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Conserved domains on  [gi|1934805533|emb|CAB4243408|]
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conserved protein of unknown function [Methylacidimicrobium sp. AP8]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 8-544 6.19e-127

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PRK14491:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 597  Bit Score: 385.51  E-value: 6.19e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   8 PAIAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELAPPRE 87
Cdd:PRK14491   11 PLLGFCAYSGTGKTTLLEQLIPELNQRGLRLAVIKHAHHNFDVDQPGKDSYRLRKAGASQMLVASRVRWALMTETPRDGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  88 PEIAEAIALLGPTPVDLLLIEGFRAEGVPKIELFVPSLGQ-LFCRNDPDLLAVASegDGAVLPEGVLSFDRNDAEGIAAL 166
Cdd:PRK14491   91 PELPHLLKQIDADKVDIVLVEGFKKLALPKIELHRAAHGKpWIYPHDENIIAIAC--DDTPLPSELPRLDINDVAAIADF 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 167 ILRACGLF--PRSDGGCRGSA---STPKGAIPLKEARRKLREAMAAdrPNAAEEVSLSQSAGRVLARDLVSPFDLPLAPT 241
Cdd:PRK14491  169 VLEYAQNWqaPAQDLPLAPACccdLLSPAFLSVSQGLDKILSLVTP--VTETEDVALDELDGRVLAQDVISPVNVPQHTN 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 242 AAMDGYAVRASELGEEGraFSVAGTAAAGAPFAGVPPEGSCVRIFTGAVLPEGTDLVIPQEEVVLHGDRVILPAGRRAGE 321
Cdd:PRK14491  247 SAMDGYAFRSDDLEPES--YTLVGEVLAGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQ 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 322 NVRARGESFLRGQELLRAGTRIGPGALALLAAAGQDTVPVYPKLRVGLLCTGRELRPVGAPLRHGEIYDSNRAFLSSALA 401
Cdd:PRK14491  325 NVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAK 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 402 ELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGGVSAGESDYVGKLLAERNAVVIRQIAVKPGRPFLFARWRGKPL 481
Cdd:PRK14491  405 KLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPF 484

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934805533 482 FGLPGTPAAVFVLYYDLIRPRVRSAMGER--EPvERARLPALSRIPKKAGRTEYWAGRLALGTKG 544
Cdd:PRK14491  485 FGLPGNPVAVMVSFLQFVEPALRKLAGEQnwQP-LLFPAIADETLRSRQGRTEFSRGIYHLGADG 548
 
Name Accession Description Interval E-value
PRK14491 PRK14491
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ...
 8-544 6.19e-127

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional


Pssm-ID: 237729 [Multi-domain]  Cd Length: 597  Bit Score: 385.51  E-value: 6.19e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   8 PAIAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELAPPRE 87
Cdd:PRK14491   11 PLLGFCAYSGTGKTTLLEQLIPELNQRGLRLAVIKHAHHNFDVDQPGKDSYRLRKAGASQMLVASRVRWALMTETPRDGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  88 PEIAEAIALLGPTPVDLLLIEGFRAEGVPKIELFVPSLGQ-LFCRNDPDLLAVASegDGAVLPEGVLSFDRNDAEGIAAL 166
Cdd:PRK14491   91 PELPHLLKQIDADKVDIVLVEGFKKLALPKIELHRAAHGKpWIYPHDENIIAIAC--DDTPLPSELPRLDINDVAAIADF 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 167 ILRACGLF--PRSDGGCRGSA---STPKGAIPLKEARRKLREAMAAdrPNAAEEVSLSQSAGRVLARDLVSPFDLPLAPT 241
Cdd:PRK14491  169 VLEYAQNWqaPAQDLPLAPACccdLLSPAFLSVSQGLDKILSLVTP--VTETEDVALDELDGRVLAQDVISPVNVPQHTN 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 242 AAMDGYAVRASELGEEGraFSVAGTAAAGAPFAGVPPEGSCVRIFTGAVLPEGTDLVIPQEEVVLHGDRVILPAGRRAGE 321
Cdd:PRK14491  247 SAMDGYAFRSDDLEPES--YTLVGEVLAGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQ 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 322 NVRARGESFLRGQELLRAGTRIGPGALALLAAAGQDTVPVYPKLRVGLLCTGRELRPVGAPLRHGEIYDSNRAFLSSALA 401
Cdd:PRK14491  325 NVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAK 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 402 ELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGGVSAGESDYVGKLLAERNAVVIRQIAVKPGRPFLFARWRGKPL 481
Cdd:PRK14491  405 KLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPF 484

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934805533 482 FGLPGTPAAVFVLYYDLIRPRVRSAMGER--EPvERARLPALSRIPKKAGRTEYWAGRLALGTKG 544
Cdd:PRK14491  485 FGLPGNPVAVMVSFLQFVEPALRKLAGEQnwQP-LLFPAIADETLRSRQGRTEFSRGIYHLGADG 548
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 192-551 3.76e-122

Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440072 [Multi-domain]  Cd Length: 401  Bit Score: 366.34  E-value: 3.76e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 192 IPLKEARRKLREAMaadRPNAAEEVSLSQSAGRVLARDLVSPFDLPLAPTAAMDGYAVRASEL-GEEGRAFSVAGTAAAG 270
Cdd:COG0303     2 ISVEEALALILAAV---RPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLaGANPVTLRVVGEIAAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 271 APFAGVPPEGSCVRIFTGAVLPEGTDLVIPQEEVVLHGDRVILPAGRRAGENVRARGESFLRGQELLRAGTRIGPGALAL 350
Cdd:COG0303    79 SPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 351 LAAAGQDTVPVYPKLRVGLLCTGRELRPVGAPLRHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEK 430
Cdd:COG0303   159 LASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 431 ADLLVTTGGVSAGESDYVGKLLAERNA-VVIRQIAVKPGRPFLFARWRGKPLFGLPGTPAAVFVLYYDLIRPRVRSAMGE 509
Cdd:COG0303   239 ADLVITSGGVSVGDYDLVKEALEELGAeVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGL 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1934805533 510 REP-VERARLPALSRIPKKAGRTEYWAGRLAlGTKGEAAFAPV 551
Cdd:COG0303   319 PPPpPPRVRARLAEDLPKKPGRTEFLRVRLE-RDDGELVVEPL 360
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 196-538 1.20e-119

MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes.


Pssm-ID: 238452 [Multi-domain]  Cd Length: 394  Bit Score: 359.50  E-value: 1.20e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 196 EARRKLREAMAadRPNAAEEVSLSQSAGRVLARDLVSPFDLPLAPTAAMDGYAVRASELGEEGRAFSVAGTAAAGAPFAG 275
Cdd:cd00887     2 EAARELLLALA--PPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRVVGEIPAGEPPDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 276 VPPEGSCVRIFTGAVLPEGTDLVIPQEEVVLHGDRVILPAGRRAGENVRARGESFLRGQELLRAGTRIGPGALALLAAAG 355
Cdd:cd00887    80 PLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 356 QDTVPVYPKLRVGLLCTGRELRPVGAPLRHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEKADLLV 435
Cdd:cd00887   160 IAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 436 TTGGVSAGESDYVGKLLAERNA-VVIRQIAVKPGRPFLFARWRGKPLFGLPGTPAAVFVLYYDLIRPRVRSAMGEREPV- 513
Cdd:cd00887   240 TSGGVSVGDYDFVKEVLEELGGeVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEp 319

                         330       340
                  ....*....|....*....|....*
gi 1934805533 514 ERARLPALSRIPKKAGRTEYWAGRL 538
Cdd:cd00887   320 PRVKARLAEDLKSKPGRREFLRVRL 344
MobB pfam03205
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
 10-142 5.89e-49

Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.


Pssm-ID: 427196 [Multi-domain]  Cd Length: 133  Bit Score: 166.19  E-value: 5.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  10 IAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELAPPREPE 89
Cdd:pfam03205   2 LGIVGWSGSGKTTLLEKLIPELKARGLRVGTIKHAHHGFDIDKPGKDSWRHRKAGASEVLVASPGRWALMHELRDEPEPS 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1934805533  90 IAEAIALLGptPVDLLLIEGFRAEGVPKIELFVPSLGQ-LFCRNDPDLLAVASE 142
Cdd:pfam03205  82 LEELLARLS--PVDLVLVEGFKKEPYPKIEVHRAALGKpPLLPCDPDIIAVASD 133
mobB TIGR00176
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor ...
 10-170 2.41e-35

molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor biosynthesis enzyme is similar to the urease accessory protein UreG and to the hydrogenase accessory protein HypB, both GTP hydrolases involved in loading nickel into the metallocenters of their respective target enzymes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 272943 [Multi-domain]  Cd Length: 155  Bit Score: 130.19  E-value: 2.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  10 IAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELAPprEPE 89
Cdd:TIGR00176   2 LQIVGPKNSGKTTLIERLVKALKARGYRVATIKHDHHDFDIDKNGKDSYRHREAGADQVIVASSRRYAFMHETQE--ERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  90 IAEAIALLgpTPVDLLLIEGFRAEGVPKIELF-VPSLGQLFCRndPDLLAVASegDGAVLPEGVLSFDRNDAEGIAALIL 168
Cdd:TIGR00176  80 LEALLDRL--PDLDIILVEGFKDSPLPKIVVFrNPAEESEIIR--PKIIAIAS--DESLSALKLPVLDLNDVEAIAAFIE 153


                  ..
gi 1934805533 169 RA 170
Cdd:TIGR00176 154 KN 155
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 368-493 5.27e-21

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 89.19  E-value: 5.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  368 GLLCTGRELrpvgapLRHGEIYDSNRAFLSSALAELGVVLVDEGIV--DDDSRVLEERLDALAEKADLLVTTGGVSAGES 445
Cdd:smart00852   1 AIISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1934805533  446 DYVGKLLAERNAVVI--RQIAVKPGRPF-----LFAR----WRGKPLFGLPGTPAAVFV 493
Cdd:smart00852  75 DLTPEALAELGGRELlgHGVAMRPGGPPgplanLSGTapgvRGKKPVFGLPGNPVAALV 133
 
Name Accession Description Interval E-value
PRK14491 PRK14491
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ...
 8-544 6.19e-127

