETNRILRVAgnpyhPLATTQPAPmhapvrevyarlggdnglegratsCARGSAMLEQLTSP 170
Cdd:cd02751 1 PTACHWG------PFKAHVKDGVIVRVE-----PDDTDQPRP------------------------CPRGRSVRDRVYSP 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 171 YRVLQPLKRVGP----------RGAGQWRTISFEQLVEEVceggdlfgeghVDGLRAIYDpvtpldpdnpEYGPRSnqlL 240
Cdd:cd02751 46 DRIKYPMKRVGWlgngpgsrelRGEGEFVRISWDEALDLV-----------ASELKRIRE----------KYGNEA---I 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 241 FTDS---ANEGRTP----LIQRFAAQSFGTVNvsNHGSYCGQSFRVGTGAAFGDLKGMPHGkPDW-TRARFG---LFIG- 308
Cdd:cd02751 102 FGGSygwASAGRLHhaqsLLHRFLNLIGGYLG--SYGTYSTGAAQVILPHVVGSDEVYEQG-TSWdDIAEHSdlvVLFGa 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 309 ----TAPAQSGNPFQRQGRQLAEARvrddGAGFHYVVVSPVLPASASLAAgsgNEWLAVDPAGDLALVMGMIRWILEHDR 384
Cdd:cd02751 179 nplkTRQGGGGGPDHGSYYYLKQAK----DAGVRFICIDPRYTDTAAVLA---AEWIPIRPGTDVALMLAMAHTLITEDL 251
|
....*.
gi 33567827 385 YDAAML 390
Cdd:cd02751 252 HDQAFL 257
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
908-986 |
1.94e-08 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 53.74 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 908 WPFLLSSF--KSNLMSSMSiGVSRLRQ---VHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIA 982
Cdd:cd02777 1 YPLQLISPhpKRRLHSQLD-NVPWLREaykVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVA 79
|
....
gi 33567827 983 IEHG 986
Cdd:cd02777 80 LPEG 83
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
91-714 |
4.22e-08 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 57.24 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 91 PSSCLGCWTQCGVRlrVDTETNRILRVAGNPYHPlattqpapmhapvrevyarlgGDNGLegratSCARGSAMLEQLTSP 170
Cdd:cd02754 1 KTTCPYCGVGCGVE--IGVKDGKVVAVRGDPEHP---------------------VNRGR-----LCIKGLNLHKTLNGP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 171 YRVLQPLKRvgpRGAGQWRTISFEQLVEEVCEGgdlfgeghvdgLRAIYDpvtpldpdnpEYGPR------SNQLLFTDS 244
Cdd:cd02754 53 ERLTRPLLR---RNGGELVPVSWDEALDLIAER-----------FKAIQA----------EYGPDsvafygSGQLLTEEY 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 245 AnegrtpLIQRFAAQSFGTVNVSNHGSYCGQSFRVGTGAAFGdLKGMPHGKPDWTRARFGLFIGTAPAQsGNP--FQRqg 322
Cdd:cd02754 109 Y------AANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFG-ADGPPGSYDDIEHADCFFLIGSNMAE-CHPilFRR-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 323 rqLAEARVRDDGAGFhyVVVSPVLPASASLAagsgNEWLAVDPAGDLALVMGMIRWILEHDRYDAAMlsqpgpaamdaag 402
Cdd:cd02754 179 --LLDRKKANPGAKI--IVVDPRRTRTADIA----DLHLPIRPGTDLALLNGLLHVLIEEGLIDRDF------------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 403 eaawtnathlvIDApgharhgsclrgadlgwpragadpqaedvyvvqrpdgtlapHThagpaALFVErdlpaegvapglg 482
Cdd:cd02754 238 -----------IDA-----------------------------------------HT-----EGFEE------------- 247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 483 gvrassalalLRREARRMTLDEYARHSGVPAARIAGLAERFTSHGKQAVADAHGGTMSGAGFYTAYAIAMLNTLVGNLNV 562
Cdd:cd02754 248 ----------LKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGR 317
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 563 AGGlvldgGPFA----PYGKGPRyDIAGFAgrvaprgvslsrNRFPYEKS---SEYRRK-AEAGQSPyPARSPWYPATGA 634
Cdd:cd02754 318 PGS-----GPFSltgqPNAMGGR-EVGGLA------------NLLPGHRSvnnPEHRAEvAKFWGVP-EGTIPPKPGLHA 378
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 635 LssEMLASALAGypyRAKVWLNHMSNPVYAIAGLKNVIADKLRDPgllpLSVSINAFI-NETNALADYIVPDTITYESWG 713
Cdd:cd02754 379 V--EMFEAIEDG---EIKALWVMCTNPAVSLPNANRVREALERLE----FVVVQDAFAdTETAEYADLVLPAASWGEKEG 449
|
.
gi 33567827 714 V 714
Cdd:cd02754 450 T 450
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
906-981 |
8.76e-08 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 51.47 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 906 ADWPFLLSSFKsNL----MSSMSIGVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAI 981
Cdd:cd02790 1 EEYPLVLTTGR-VLyhyhTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVV 79
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
88-169 |
1.33e-07 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 49.17 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 88 TVSPSSCLGCWTQCGVRLRVdtETNRILRVAGNPYHPLattqpapmhapvrevyarlggdNglEGRAtsCARGSAMLEQL 167
Cdd:smart00926 2 KWVPTVCPLCGVGCGLLVEV--KDGRVVRVRGDPDHPV----------------------N--RGRL--CPKGRAGLEQV 53
|
..
