|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
9-410 |
1.26e-164 |
|
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: 467.36 E-value: 1.26e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 9 FEKAKESIIHSLRHIRAdqEKVDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTFGASESapslFLVAGEVSMG 88
Cdd:cd00887 1 VEAARELLLALAPPLGT--ETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVT----LRVVGEIPAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 89 AAASMTLQPGEAVIIPTGGMLPPGADAVVMVEHSEQPDDqTALITKMVAPGENVVMKGEDLSIGTTIVAEGQKITSPHIG 168
Cdd:cd00887 75 EPPDGPLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGG-RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 169 ALAAAGMASVNVRKKIFVTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALS 248
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 249 YSDVVVISGGSSVGTRDYTVQAIKGMNqAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLVKLAIRQLQ 328
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLEELG-GEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 329 GHQEaSSRHTLVASLTRNIPSAPGRDDFFPAKLFKQEGQYRATPLFG-KSGLIHLLTEADGLIHIPSEKSGLYEGDKVDV 407
Cdd:cd00887 313 GAPE-PEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGqGSGLLSSLARADGLIVIPEGVEGLEAGEEVEV 391
|
...
gi 1774439266 408 LVM 410
Cdd:cd00887 392 LLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
7-408 |
7.31e-164 |
|
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: 465.72 E-value: 7.31e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 7 ISFEKAKESIihsLRHIRA-DQEKVDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTFGAsesAPSLFLVAGEV 85
Cdd:COG0303 2 ISVEEALALI---LAAVRPlGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGA---NPVTLRVVGEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 86 SMGAAASMTLQPGEAVIIPTGGMLPPGADAVVMVEHSEQPDDqTALITKMVAPGENVVMKGEDLSIGTTIVAEGQKITSP 165
Cdd:COG0303 76 AAGSPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGD-RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 166 HIGALAAAGMASVNVRKKIFVTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALAD 245
Cdd:COG0303 155 DLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 246 ALSYSDVVVISGGSSVGTRDYTVQAIKGMNqAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLVKLAIR 325
Cdd:COG0303 235 ALAEADLVITSGGVSVGDYDLVKEALEELG-AEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 326 QLQGHQEASSRhTLVASLTRNIPSAPGRDDFFPAKLFKQEGQYRATPL-FGKSGLIHLLTEADGLIHIPSEKSGLYEGDK 404
Cdd:COG0303 314 KLAGLPPPPPP-RVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLgGQGSGLLSSLAEADGLIVLPEGVEGVEAGEE 392
|
....
gi 1774439266 405 VDVL 408
Cdd:COG0303 393 VEVL 396
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
1-407 |
1.32e-146 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 430.40 E-value: 1.32e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 1 MEFFQAISFEKAKESIIHSLRHIRADQEKVDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTFGASESAPSLFL 80
Cdd:PRK14498 4 KIFLTLVSLEEAREILESLLSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 81 VAGEVSMGAAASMTLQPGEAVIIPTGGMLPPGADAVVMVEHSEQPDDQTALITKMVAPGENVVMKGEDLSIGTTIVAEGQ 160
Cdd:PRK14498 84 LGGEVHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 161 KITSPHIGALAAAGMASVNVRKKIFVTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFS 240
Cdd:PRK14498 164 RLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 241 KALADALSYSDVVVISGGSSVGTRDYTVQAIKgmNQAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLV 320
Cdd:PRK14498 244 AALRKALKECDLVLLSGGTSAGAGDVTYRVIE--ELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 321 KLAIRQLQGhQEASSRHTLVASLTRNIPSAPGRDDFFPAKLFKQEGQYRATPLFGKSGLIHLLTEADGLIHIPSEKSGLY 400
Cdd:PRK14498 322 APLLRKLAG-LPPPERATVKARLARRVRSELGREEFVPVSLGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGLE 400
|
....*..