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional


Pssm-ID: 237729 [Multi-domain]  Cd Length: 597  Bit Score: 385.51  E-value: 6.19e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   8 PAIAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELAPPRE 87
Cdd:PRK14491   11 PLLGFCAYSGTGKTTLLEQLIPELNQRGLRLAVIKHAHHNFDVDQPGKDSYRLRKAGASQMLVASRVRWALMTETPRDGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  88 PEIAEAIALLGPTPVDLLLIEGFRAEGVPKIELFVPSLGQ-LFCRNDPDLLAVASegDGAVLPEGVLSFDRNDAEGIAAL 166
Cdd:PRK14491   91 PELPHLLKQIDADKVDIVLVEGFKKLALPKIELHRAAHGKpWIYPHDENIIAIAC--DDTPLPSELPRLDINDVAAIADF 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 167 ILRACGLF--PRSDGGCRGSA---STPKGAIPLKEARRKLREAMAAdrPNAAEEVSLSQSAGRVLARDLVSPFDLPLAPT 241
Cdd:PRK14491  169 VLEYAQNWqaPAQDLPLAPACccdLLSPAFLSVSQGLDKILSLVTP--VTETEDVALDELDGRVLAQDVISPVNVPQHTN 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 242 AAMDGYAVRASELGEEGraFSVAGTAAAGAPFAGVPPEGSCVRIFTGAVLPEGTDLVIPQEEVVLHGDRVILPAGRRAGE 321
Cdd:PRK14491  247 SAMDGYAFRSDDLEPES--YTLVGEVLAGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQ 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 322 NVRARGESFLRGQELLRAGTRIGPGALALLAAAGQDTVPVYPKLRVGLLCTGRELRPVGAPLRHGEIYDSNRAFLSSALA 401
Cdd:PRK14491  325 NVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAK 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 402 ELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGGVSAGESDYVGKLLAERNAVVIRQIAVKPGRPFLFARWRGKPL 481
Cdd:PRK14491  405 KLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPF 484

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934805533 482 FGLPGTPAAVFVLYYDLIRPRVRSAMGER--EPvERARLPALSRIPKKAGRTEYWAGRLALGTKG 544
Cdd:PRK14491  485 FGLPGNPVAVMVSFLQFVEPALRKLAGEQnwQP-LLFPAIADETLRSRQGRTEFSRGIYHLGADG 548
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 192-551 3.76e-122

Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440072 [Multi-domain]  Cd Length: 401  Bit Score: 366.34  E-value: 3.76e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 192 IPLKEARRKLREAMaadRPNAAEEVSLSQSAGRVLARDLVSPFDLPLAPTAAMDGYAVRASEL-GEEGRAFSVAGTAAAG 270
Cdd:COG0303     2 ISVEEALALILAAV---RPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLaGANPVTLRVVGEIAAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 271 APFAGVPPEGSCVRIFTGAVLPEGTDLVIPQEEVVLHGDRVILPAGRRAGENVRARGESFLRGQELLRAGTRIGPGALAL 350
Cdd:COG0303    79 SPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 351 LAAAGQDTVPVYPKLRVGLLCTGRELRPVGAPLRHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEK 430
Cdd:COG0303   159 LASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 431 ADLLVTTGGVSAGESDYVGKLLAERNA-VVIRQIAVKPGRPFLFARWRGKPLFGLPGTPAAVFVLYYDLIRPRVRSAMGE 509
Cdd:COG0303   239 ADLVITSGGVSVGDYDLVKEALEELGAeVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGL 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1934805533 510 REP-VERARLPALSRIPKKAGRTEYWAGRLAlGTKGEAAFAPV 551
Cdd:COG0303   319 PPPpPPRVRARLAEDLPKKPGRTEFLRVRLE-RDDGELVVEPL 360
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 196-538 1.20e-119

MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes.


Pssm-ID: 238452 [Multi-domain]  Cd Length: 394  Bit Score: 359.50  E-value: 1.20e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 196 EARRKLREAMAadRPNAAEEVSLSQSAGRVLARDLVSPFDLPLAPTAAMDGYAVRASELGEEGRAFSVAGTAAAGAPFAG 275
Cdd:cd00887     2 EAARELLLALA--PPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRVVGEIPAGEPPDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 276 VPPEGSCVRIFTGAVLPEGTDLVIPQEEVVLHGDRVILPAGRRAGENVRARGESFLRGQELLRAGTRIGPGALALLAAAG 355
Cdd:cd00887    80 PLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 356 QDTVPVYPKLRVGLLCTGRELRPVGAPLRHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEKADLLV 435
Cdd:cd00887   160 IAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 436 TTGGVSAGESDYVGKLLAERNA-VVIRQIAVKPGRPFLFARWRGKPLFGLPGTPAAVFVLYYDLIRPRVRSAMGEREPV- 513
Cdd:cd00887   240 TSGGVSVGDYDFVKEVLEELGGeVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEp 319

                         330       340
                  ....*....|....*....|....*
gi 1934805533 514 ERARLPALSRIPKKAGRTEYWAGRL 538
Cdd:cd00887   320 PRVKARLAEDLKSKPGRREFLRVRL 344
PRK10680 PRK10680
molybdopterin biosynthesis protein MoeA; Provisional
 190-545 4.16e-79

