|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
3-399 |
7.30e-145 |
|
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: 417.18 E-value: 7.30e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 3 LTSVNDATRIILENTLDYGAESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQWQSYQK-GQRDFRIESTQTAGDV 81
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGaNPVTLRVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 82 QHTLQNPAACIEVMTGASLPINTDTVIKYEDVAIENGVAQLKFTVREKQNVHFRGEDRMAGSAIVPTGTLLGPPEIAIAA 161
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 162 SVGATKVKVKKLPSVVIITSGDELVPVEATPLPHQIRSSNVHCIATLLKPYQIEV-DFIHIPDDLATTQEAIQQALQQYD 240
Cdd:COG0303 161 SLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVvDLGIVPDDPEALRAALREALAEAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 241 VLILCGGVSQGKKDFIPKALQAEGVQKYFHKLSQQPGKPFWFGRKDRNVVFALPGNPVSSFLCARRYFIPWLRQSLGLVA 320
Cdd:COG0303 241 LVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 321 FDHT--YAALSADYVYTSPLTYFLQVQLYQENATLMARPVMGHGSGDFANLVENQGFLELPKEQTEFKKGDIFPLWRYDT 398
Cdd:COG0303 321 PPPPrvRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLLLDG 400
|
.
gi 1509195002 399 L 399
Cdd:COG0303 401 L 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
6-394 |
3.40e-139 |
|
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: 402.64 E-value: 3.40e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 6 VNDATRIILENTLDYGAESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQWQSYQKGQRDFRIESTQTAGDVQHTL 85
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRVVGEIPAGEPPDGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 86 QNPAACIEVMTGASLPINTDTVIKYEDVAIENGVAQLKFTVREKQNVHFRGEDRMAGSAIVPTGTLLGPPEIAIAASVGA 165
Cdd:cd00887 81 LGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 166 TKVKVKKLPSVVIITSGDELVPVEATPLPHQIRSSNVHCIATLLKPYQIEV-DFIHIPDDLATTQEAIQQALQQYDVLIL 244
Cdd:cd00887 161 AEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVvDLGIVPDDPEALREALEEALEEADVVIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 245 CGGVSQGKKDFIPKALQAEGVQKYFHKLSQQPGKPFWFGRKDRNVVFALPGNPVSSFLCARRYFIPWLRQSLGLVAFDHT 324
Cdd:cd00887 241 SGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1509195002 325 --YAALSADYVYTSPLTYFLQVQLYQENATLMARPVMGHGSGDFANLVENQGFLELPKEQTEFKKGDIFPLW 394
Cdd:cd00887 321 rvKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVL 392
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
2-385 |
6.82e-68 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 226.25 E-value: 6.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 2 ELTSVNDATRIILE--NTLDYGAESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQ----WQSYQKGQRDFRIEST 75
Cdd:PRK14498 8 TLVSLEEAREILESllSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRaadtFGASEANPVRLKLGGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 76 QTAGDVQHTLQNPAACIEVMTGASLPINTDTVIKYEDV-AIENGVAQLKFTVREKQNVHFRGEDRMAGSAIVPTGTLLGP 154
Cdd:PRK14498 88 VHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTeEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 155 PEIAIAASVGATKVKVKKLPSVVIITSGDELVPVEATPLPHQIRSSNVHCIATLLKPYQIEVDFI-HIPDDLATTQEAIQ 233
Cdd:PRK14498 168 RDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYgIVPDDEEELEAALR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 234 QALQQYDVLILCGGVSQGKKDFIPKALQAEGvQKYFHKLSQQPGKPFWFGRKDRNVVFALPGNPVSSFLCARRYFIPWLR 313
Cdd:PRK14498 248 KALKECDLVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLR 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1509195002 314 QSLGLvaFDHTYAALSAD--YVYTSPL--TYFLQVQLYQENATLMARPVMGhGSGDFANLVENQGFLELPkEQTEF 385
Cdd:PRK14498 327 KLAGL--PPPERATVKARlaRRVRSELgrEEFVPVSLGRVGDGYVAYPLSR-GSGAITSLVRADGFIEIP-ANTEG 398
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
24-164 |
2.04e-40 |
|