gi 1774439266 401 EGDKVDV 407
Cdd:PRK14498 401 AGEEVEV 407
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
23-174 |
7.07e-49 |
|
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: 162.74 E-value: 7.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 23 IRADQEKVDLP--QALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTFGASESAPslflvageVSMGAAASMTLQPGEA 100
Cdd:pfam03453 2 LLGTEETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774439266 101 VIIPTGGMLPPGADAVVMVEHSEQPDDQTALITKMVAPGENVVMKGEDLSIGTTIVAEGQKITSPHIGALAAAG 174
Cdd:pfam03453 74 VRIMTGAPLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
188-319 |
2.88e-37 |
|
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: 131.94 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 188 ILSTGDELVditataEVGQIRDTNSYALAAMLEAYGCEVRRWGIV--KDRYEDFSKALADALSYSDVVVISGGSSVGTRD 265
Cdd:smart00852 2 IISTGDELL------SGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774439266 266 YTVQAIKGMNQAQLLFHGLAIKPGKPTIY---------GIVGSVPVFGLPGHPVAAMTICELL 319
Cdd:smart00852 76 LTPEALAELGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
186-321 |
6.36e-34 |
|
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: 123.58 E-value: 6.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 186 VTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGGSSVGTRD 265
Cdd:TIGR00177 3 VAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRD 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774439266 266 YTVQAIKGM---------NQAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLVK 321
Cdd:TIGR00177 83 VTPEALEELgekeipgfgEFRMLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLIL 147
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
9-410 |
1.26e-164 |
|
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: 467.36 E-value: 1.26e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 9 FEKAKESIIHSLRHIRAdqEKVDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTFGASESapslFLVAGEVSMG 88
Cdd:cd00887 1 VEAARELLLALAPPLGT--ETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVT----LRVVGEIPAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 89 AAASMTLQPGEAVIIPTGGMLPPGADAVVMVEHSEQPDDqTALITKMVAPGENVVMKGEDLSIGTTIVAEGQKITSPHIG 168
Cdd:cd00887 75 EPPDGPLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGG-RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 169 ALAAAGMASVNVRKKIFVTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALS 248
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 249 YSDVVVISGGSSVGTRDYTVQAIKGMNqAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLVKLAIRQLQ 328
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLEELG-GEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 329 GHQEaSSRHTLVASLTRNIPSAPGRDDFFPAKLFKQEGQYRATPLFG-KSGLIHLLTEADGLIHIPSEKSGLYEGDKVDV 407
Cdd:cd00887 313 GAPE-PEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGqGSGLLSSLARADGLIVIPEGVEGLEAGEEVEV 391
|
...
gi 1774439266 408 LVM 410
Cdd:cd00887 392 LLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
7-408 |
7.31e-164 |
|
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: 465.72 E-value: 7.31e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 7 ISFEKAKESIihsLRHIRA-DQEKVDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTFGAsesAPSLFLVAGEV 85
Cdd:COG0303 2 ISVEEALALI---LAAVRPlGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGA---NPVTLRVVGEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 86 SMGAAASMTLQPGEAVIIPTGGMLPPGADAVVMVEHSEQPDDqTALITKMVAPGENVVMKGEDLSIGTTIVAEGQKITSP 165
Cdd:COG0303 76 AAGSPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGD-RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 166 HIGALAAAGMASVNVRKKIFVTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALAD 245
Cdd:COG0303 155 DLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 246 ALSYSDVVVISGGSSVGTRDYTVQAIKGMNqAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLVKLAIR 325
Cdd:COG0303 235 ALAEADLVITSGGVSVGDYDLVKEALEELG-AEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 326 QLQGHQEASSRhTLVASLTRNIPSAPGRDDFFPAKLFKQEGQYRATPL-FGKSGLIHLLTEADGLIHIPSEKSGLYEGDK 404
Cdd:COG0303 314 KLAGLPPPPPP-RVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLgGQGSGLLSSLAEADGLIVLPEGVEGVEAGEE 392
|
....