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 182643 [Multi-domain]  Cd Length: 411  Bit Score: 255.40  E-value: 4.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 190 GAIPLKEArrkLREAMAADRP-NAAEEVSLSQSAGRVLARDLVSPFDLPLAPTAAMDGYAVRASELgEEGRAFSVAGTAA 268
Cdd:PRK10680    6 GLMSLETA---LTEMLSRVTPlTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADL-ASGQPLPVAGKAF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 269 AGAPFAGVPPEGSCVRIFTGAVLPEGTDLVIPQEEVVLHGDRVILPAGRRAGENVRARGESFLRGQELLRAGTRIGPGAL 348
Cdd:PRK10680   82 AGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAEL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 349 ALLAAAGQDTVPVYPKLRVGLLCTGRELRPVGAPLRHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALA 428
Cdd:PRK10680  162 PVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEAD 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 429 EKADLLVTTGGVSAGESDYVGKLLAERNAVVIRQIAVKPGRPFLFARWRGKPLFGLPGTPAAVFVLYYDLIRPRVRSAMG 508
Cdd:PRK10680  242 SQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSG 321

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1934805533 509 EREPVE--RARLPALSRIPKKAGRTEYWAGRLALGTKGE 545
Cdd:PRK10680  322 NTASGLppRQRVRTASRLKKTPGRLDFQRGILQRNADGE 360
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 192-552 1.03e-72

putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 244.74  E-value: 1.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 192 IPLKEARRKLREAMAaDRPNAAEEVSLSQSAGRVLARDLVSPFDLPLAPTAAMDGYAVRASEL--GEEG--RAFSVAGTA 267
Cdd:PRK14498   10 VSLEEAREILESLLS-ELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTfgASEAnpVRLKLGGEV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 268 AAGAPFAGVPPEGSCVRIFTGAVLPEGTDLVIPQEEVVLHGDRVIlpAGRRA---GENVRARGESFLRGQELLRAGTRIG 344
Cdd:PRK14498   89 HAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTV--EIYRPvapGENVRPAGEDIVAGELILPKGTRLT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 345 PGALALLAAAGQDTVPVYPKLRVGLLCTGRELRPVGAPLRHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERL 424
Cdd:PRK14498  167 PRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAAL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 425 DALAEKADLLVTTGGVSAGESDYVGKLLAERNAVVIRQIAVKPGRPFLFARWRGKPLFGLPGTPAAVFVLYYDLIRPRVR 504
Cdd:PRK14498  247 RKALKECDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLR 326

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1934805533 505 SAMGEREPVER---ARLPAlsRIPKKAGRTEYWagRLALGTKGEAAFA-PVS 552
Cdd:PRK14498  327 KLAGLPPPERAtvkARLAR--RVRSELGREEFV--PVSLGRVGDGYVAyPLS 374
PRK14690 PRK14690
molybdopterin biosynthesis protein MoeA; Provisional
 213-541 5.82e-64

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 237789 [Multi-domain]  Cd Length: 419  Bit Score: 215.94  E-value: 5.82e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 213 AEEVSLSQSAGRVLARDLVSPFDLPLAPTAAMDGYAVRASELGEEGRAFSVAGTAAAGAPFAGVPPEGSCVRIFTGAVLP 292
Cdd:PRK14690   42 IKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPLIEGRAAAGVPFSGRVPEGMALRILTGAALP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 293 EGTDLVIPQEEVVLHGDRVILPAGRRAGENVRARGESFLRGQELLRAGTRIGPGALALLAAAGQDTVPVYPKLRVGLLCT 372
Cdd:PRK14690  122 EGVDTVVLEEDVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVLST 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 373 GRELRPVGAPLRHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGGVSAGESDYVGKLL 452
Cdd:PRK14690  202 GDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHVSALL 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 453 AERNAVVIRQIAVKPGRPFLFARWRGKPLFGLPGTPAAVFVLYYDLIRPRVRSAMGE--REPVErARLPALSRIPKKAGR 530
Cdd:PRK14690  282 REAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEgwSEPQG-FTVPAAFEKRKKPGR 360

                         330
                  ....*....|.
gi 1934805533 531 TEYWAGRLALG 541
Cdd:PRK14690  361 REYLRARLRQG 371
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 7-169 5.63e-59

Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 441369 [Multi-domain]  Cd Length: 162  Bit Score: 193.86  E-value: 5.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   7 PPAIAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELapPR 86
Cdd:COG1763     1 MPVLGIVGYSGSGKTTLLEKLIPELKARGLRVGTIKHAHHDFDIDTPGKDSYRHREAGADEVLVASPERWALMTEL--PE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  87 EPEIAEAIALLGptPVDLLLIEGFRAEGVPKIELFVPSLGQ-LFCRNDPDLLAVASEGDgavLPEGVLSFDRNDAEGIAA 165
Cdd:COG1763    79 EPSLDELLARLD--DVDLVLVEGFKHEPLPKIEVHRAEEGKpLLYPEDPNIIAVASDAP---LPTGLPVFDLNDPEAIAD 153