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: 140.39 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 24 SVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQWQSYQKGQRDFRIEstqtAGDVQHTLQNPAACIEVMTGASLPIN 103
Cdd:pfam03453 10 PLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIA----AGEPPGPLLPGGEAVRIMTGAPLPEG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1509195002 104 TDTVIKYEDVAIENGVAQLKFT-VREKQNVHFRGEDRMAGSAIVPTGTLLGPPEIAIAASVG 164
Cdd:pfam03453 86 ADAVVMVEDTEEGGGRTVEIRApVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
174-310 |
3.15e-27 |
|
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: 105.48 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 174 PSVVIITSGDELVPVEATPLPHQIRSSNVHCIATLLKPYQIEVDFI-HIPDDLATTQEAIQQALQQYDVLILCGGVSQGK 252
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLgIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1509195002 253 KDFIPKALQA------EGVQKYFHKLSQ----QPGKPFWFGRKDRNVVFALPGNPVSSFLCARRYFIP 310
Cdd:TIGR00177 81 RDVTPEALEElgekeiPGFGEFRMLSSLpvlsRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-303 |
1.26e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 100.74 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 178 IITSGDELVPveatplPHQIRSSNVHCIATLLKPYQIEVDFIHI---PDDLATTQEAIQQALQQYDVLILCGGVSQGKKD 254
Cdd:smart00852 2 IISTGDELLS------GGQIRDSNGPMLAALLRELGIEVVRVVVvggPDDPEAIREALREALAEADVVITTGGTGPGPDD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1509195002 255 FIPKAL-QAEGVQKYFHKLSQQPGKPF-----WFGRKD----RNVVFALPGNPVSSFLC 303
Cdd:smart00852 76 LTPEALaELGGRELLGHGVAMRPGGPPgplanLSGTAPgvrgKKPVFGLPGNPVAALVM 134
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
3-399 |
7.30e-145 |
|
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: 417.18 E-value: 7.30e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 3 LTSVNDATRIILENTLDYGAESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQWQSYQK-GQRDFRIESTQTAGDV 81
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGaNPVTLRVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 82 QHTLQNPAACIEVMTGASLPINTDTVIKYEDVAIENGVAQLKFTVREKQNVHFRGEDRMAGSAIVPTGTLLGPPEIAIAA 161
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 162 SVGATKVKVKKLPSVVIITSGDELVPVEATPLPHQIRSSNVHCIATLLKPYQIEV-DFIHIPDDLATTQEAIQQALQQYD 240
Cdd:COG0303 161 SLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVvDLGIVPDDPEALRAALREALAEAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 241 VLILCGGVSQGKKDFIPKALQAEGVQKYFHKLSQQPGKPFWFGRKDRNVVFALPGNPVSSFLCARRYFIPWLRQSLGLVA 320
Cdd:COG0303 241 LVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 321 FDHT--YAALSADYVYTSPLTYFLQVQLYQENATLMARPVMGHGSGDFANLVENQGFLELPKEQTEFKKGDIFPLWRYDT 398
Cdd:COG0303 321 PPPPrvRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLLLDG 400
|
.
gi 1509195002 399 L 399
Cdd:COG0303 401 L 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
6-394 |
3.40e-139 |
|
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: 402.64 E-value: 3.40e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 6 VNDATRIILENTLDYGAESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQWQSYQKGQRDFRIESTQTAGDVQHTL 85
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRVVGEIPAGEPPDGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 86 QNPAACIEVMTGASLPINTDTVIKYEDVAIENGVAQLKFTVREKQNVHFRGEDRMAGSAIVPTGTLLGPPEIAIAASVGA 165
Cdd:cd00887 81 LGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 166 TKVKVKKLPSVVIITSGDELVPVEATPLPHQIRSSNVHCIATLLKPYQIEV-DFIHIPDDLATTQEAIQQALQQYDVLIL 244
Cdd:cd00887 161 AEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVvDLGIVPDDPEALREALEEALEEADVVIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 245 CGGVSQGKKDFIPKALQAEGVQKYFHKLSQQPGKPFWFGRKDRNVVFALPGNPVSSFLCARRYFIPWLRQSLGLVAFDHT 324
Cdd:cd00887 241 SGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1509195002 325 --YAALSADYVYTSPLTYFLQVQLYQENATLMARPVMGHGSGDFANLVENQGFLELPKEQTEFKKGDIFPLW 394