gi 1774439266 405 VDVL 408
Cdd:COG0303 393 VEVL 396
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
1-407 |
1.32e-146 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 430.40 E-value: 1.32e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 1 MEFFQAISFEKAKESIIHSLRHIRADQEKVDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTFGASESAPSLFL 80
Cdd:PRK14498 4 KIFLTLVSLEEAREILESLLSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 81 VAGEVSMGAAASMTLQPGEAVIIPTGGMLPPGADAVVMVEHSEQPDDQTALITKMVAPGENVVMKGEDLSIGTTIVAEGQ 160
Cdd:PRK14498 84 LGGEVHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 161 KITSPHIGALAAAGMASVNVRKKIFVTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFS 240
Cdd:PRK14498 164 RLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 241 KALADALSYSDVVVISGGSSVGTRDYTVQAIKgmNQAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLV 320
Cdd:PRK14498 244 AALRKALKECDLVLLSGGTSAGAGDVTYRVIE--ELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 321 KLAIRQLQGhQEASSRHTLVASLTRNIPSAPGRDDFFPAKLFKQEGQYRATPLFGKSGLIHLLTEADGLIHIPSEKSGLY 400
Cdd:PRK14498 322 APLLRKLAG-LPPPERATVKARLARRVRSELGREEFVPVSLGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGLE 400
|
....*..
gi 1774439266 401 EGDKVDV 407
Cdd:PRK14498 401 AGEEVEV 407
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
28-409 |
3.72e-80 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 256.66 E-value: 3.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 28 EKVDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTfgasesaPSLFLVAGEVSMGAAASMTLQPGEAVIIPTGG 107
Cdd:PRK14497 31 VKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCT-------PGEFKVIDKIGIGEFKEIHIKECEAVEVDTGS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 108 MLPPGADAVVMVEHSEQPDDQTALITKMVAPGENVVMKGEDLSIGTTIVAEGQKITSPHIGALAAAGMASVNVRKKIFVT 187
Cdd:PRK14497 104 MIPMGADAVIKVENTKVINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 188 ILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGGSSVGTRDYT 267
Cdd:PRK14497 184 LIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKDFV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 268 VQAIKGMnqAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLVKLAIRQLQG-HQEASSRHTLVASLTRN 346
Cdd:PRK14497 264 HQAIREL--GNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPsRKEILGLGKIKARLALR 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774439266 347 IPSAPGRDDFFPAKLFKQEGQYRATPLFGKSGLIHLLTEADGLIHI-PSEKsgLYEGDKVDVLV 409
Cdd:PRK14497 342 VKADEHRNTLIPVYLFKSDNSYYALPVPFDSYMVGTFSLTDGYIMLgPNEE--IEEGKEVEVDL 403
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
25-405 |
3.16e-73 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 239.90 E-value: 3.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 25 ADQEKVDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTfgasesAPSLFLVAGEVSMGAAASMTLQPGEAVIIP 104
Cdd:PRK14491 216 TETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDL------EPESYTLVGEVLAGHQYDGTLQAGEAVRIM 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 105 TGGMLPPGADAVVMVEHSEQPDDQTALITKMVApGENVVMKGEDLSIGTTIVAEGQKITSPHIGALAAAGMASVNVRKKI 184
Cdd:PRK14491 290 TGAPVPAGADTVVMRELATQDGDKVSFDGGIKA-GQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRP 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 185 FVTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGGSSVGTR 264
Cdd:PRK14491 369 KVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 265 DYTVQAIKGMNQAQllFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMtICEL-LVKLAIRQLQGHQEASSRhTLVASL 343
Cdd:PRK14491 449 DYIKTALAKLGQID--FWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVM-VSFLqFVEPALRKLAGEQNWQPL-LFPAIA 524
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774439266 344 TRNIPSAPGRDDFFPAKL-FKQEGQY--RATPLFGkSGLIHLLTEADGLIHIPSEKSGLYEGDKV 405
Cdd:PRK14491 525 DETLRSRQGRTEFSRGIYhLGADGRLhvRTTGKQG-SGILSSMSEANCLIEIGPAAETVNAGETV 588
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
7-356 |