                  ....
gi 1934805533 166 LILR 169
Cdd:COG1763   154 FILE 157
PRK14497 PRK14497
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
 214-533 5.16e-51

putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional


Pssm-ID: 172968 [Multi-domain]  Cd Length: 546  Bit Score: 184.24  E-value: 5.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 214 EEVSLSQSAGRVLARDLVSPFDLPLAPTAAMDGYAVRASELGEEgraFSVAGTAAAGApFAGVP-PEGSCVRIFTGAVLP 292
Cdd:PRK14497   31 VKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGE---FKVIDKIGIGE-FKEIHiKECEAVEVDTGSMIP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 293 EGTDLVIPQEEV-VLHGDRVILPAGRRAGENVRARGESFLRGQELLRAGTRIGPGALALLAAAGQDTVPVYPKLRVGLLC 371
Cdd:PRK14497  107 MGADAVIKVENTkVINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLIA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 372 TGRELRPVGAPLRHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGGVSAGESDYVGKL 451
Cdd:PRK14497  187 TGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKDFVHQA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 452 LAERNAVVIRQIAVKPGRPFLFARWRGKPLFGLPGTPAAVFVLYYDLIRPRVRSAMGER-EPVERARLPALSRIPKKAGR 530
Cdd:PRK14497  267 IRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSRkEILGLGKIKARLALRVKADE 346


                  ...
gi 1934805533 531 TEY 533
Cdd:PRK14497  347 HRN 349
MobB cd03116
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace ...
 8-168 2.05e-49

molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace element in the form of molybdenum cofactor (Moco) which is associated with the metabolism of nitrogen, carbon and sulfur by redox active enzymes. In Escherichia coli, the synthesis of Moco involves genes from several loci: moa, mob, mod, moe and mog. The mob locus contains mobA and mobB genes. MobB catalyzes the attachment of the guanine dinucleotide to molybdopterin.


Pssm-ID: 349770 [Multi-domain]  Cd Length: 157  Bit Score: 168.59  E-value: 2.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   8 PAIAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEElAPPRE 87
Cdd:cd03116     1 KIVGVVGKSGSGKTTLIEKLIPELKARGLRVAVIKHTHHGFDIDTPGKDSYRHRQAGADAVLVSSPNRLALIHE-RPEWE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  88 PEIAEAIALLgpTPVDLLLIEGFRAEGVPKIELFVPSLG-QLFCRNDPDLLAVASegDGAVLPEGVLSFDRNDAEGIAAL 166
Cdd:cd03116    80 LTLLELLARF--SDVDLVLVEGFKKEPIPKIEVFREEEGkPLLLPEDPNVIAVAT--DEPLDMLGLPVFDLNDVEEIADF 155


                  ..
gi 1934805533 167 IL 168
Cdd:cd03116   156 IL 157
MobB pfam03205
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
 10-142 5.89e-49

Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.


Pssm-ID: 427196 [Multi-domain]  Cd Length: 133  Bit Score: 166.19  E-value: 5.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  10 IAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELAPPREPE 89
Cdd:pfam03205   2 LGIVGWSGSGKTTLLEKLIPELKARGLRVGTIKHAHHGFDIDKPGKDSWRHRKAGASEVLVASPGRWALMHELRDEPEPS 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1934805533  90 IAEAIALLGptPVDLLLIEGFRAEGVPKIELFVPSLGQ-LFCRNDPDLLAVASE 142
Cdd:pfam03205  82 LEELLARLS--PVDLVLVEGFKKEPYPKIEVHRAALGKpPLLPCDPDIIAVASD 133
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 215-533 1.76e-43

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 164.99  E-value: 1.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 215 EVSLSQSAGRVLARDLVSPFDLPLAPTAAMDGYAVRASELGEEgraFSVAGTAAAGAPFAGVPPE-GSCVRIFTGAVLPE 293
Cdd:PLN02699   28 IVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGE---YPVITESRAGNDGLGVTLTpGTVAYVTTGGPIPD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 294 GTDLVIPQEEVVLHGD------RVILPAGRRAGENVRARGESFLRGQELLRAGTRIGPGALALLAAAGQDTVPVYPKLRV 367
Cdd:PLN02699  105 GADAVVQVEDTEVVEDpldgskRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVYPRPTV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 368 GLLCTGREL-RPVGAPLRHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLD-ALAEKADLLVTTGGVSAGES 445
Cdd:PLN02699  185 AILSTGDELvEPTTGTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDeAISSGVDILLTSGGVSMGDR 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 446 DYVGKLLAERNAVVIRQIAVKPGRPFLFARWRGKP---------LFGLPGTPAAVFVLYYDLIRPRVRSAMGEREPVERa 516
Cdd:PLN02699  265 DFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIDAKSapsnskkmlAFGLPGNPVSCLVCFNLFVVPAIRYLAGWSNPHLL- 343

                         330
                  ....*....|....*....
gi 1934805533 517 RLPALSRIPKKAG--RTEY 533
Cdd:PLN02699  344 RVQARLREPIKLDpvRPEF 362
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
 214-346 2.24e-38

MoeA N-terminal region (domain I and II); This family contains two structural domains. One of these contains the conserved DGXA motif. This region is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this region is uncertain.