Cdd:cd00887 321 rvKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVL 392
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
2-385 |
6.82e-68 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 226.25 E-value: 6.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 2 ELTSVNDATRIILE--NTLDYGAESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQ----WQSYQKGQRDFRIEST 75
Cdd:PRK14498 8 TLVSLEEAREILESllSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRaadtFGASEANPVRLKLGGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 76 QTAGDVQHTLQNPAACIEVMTGASLPINTDTVIKYEDV-AIENGVAQLKFTVREKQNVHFRGEDRMAGSAIVPTGTLLGP 154
Cdd:PRK14498 88 VHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTeEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 155 PEIAIAASVGATKVKVKKLPSVVIITSGDELVPVEATPLPHQIRSSNVHCIATLLKPYQIEVDFI-HIPDDLATTQEAIQ 233
Cdd:PRK14498 168 RDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYgIVPDDEEELEAALR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 234 QALQQYDVLILCGGVSQGKKDFIPKALQAEGvQKYFHKLSQQPGKPFWFGRKDRNVVFALPGNPVSSFLCARRYFIPWLR 313
Cdd:PRK14498 248 KALKECDLVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLR 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1509195002 314 QSLGLvaFDHTYAALSAD--YVYTSPL--TYFLQVQLYQENATLMARPVMGhGSGDFANLVENQGFLELPkEQTEF 385
Cdd:PRK14498 327 KLAGL--PPPERATVKARlaRRVRSELgrEEFVPVSLGRVGDGYVAYPLSR-GSGAITSLVRADGFIEIP-ANTEG 398
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
2-300 |
7.67e-53 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 184.24 E-value: 7.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 2 ELTSVNDATRIILeNTLDY--GAESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQwQSYQKGQrdFRIESTQTAG 79
Cdd:PRK14497 9 SLYSIDEAIKVFL-SSLNFkpKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALK-SSCTPGE--FKVIDKIGIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 80 DVQHTLQNPAACIEVMTGASLPINTDTVIKYEDVAIENG-VAQLKFTVREKQNVHFRGEDRMAGSAIVPTGTLLGPPEIA 158
Cdd:PRK14497 85 EFKEIHIKECEAVEVDTGSMIPMGADAVIKVENTKVINGnFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 159 IAASVGATKVKVKKLPSVVIITSGDELVPVEATPLPHQIRSSNVHCIATLLKP--YQIeVDFIHIPDDLATTQEAIQQAL 236
Cdd:PRK14497 165 LLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSegYKI-VGLSLLSDDKESIKNEIKRAI 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1509195002 237 QQYDVLILCGGVSQGKKDFIPKALQAEGvQKYFHKLSQQPGKPFWFGRKDRNVVFALPGNPVSS 300
Cdd:PRK14497 244 SVADVLILTGGTSAGEKDFVHQAIRELG-NIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVST 306
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
4-393 |
9.22e-51 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 179.42 E-value: 9.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 4 TSVNDATRIILE--NTLDyGAESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQWQsyqkgqrDFRIESTQTAGDV 81
Cdd:PRK14491 199 LSVSQGLDKILSlvTPVT-ETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSD-------DLEPESYTLVGEV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 82 ------QHTLQNPAAcIEVMTGASLPINTDTVIKYEDVAIENGVAQLKFTVREKQNVHFRGEDRMAGSAIVPTGTLLGPP 155
Cdd:PRK14491 271 laghqyDGTLQAGEA-VRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAP 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 156 EIAIAASVGATKVKVKKLPSVVIITSGDElVPVEATPL-PHQIRSSNVHCIATLLKPYQIEV-DFIHIPDDLATTQEAIQ 233
Cdd:PRK14491 350 EQGLLASLGFAEVPVFRRPKVAVFSTGDE-VQAPGETLkPNCIYDSNRFTIKAMAKKLGCEViDLGIIEDSEAALEATLE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 234 QALQQYDVLILCGGVSQGKKDFIPKALQAEGvQKYFHKLSQQPGKPFWFGRKDRNVVFALPGNPVSSFLCARRYFIPWLR 313
Cdd:PRK14491 429 QAAAQADVVISSGGVSVGDADYIKTALAKLG-QIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 314 QSLGLVAFDHTYAALSADYVYTSPL--TYFLQ-VQLYQENATLMARPVMGHGSGDFANLVENQGFLELPKEQTEFKKGD- 389
Cdd:PRK14491 508 KLAGEQNWQPLLFPAIADETLRSRQgrTEFSRgIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGEt 587
|
....*.