1.00e-65 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 215.34 E-value: 1.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 7 ISFEKAKESIIHSLRHIrADQEKVDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTfgaSESAPslFLVAGEVS 86
Cdd:PRK10680 8 MSLETALTEMLSRVTPL-TATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADL---ASGQP--LPVAGKAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 87 MGAAASMTLQPGEAVIIPTGGMLPPGADAVVMVEHSEQPDDqTALITKMVAPGENVVMKGEDLSIGTTIVAEGQKITSPH 166
Cdd:PRK10680 82 AGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDD-GVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 167 IGALAAAGMASVNVRKKIFVTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADA 246
Cdd:PRK10680 161 LPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 247 LSYSDVVVISGGSSVGTRDYTVQAIKGMnqAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPV-AAMTICELLVKLaIR 325
Cdd:PRK10680 241 DSQADVVISSGGVSVGEADYTKTILEEL--GEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVsAALTFYQLVQPL-LA 317
|
330 340 350
....*....|....*....|....*....|.
gi 1774439266 326 QLQGHQEASSRHTLVASLTRNIPSAPGRDDF 356
Cdd:PRK10680 318 KLSGNTASGLPPRQRVRTASRLKKTPGRLDF 348
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
26-405 |
5.18e-50 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 174.34 E-value: 5.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 26 DQEKVDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSAdtfgASESAPSLFLVAGEVSMGAAASMTLQPGEAVIIPT 105
Cdd:PRK14690 41 DIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGA----APEGAQVLPLIEGRAAAGVPFSGRVPEGMALRILT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 106 GGMLPPGADAVVMvEHSEQPDDQTALITKMVAPGENVVMKGEDLSIGTTIVAEGQKITSPHIGALAAAGMASVNVRKKIF 185
Cdd:PRK14690 117 GAALPEGVDTVVL-EEDVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 186 VTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGGSSVGTRD 265
Cdd:PRK14690 196 VAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDED 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 266 YT---VQAIKGMNQAQllfhgLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLVKLAIRQLQGHQ-EASSRHTLVA 341
Cdd:PRK14690 276 HVsalLREAGAMQSWR-----IALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEGwSEPQGFTVPA 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774439266 342 SLTRNipSAPGRDDFFPAKL-------FKQEGqyratplfgkSGLIHLLTEADGLIHIPSEKSGLYEGDKV 405
Cdd:PRK14690 351 AFEKR--KKPGRREYLRARLrqghaevFRSEG----------SGRISGLSWAEGLVELGDGARRIAPGDPV 409
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
23-174 |
7.07e-49 |
|
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: 162.74 E-value: 7.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 23 IRADQEKVDLP--QALHRIAATHVIAQENLPPFSRSTVDGFAVRSADTFGASESAPslflvageVSMGAAASMTLQPGEA 100
Cdd:pfam03453 2 LLGTEETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774439266 101 VIIPTGGMLPPGADAVVMVEHSEQPDDQTALITKMVAPGENVVMKGEDLSIGTTIVAEGQKITSPHIGALAAAG 174
Cdd:pfam03453 74 VRIMTGAPLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
30-356 |
2.13e-46 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 168.84 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 30 VDLPQALHRIAATHVIAQENLPPFSRSTVDGFAVRSADtfgasesAPSLFLVAGEVSMGAAAS-MTLQPGEAVIIPTGGM 108
Cdd:PLN02699 29 VPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASD-------GPGEYPVITESRAGNDGLgVTLTPGTVAYVTTGGP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 109 LPPGADAVVMVEHSEQPDD-----QTALITKMVAPGENVVMKGEDLSIGTTIVAEGQKITSPHIGALAAAGMASVNVRKK 183
Cdd:PLN02699 102 IPDGADAVVQVEDTEVVEDpldgsKRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVYPR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 184 IFVTILSTGDELVD-ITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYS-DVVVISGGSSV 261
Cdd:PLN02699 182 PTVAILSTGDELVEpTTGTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAISSGvDILLTSGGVSM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 262 GTRDYTVQAIKgmNQAQLLFHGLAIKPGKPTIYGIVGSVP---------VFGLPGHPVAAMTICELLVKLAIRQLQGHQE 332
Cdd:PLN02699 262 GDRDFVKPLLE--KRGTVYFSKVLMKPGKPLTFAEIDAKSapsnskkmlAFGLPGNPVSCLVCFNLFVVPAIRYLAGWSN 339
|
330 340
....*....|....*....|....