Pssm-ID: 460923 [Multi-domain]  Cd Length: 147  Bit Score: 138.08  E-value: 2.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 214 EEVSLS--QSAGRVLARDLVSPFDLPLAPTAAMDGYAVRAselgEEGRAFSVAGTAAAGAPFAGVPPEGSCVRIFTGAVL 291
Cdd:pfam03453   7 ETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRA----ADGFGASEVNPIAAGEPPGPLLPGGEAVRIMTGAPL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1934805533 292 PEGTDLVIPQEEVVLHGDRVIL-PAGRRAGENVRARGESFLRGQELLRAGTRIGPG 346
Cdd:pfam03453  83 PEGADAVVMVEDTEEGGGRTVEiRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPA 138
mobB TIGR00176
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor ...
 10-170 2.41e-35

molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor biosynthesis enzyme is similar to the urease accessory protein UreG and to the hydrogenase accessory protein HypB, both GTP hydrolases involved in loading nickel into the metallocenters of their respective target enzymes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 272943 [Multi-domain]  Cd Length: 155  Bit Score: 130.19  E-value: 2.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  10 IAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELAPprEPE 89
Cdd:TIGR00176   2 LQIVGPKNSGKTTLIERLVKALKARGYRVATIKHDHHDFDIDKNGKDSYRHREAGADQVIVASSRRYAFMHETQE--ERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  90 IAEAIALLgpTPVDLLLIEGFRAEGVPKIELF-VPSLGQLFCRndPDLLAVASegDGAVLPEGVLSFDRNDAEGIAALIL 168
Cdd:TIGR00176  80 LEALLDRL--PDLDIILVEGFKDSPLPKIVVFrNPAEESEIIR--PKIIAIAS--DESLSALKLPVLDLNDVEAIAAFIE 153


                  ..
gi 1934805533 169 RA 170
Cdd:TIGR00176 154 KN 155
PRK10751 PRK10751
molybdopterin-guanine dinucleotide biosynthesis protein B; Provisional
 6-169 2.52e-31

molybdopterin-guanine dinucleotide biosynthesis protein B; Provisional


Pssm-ID: 236750 [Multi-domain]  Cd Length: 173  Bit Score: 119.80  E-value: 2.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   6 RPPAIAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELAPP 85
Cdd:PRK10751    5 MIPLLAIAAWSGTGKTTLLKKLIPALCARGIRPGLIKHTHHDMDVDKPGKDSYELRKAGAAQTLVASQQRWALMTETPDQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  86 REPEIAEAIALLGPTPVDLLLIEGFRAEGVPKIELFVPSLGQLFCRNDPD--LLAVASEGDGAVlpeGVLSFDRNDAEGI 163
Cdd:PRK10751   85 EELDLHYLASRMDASKLDLILVEGFKHEPIAKIALFRDGAGHRPEELVIDehVIAVASDVPLNL---DVPLLDINDVEQI 161


                  ....*.
gi 1934805533 164 AALILR 169
Cdd:PRK10751  162 ADFIVE 167
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 6-170 7.51e-31

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 123.71  E-value: 7.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   6 RPPAIAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELaPP 85
Cdd:PRK14489  204 APPLLGVVGYSGTGKTTLLEKLIPELIARGYRIGLIKHSHHRVDIDKPGKDSHRLRAAGANPTMIVCPERWALMRET-PE 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  86 REPEIAEAIALLGPTPVDLLLIEGFRAEGVPKIELFVPSLGQLFCRNDPDLLAVASEGDGAVLPegvlSFDRNDAEGIAA 165
Cdd:PRK14489  283 EAVPFKVLIATFDPEEVDLILVEGFKHEPLPKIQLHRQLISKPLPELDLWTIATATDYPLARDP----RLDINDVKQIAD 358


                  ....*
gi 1934805533 166 LILRA 170
Cdd:PRK14489  359 FVRQW 363
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 368-504 6.62e-25

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 100.40  E-value: 6.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 368 GLLCTGRELRPvgaplrhGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGGVSAGESDY 447
Cdd:pfam00994   1 AIITTGDELLP-------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934805533 448 VGKLLAE-------RNAVVIRQIAVKPGRPFLFARW-----RGKPLFGLPGTPAAVFVLYYDLIRPRVR 504
Cdd:pfam00994  74 TPEALAElggrelpGFEELFRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLLR 142
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 365-501 5.25e-24

molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.


Pssm-ID: 272944 [Multi-domain]  Cd Length: 148  Bit Score: 98.16  E-value: 5.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 365 LRVGLLCTGRELRPVGAPLRHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGGVSAGE 444
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934805533 445 SDYVGKLLAERNAVVI-----------RQIAVKPGRPFLFARWRGKPLFGLPGTPAAVFVLYYDLIRP 501
Cdd:TIGR00177  81 RDVTPEALEELGEKEIpgfgefrmlssLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
PRK14490 PRK14490
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ...
 7-167 2.35e-22

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional


Pssm-ID: 237728 [Multi-domain]  Cd Length: 369  Bit Score: 98.97  E-value: 2.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   7 PPAIAFVGRSGAGKTTLLCSVLRILRAKgIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEELAPPR 86
Cdd:PRK14490    5 PFEIAFCGYSGSGKTTLITALVRRLSER-FSVGYYKHGCHRFDIDREGKDSDLARKAGASTVMISDPEKHALIAGGPPDP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  87 epeIAEAIALLGptpVDLLLIEGFRAEGVPKIEL------FVPSLGQlfcRNDPDLLAVASEGDGAVLPE-GVLSFDRND 159
Cdd:PRK14490   84 ---LLERGAFLD---CDLLLVEGLKELPLPKILLvdrerkILDLLEQ---GSVTNVVALVVPDDPASYPDfGLPVFHRDD 154