gi 33567827 168 TS 169
Cdd:smart00926 54 YS 55
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
926-1052 |
2.84e-07 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 50.38 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 926 GVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGYGHTELGARAHVVDGqpmp 1005
Cdd:cd02781 22 QLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEHGWWYPEREAGEPALGG---- 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 33567827 1006 hdpalAAGVNLNdlgfgdatrALRDNVWIDWVSGAAVRQGLPARLEK 1052
Cdd:cd02781 98 -----VWESNAN---------ALTSDDWNDPVSGSSPLRSMLCKIYK 130
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| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
927-979 |
1.48e-06 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 48.34 E-value: 1.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 33567827 927 VSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPG 979
Cdd:cd02791 25 VPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPG 77
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| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
935-992 |
2.07e-06 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 47.60 E-value: 2.07e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 33567827 935 PHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGYGHTEL 992
Cdd:cd02792 33 PEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIPYHWGGMGL 90
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| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
908-987 |
7.73e-06 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 46.21 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 908 WPFLLSSFKSNL-MSSMSIGVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHG 986
Cdd:cd02785 2 YPLACIQRHSRFrVHSQFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQG 81
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.
gi 33567827 987 Y 987
Cdd:cd02785 82 W 82
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| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
926-986 |
1.61e-05 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 45.32 E-value: 1.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33567827 926 GVSRLRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHG 986
Cdd:cd02793 22 SLSRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLPTG 82
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| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
934-987 |
1.08e-04 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 42.83 E-value: 1.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 33567827 934 HPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGY 987
Cdd:cd02779 30 VPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAH 83
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| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
650-762 |
1.84e-04 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 45.17 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 650 RAKVWLNHMSNPVYAIA-GLKNviADKLRDpglLPLSVSINAFINETNALADYIVPDTITYESWGVSAPWADVQAKAStv 728
Cdd:cd02764 383 KVSALLVYDVNPVYDLPqGLGF--AKALEK---VPLSVSFGDRLDETAMLCDWVAPMSHGLESWGDAETPDGTYSICQ-- 455
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90 100 110
....*....|....*....|....*....|....*
gi 33567827 729 rwPAVAPRV-ARTADgepvclESFLIACAKRLGMP 762
Cdd:cd02764 456 --PVIAPLFdTRSAQ------ESLLLALGGSLGGY 482
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| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
88-124 |
2.78e-04 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 39.58 E-value: 2.78e-04
10 20 30
....*....|....*....|....*....|....*..
gi 33567827 88 TVSPSSCLGCWTQCGvrLRVDTETNRILRVAGNPYHP 124
Cdd:pfam04879 2 KVVKTICPYCGVGCG--LEVHVKDGKIVKVEGDPDHP 36
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| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
317-834 |
4.30e-04 |
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Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 44.48 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 317 PFQRQGR--QLAEARVRDDGAGFHYVVVSPVLPASASLAAGSGNEWLAVDPAGDLALVMGMIRWILEHDRYDAAMLSQPG 394
Cdd:COG3321 867 PFQREDAaaALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALA 946
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 395 PAAMDAAGEAAWTNATHLVIDAPGHARHGSCLRGADLGWPRAGADPQAEDVYVVQRPDGTLAPHTHAGPAALFVERDLPA 474
Cdd:COG3321 947 AAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAA 1026
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 475 EGVAPGLGGVRASSALALLRREARRMTLDEYARHSGVPAARIAGLAERFTSHGKQAVADAHGGTMSGAGFYTAYAIAMLN 554
Cdd:COG3321 1027 LLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAAL 1106
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 555 TLVGNLNVAGGLVLDGGPFAPYGKGPRYDIAGFAGRVAPRGVSLSRNRFPYEKSSEYRRKAEAGQSPYPARSPWYPATGA 634
Cdd:COG3321 1107 LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALA 1186
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330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 635 LSSEMLASALAGYPYRAKVWLNHMSNPVYAIAGLKNVIADKLRDPGLLPLSVSINAFINETNALADYIVPDTITYESWGV 714
Cdd:COG3321 1187 AALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLA 1266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 715 SAPWADVQAKASTVRWPAVAPRVARTADGEPVCLESFLIACAKRLGMPGFGADAIAGRDGRRHALDTASDFFLRGMANMA 794
Cdd:COG3321 1267 AAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAA 1346
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 33567827 795 YAGGAPVAEASEDDLALTGVDRHADLLRRTLHEDEWRRVA 834
Cdd:COG3321 1347 AAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
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| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
939-1002 |
8.45e-04 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 40.34 E-value: 8.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33567827 939 VSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGYghtelgARAHVVDGQ 1002
Cdd:cd02786 33 LLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGGW------WREHSPDGR 90
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| MopB_CT_2 |
cd02783 |
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal ... |
930-981 |
1.15e-03 |
|
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239184 [Multi-domain] Cd Length: 156 Bit Score: 40.52 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 33567827 930 LRQVHPHNPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAI 981
Cdd:cd02783 25 LRQIHTRNYLYMHPKTAKELGIKDGDWVWVESVNGRVKGQARFTETVEPGTV 76
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| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
913-990 |
1.57e-03 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 40.05 E-value: 1.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33567827 913 SSFKSNLMssmsigVSRLRQVHPhnPVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHGYGHT 990
Cdd:cd02776 15 STYRDNLL------MLRLQRGGP--VVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHAQERH 84
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| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
938-1003 |
3.94e-03 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 41.20 E-value: 3.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33567827 938 PVSISRADASRLGIGNGDAVRIVTPGGAVTGLALVRDGVQPGAIAIEHG--YGhTELGARAHVVD--GQP 1003
Cdd:PRK15102 711 PVYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGawYG-PDKGGEIGALCtyGDP 779
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