gi 1774439266 333 ASSRHtLVASLTRNIPSAPGRDDF 356
Cdd:PLN02699 340 PHLLR-VQARLREPIKLDPVRPEF 362
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
188-319 |
2.88e-37 |
|
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: 131.94 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 188 ILSTGDELVditataEVGQIRDTNSYALAAMLEAYGCEVRRWGIV--KDRYEDFSKALADALSYSDVVVISGGSSVGTRD 265
Cdd:smart00852 2 IISTGDELL------SGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774439266 266 YTVQAIKGMNQAQLLFHGLAIKPGKPTIY---------GIVGSVPVFGLPGHPVAAMTICELL 319
Cdd:smart00852 76 LTPEALAELGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
186-321 |
6.36e-34 |
|
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: 123.58 E-value: 6.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 186 VTILSTGDELVDITATAEVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGGSSVGTRD 265
Cdd:TIGR00177 3 VAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRD 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774439266 266 YTVQAIKGM---------NQAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLVK 321
Cdd:TIGR00177 83 VTPEALEELgekeipgfgEFRMLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLIL 147
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
188-326 |
1.10e-33 |
|
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: 122.74 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 188 ILSTGDELVDitataevGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGGSSVGTRDYT 267
Cdd:pfam00994 2 IITTGDELLP-------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVT 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774439266 268 VQAI-----KGMNQAQLLFHGLAIKPGKPTIYGIV-----GSVPVFGLPGHPVAAMTICELLVKLAIRQ 326
Cdd:pfam00994 75 PEALaelggRELPGFEELFRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
186-324 |
9.89e-32 |
|
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: 117.06 E-value: 9.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 186 VTILSTGDELVDitataevGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGGSSVGTRD 265
Cdd:cd00758 2 VAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1774439266 266 YTVQAIKGMNQAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPGHPVAAMTICELLVKLAI 324
Cdd:cd00758 75 VTPEALAELGEREAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
341-409 |
3.92e-13 |
|
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this domain is uncertain. The structure of this domain is known and forms an incomplete beta barrel.
Pssm-ID: 460924 [Multi-domain] Cd Length: 72 Bit Score: 64.17 E-value: 3.92e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 341 ASLTRNIPSAPGRDDFFPAKLFKQEGQYRATPL-FGKSGLIHLLTEADGLIHIPSEKSGLYEGDKVDVLV 409
Cdd:pfam03454 2 ARLARDLKSDPGRREFVRVRLHEEDGRYYAEPIgKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVIL 71
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
188-271 |
2.21e-11 |
|
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: 62.12 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 188 ILSTGDELVDitataevGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGGssVG-TR-D 265
Cdd:cd00885 4 IIAIGDELLS-------GQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG--LGpTHdD 74
|
....*.