                  ....*...
gi 1934805533 160 AEGIAALI 167
Cdd:PRK14490  155 IAAIADFI 162
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 368-493 5.27e-21

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 89.19  E-value: 5.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  368 GLLCTGRELrpvgapLRHGEIYDSNRAFLSSALAELGVVLVDEGIV--DDDSRVLEERLDALAEKADLLVTTGGVSAGES 445
Cdd:smart00852   1 AIISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1934805533  446 DYVGKLLAERNAVVI--RQIAVKPGRPF-----LFAR----WRGKPLFGLPGTPAAVFV 493
Cdd:smart00852  75 DLTPEALAELGGRELlgHGVAMRPGGPPgplanLSGTapgvRGKKPVFGLPGNPVAALV 133
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 366-503 8.08e-21

MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin.


Pssm-ID: 238387 [Multi-domain]  Cd Length: 133  Bit Score: 88.55  E-value: 8.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 366 RVGLLCTGRELRPvgaplrhGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGGVSAGES 445
Cdd:cd00758     1 RVAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 446 DYVGKLLAERNAV--VIRQIAVKPGRPFLFARWRGKPLFGLPGTPAAVFVLYYDLIRPRV 503
Cdd:cd00758    74 DVTPEALAELGEReaHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
PRK14495 PRK14495
putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/unknown domain fusion ...
 13-173 3.26e-19

putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/unknown domain fusion protein; Provisional


Pssm-ID: 172967  Cd Length: 452  Bit Score: 90.51  E-value: 3.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  13 VGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGKDSRRLREAGANPVLLVGPTRLARIEEL--APPREPEI 90
Cdd:PRK14495    7 IGWKDAGKTGLVERLVAAIAARGFSVSTVKHSHHDVDPDPPGSDSHRHRAAGAAEVVLAGPRRLILTREHrgEPPRLAAI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  91 AEAIAllgptPVDLLLIEGFRAEGVPKIELFVPSLGQ-LFCRNDPDLLAVASEGDGAvLPEGVLSFDrnDAEGIAALILR 169
Cdd:PRK14495   87 LERMA-----PVDLVLVEGYKTEPHPKIEVFRKAAGHaLRQPEDPWVRAVASDTQMA-LPVPVLDLD--DTEAVADFLLT 158


                  ....
gi 1934805533 170 ACGL 173
Cdd:PRK14495  159 DSGL 162
PRK14494 PRK14494
putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/FeS domain-containing ...
 9-118 6.22e-19

putative molybdopterin-guanine dinucleotide biosynthesis protein MobB/FeS domain-containing protein protein; Provisional


Pssm-ID: 237731 [Multi-domain]  Cd Length: 229  Bit Score: 86.19  E-value: 6.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   9 AIAFVGRSGAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFeiDYPGKDSRRLREAGANPVLLVGPTRLARIEelappREP 88
Cdd:PRK14494    3 AIGVIGFKDSGKTTLIEKILKNLKERGYRVATAKHTHHEF--DKPDTDTYRFKKAGAEVVVVSTDETAAFLY-----DRM 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1934805533  89 EIAEAIALLGptpVDLLLIEGFRAEG-VPKI 118
Cdd:PRK14494   76 DLNEILSLLD---ADFLLIEGFKELLnIPKI 103
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 364-503 1.58e-10

MoeA_like. This domain is similar to a domain found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. There this domain is presumed to bind molybdopterin. The exact function of this subgroup is unknown.


Pssm-ID: 239599  Cd Length: 312  Bit Score: 62.56  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533 364 KLRVGLLCTGRElrpVGaplrHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERL-DALAEKADLLVTTGGVSA 442
Cdd:cd03522   159 PLRVGLIVTGSE---VY----GGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIaEALEAGAELLILTGGASV 231

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934805533 443 GESDYVGKLLAERNAVVIRQIA-VKPGRPFLFARWRGKPLFGLPGTpaavfVLYY-----DLIRPRV 503
Cdd:cd03522   232 DPDDVTPAAIRAAGGEVIRYGMpVDPGNLLLLGYLGGVPVIGLPGC-----ARSPklngfDLVLPRL 293
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 366-439 2.09e-07

Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.


Pssm-ID: 238450 [Multi-domain]  Cd Length: 170  Bit Score: 50.95  E-value: 2.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934805533 366 RVGLLCTGRELrpvgapLrHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGG 439
Cdd:cd00885     1 TAEIIAIGDEL------L-SGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
PRK14493 PRK14493
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoaE; ...
 9-120 2.12e-06

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoaE; Provisional


Pssm-ID: 237730 [Multi-domain]  Cd Length: 274  Bit Score: 49.61  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   9 AIAFVGRSGAGKTTLLCSVLRILRAKGiRVAAIKHAHKGfEIDYPGKDSRRLREAGANPVLLVGPTRLARIEelappREP 88
Cdd:PRK14493    3 VLSIVGYKATGKTTLVERLVDRLSGRG-RVGTVKHMDTE-RLNPDGTDTGRHFDAGADVVYGLTDGEWVASG-----RDR 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1934805533  89 EIAEAIALLGPTpVDLLLIEGFRAEGVPKIEL 120
Cdd:PRK14493   76 SLDDALDDLAPG-MDYAVVEGFKDSRLPKVVL 106
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 5-108 6.23e-05

Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 44.28  E-value: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   5 WRPPAIAFVGRSGAGKTTLLCSVLRILRAKgIRVAAIkhahkgfEID-YPGKDSRRLREAGAnPVLLV----GPTRLARI 79
Cdd:COG0378    11 KGVLAVNLMGSPGSGKTTLLEKTIRALKDR-LRIAVI-------EGDiYTTEDAERLRAAGV-PVVQIntggCCHLDASM 81

                          90       100
                  ....*....|....*....|....*....
gi 1934805533  80 eelapprepeIAEAIALLGPTPVDLLLIE 108
Cdd:COG0378    82 ----------VLEALEELDLPDLDLLFIE 100
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
 366-439 7.25e-05

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 45.55  E-value: 7.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934805533 366 RVGLLCTGRELrpvgapLRhGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGG 439
Cdd:PRK00549    2 KAEIIAVGTEL------LL-GQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGG 68
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 8-44 2.74e-04

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 40.49  E-value: 2.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1934805533   8 PAIAFVG-RSGAGKTTLLCSVLRILRAKGIRVAAIKHA 44
Cdd:cd01983     1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
PRK03673 PRK03673
nicotinamide mononucleotide deamidase-related protein YfaY;
365-439 2.82e-04

nicotinamide mononucleotide deamidase-related protein YfaY;


Pssm-ID: 179629 [Multi-domain]  Cd Length: 396  Bit Score: 43.53  E-value: 2.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934805533 365 LRVGLLCTGRELRpvgaplrHGEIYDSNRAFLSSALAELGVVLVDEGIVDDDSRVLEERLDALAEKADLLVTTGG 439
Cdd:PRK03673    2 LRVEMLSTGDEVL-------HGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGG 69
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 10-109 4.03e-03

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 39.25  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  10 IAFVG-RSGAGKTTLLCSVLRILRAKGIRVAAIK-------HAHKGFEIDY-----------PGKDSRR-----LREAGA 65
Cdd:pfam01656   1 IAIAGtKGGVGKTTLAANLARALARRGLRVLLIDldpqsnnSSVEGLEGDIapalqalaeglKGRVNLDpillkEKSDEG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1934805533  66 NPVLLVGPTRL--ARIEELAPPREPEIAEAIALLGPTpVDLLLIEG 109
Cdd:pfam01656  81 GLDLIPGNIDLekFEKELLGPRKEERLREALEALKED-YDYVIIDG 125
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 6-41 5.80e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 37.74  E-value: 5.80e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1934805533    6 RPPAIAFVGRSGAGKTTLLCSVLRILRAKGIRVAAI 41
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI 36
HypB cd05390
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ...
 9-108 7.55e-03

nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the maturation of nickel-dependent hydrogenases, like carbon monoxide dehydrogenase or urease. HypB is a GTP-binding protein and has GTP hyrolase activity. It forms homodimer and is capable of binding two nickel ions and two zinc ions. The active site is located on the dimer interface. Energy from hydrolysis of GTP is used to insert nickels into hydrogenases.


Pssm-ID: 349775  Cd Length: 203  Bit Score: 37.96  E-value: 7.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533   9 AIAFVGRSGAGKTTLLCSVLRILRAKgIRVAAIkhahkgfEIDYPGK-DSRRLREAGAnPVLLVGPTRLARIEelapprE 87
Cdd:cd05390    23 ALNLMSSPGSGKTTLLERTIDALKDE-LKIAVI-------EGDLETDnDAERIRATGV-PAIQINTGGACHLD------A 87

                          90       100
                  ....*....|....*....|.
gi 1934805533  88 PEIAEAIALLGPTPVDLLLIE 108
Cdd:cd05390    88 DMVARALHDLDLDELDLLFIE 108
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
 17-123 8.11e-03

Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439902 [Multi-domain]  Cd Length: 222  Bit Score: 38.22  E-value: 8.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934805533  17 GAGKTTLLCSVLRILRAKGIRVAAIKHAHKGFEIDYPGK---DSRRLREAGANPVL--LVGPTRL---------ARIEEL 82
Cdd:COG0132    12 DVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLrngDAELLRRLSGLPLSyeLVNPYRFeeplsphlaARLEGV 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1934805533  83 APPREpEIAEAIALLgPTPVDLLLIEGfrAEGvpkieLFVP 123
Cdd:COG0132    92 PIDLD-KILAALRAL-AARYDLVLVEG--AGG-----LLVP 123
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
 8-66 9.28e-03

CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.


Pssm-ID: 396860  Cd Length: 179  Bit Score: 37.62  E-value: 9.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1934805533   8 PAIAFVGRSGAGKTTLLCSVLRiLRAKGIRVAAIKHahkgfEIDYPGKDSRRLREAGAN 66
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLK-QNRAGLRIAVIVN-----EFGETGIDAELLSETGVL 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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