gi 1774439266 266 YTVQAI 271
Cdd:cd00885 75 LTREAV 80
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
198-307 |
4.79e-08 |
|
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: 54.09 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 198 ITATAEVGQ--IRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADAL-SYSDVVVISGGSSVGTRDYTVQAIK-- 272
Cdd:cd03522 165 IVTGSEVYGgrIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEALeAGAELLILTGGASVDPDDVTPAAIRaa 244
|
90 100 110
....*....|....*....|....*....|....*
gi 1774439266 273 GmnqAQLLFHGLAIKPGKPTIYGIVGSVPVFGLPG 307
Cdd:cd03522 245 G---GEVIRYGMPVDPGNLLLLGYLGGVPVIGLPG 276
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
214-330 |
6.92e-08 |
|
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 51.66 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 214 ALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYS--DVVVISGGSSVGTRDYTVQAIKGMNQAQL-----LFHGLAI 286
Cdd:COG0521 33 ALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEgvDLVLTTGGTGLSPRDVTPEATRPLLDKELpgfgeLFRALSL 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1774439266 287 KPGKPTIY------GIVGSVPVFGLPGHPVAAMTICELLVKL---AIRQLQGH 330
Cdd:COG0521 113 EEIGPSAIlsravaGIRGGTLIFNLPGSPGAVREALEAILPElphAVDLLNGV 165
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
185-276 |
2.38e-06 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 48.47 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 185 FVTILSTGDELVditataeVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGGSSVGTR 264
Cdd:PRK01215 5 FAWIITIGNELL-------IGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYD 77
|
90
....*....|...
gi 1774439266 265 DYTVQAI-KGMNQ 276
Cdd:PRK01215 78 DKTNEGFaKALGV 90
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
214-312 |
8.28e-06 |
|
MogA_MoaB 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). MogA, together with MoeA, 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. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.
Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 45.55 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 214 ALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYS--DVVVISGGSSVGTRDYTVQAIKGMNQAQL-----LFHGLAI 286
Cdd:cd00886 24 ALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDgvDLILTTGGTGLAPRDVTPEATRPLLDKELpgfgeAFRALSL 103
|
90 100 110
....*....|....*....|....*....|.
gi 1774439266 287 KPGKPTIY-----GIVGSVPVFGLPGHPVAA 312
Cdd:cd00886 104 EETGTAMLsravaGIRGGTLIFNLPGSPKAV 134
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
186-287 |
8.94e-06 |
|
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 161761 [Multi-domain] Cd Length: 413 Bit Score: 47.59 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 186 VTILSTGDELVditataeVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGGSSVGTRD 265
Cdd:TIGR00200 3 AEIISVGDELL-------LGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDD 75
|
90 100
....*....|....*....|..
gi 1774439266 266 YTVQAIKGMNQAQLLFHGLAIK 287
Cdd:TIGR00200 76 LTAETIATAKGEPLVLNEAWLK 97
|
|
| PRK03670 |
PRK03670 |
competence damage-inducible protein A; Provisional |
184-271 |
4.32e-05 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 167581 Cd Length: 252 Bit Score: 44.79 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774439266 184 IFVTILSTGDELVditataeVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYS-DVVVISGGSSVG 262
Cdd:PRK03670 1 MFAEIITVGDELL-------TGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKpEVLVISGGLGPT 73
|
....*....
gi 1774439266 263 TRDYTVQAI 271
Cdd:PRK03670 74 HDDVTMLAV 82
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
188-258 |
2.41e-04 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 42.85 E-value: 2.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774439266 188 ILSTGDELVditataeVGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGG 258
Cdd:PRK00549 5 IIAVGTELL-------LGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGG 68
|
|
| PRK03673 |
PRK03673 |
nicotinamide mononucleotide deamidase-related protein YfaY; |
184-258 |
2.51e-03 |
|
nicotinamide mononucleotide deamidase-related protein YfaY;
Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 39.68 E-value: 2.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774439266 184 IFVTILSTGDELVDitataevGQIRDTNSYALAAMLEAYGCEVRRWGIVKDRYEDFSKALADALSYSDVVVISGG 258
Cdd:PRK03673 2 LRVEMLSTGDEVLH-------GQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGG 69
|
|
| |