gi 1509195002 390 --IFPL 393
Cdd:PRK14491 588 vtIQPL 593
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
21-389 |
1.61e-46 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 164.71 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 21 GAESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQwQSYQKGQRDFRIESTQTAGDVQHTLQNPAA-CIEVMTGAS 99
Cdd:PRK14690 41 DIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFA-GAAPEGAQVLPLIEGRAAAGVPFSGRVPEGmALRILTGAA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 100 LPINTDTVIKYEDVAIENGVAQLKFTVREKQNVHFRGEDRMAGSAIVPTGTLLGPPEIAIAASVGATKVKVKKLPSVVII 179
Cdd:PRK14690 120 LPEGVDTVVLEEDVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 180 TSGDELVPVEATPLPHQIRSSNVHCIATLLKPY-QIEVDFIHIPDDLATTQEAIQQALQQYDVLILCGGVSQGKKDFIPK 258
Cdd:PRK14690 200 STGDELVEPGALAEVGQIYDANRPMLLALARRWgHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHVSA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 259 ALQAEGVQKYFhKLSQQPGKPFWFGRKDRNVVFALPGNPVSSFLCArryfIPWLRQSLGLVAfdhtYAALSADYVYTSPL 338
Cdd:PRK14690 280 LLREAGAMQSW-RIALKPGRPLALGLWQGVPVFGLPGNPVAALVCT----LVFARPAMSLLA----GEGWSEPQGFTVPA 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1509195002 339 TY----------FLQVQLYQENATLMArpvmGHGSGDFANLVENQGFLELPKEQTEFKKGD 389
Cdd:PRK14690 351 AFekrkkpgrreYLRARLRQGHAEVFR----SEGSGRISGLSWAEGLVELGDGARRIAPGD 407
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
23-302 |
5.00e-46 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 162.95 E-value: 5.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 23 ESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQWQSYQKGQrDFRIESTQTAGDVQHTLQNPAACIEVMTGASLPI 102
Cdd:PRK10680 28 ETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQ-PLPVAGKAFAGQPFHGEWPAGTCIRIMTGAPVPE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 103 NTDTVIKYEDVAI-ENGVaqlKFT--VREKQNVHFRGEDRMAGSAIVPTGTLLGPPEIAIAASVGATKVKVKKLPSVVII 179
Cdd:PRK10680 107 GCEAVVMQEQTEQtDDGV---RFTaeVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 180 TSGDELVPVeATPLPH-QIRSSNVHCIATLLKPYQIEV-DFIHIPDDLATTQEAIQQALQQYDVLILCGGVSQGKKDFIP 257
Cdd:PRK10680 184 STGDELQLP-GQPLGDgQIYDTNRLAVHLMLEQLGCEViNLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTK 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1509195002 258 KALQAEGvQKYFHKLSQQPGKPFWFGRKDRNVVFALPGNPVSSFL 302
Cdd:PRK10680 263 TILEELG-EIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAAL 306
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
24-164 |
2.04e-40 |
|
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: 140.39 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 24 SVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIQWQSYQKGQRDFRIEstqtAGDVQHTLQNPAACIEVMTGASLPIN 103
Cdd:pfam03453 10 PLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIA----AGEPPGPLLPGGEAVRIMTGAPLPEG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1509195002 104 TDTVIKYEDVAIENGVAQLKFT-VREKQNVHFRGEDRMAGSAIVPTGTLLGPPEIAIAASVG 164
Cdd:pfam03453 86 ADAVVMVEDTEEGGGRTVEIRApVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
2-317 |
1.93e-39 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 149.19 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 2 ELTSVNDATRIILENTLDYGAESVAFTDAYRRVLAEPLVADRDFPPFDRVTMDGIAIqwqSYQKGQRDFRIESTQTAGD- 80
Cdd:PLN02699 6 EMISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAV---VASDGPGEYPVITESRAGNd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 81 -VQHTLQnPAACIEVMTGASLPINTDTVIKYEDVAI----ENGVAQLKFTVREKQNVHFR--GEDRMAGSAIVPTGTLLG 153
Cdd:PLN02699 83 gLGVTLT-PGTVAYVTTGGPIPDGADAVVQVEDTEVvedpLDGSKRVRILSQASKGQDIRpvGCDIEKDAKVLKAGERLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 154 PPEIAIAASVGATKVKVKKLPSVVIITSGDELV-PVEATPLPHQIRSSNVHCIATLLKPYQIEV-DFIHIPDDLATTQEA 231
Cdd:PLN02699 162 ASEIGLLATVGVTMVKVYPRPTVAILSTGDELVePTTGTLGRGQIRDSNRAMLLAAAIQQQCKVvDLGIARDDEEELERI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 232 IQQALQQ-YDVLILCGGVSQGKKDFIPKALQAEGvQKYFHKLSQQPGKPFWFGR---KDRN------VVFALPGNPVSSF 301
Cdd:PLN02699 242 LDEAISSgVDILLTSGGVSMGDRDFVKPLLEKRG-TVYFSKVLMKPGKPLTFAEidaKSAPsnskkmLAFGLPGNPVSCL 320
|
330
....*....|....*.
gi 1509195002 302 LCARRYFIPWLRQSLG 317
Cdd:PLN02699 321 VCFNLFVVPAIRYLAG 336
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
174-310 |
3.15e-27 |
|
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: 105.48 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 174 PSVVIITSGDELVPVEATPLPHQIRSSNVHCIATLLKPYQIEVDFI-HIPDDLATTQEAIQQALQQYDVLILCGGVSQGK 252
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLgIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1509195002 253 KDFIPKALQA------EGVQKYFHKLSQ----QPGKPFWFGRKDRNVVFALPGNPVSSFLCARRYFIP 310
Cdd:TIGR00177 81 RDVTPEALEElgekeiPGFGEFRMLSSLpvlsRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-314 |
1.03e-26 |
|
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: 103.87 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 178 IITSGDELvpveatpLPHQIRSSNVHCIATLLKPYQIEVDFI-HIPDDLATTQEAIQQALQQYDVLILCGGVSQGKKDFI 256
Cdd:pfam00994 2 IITTGDEL-------LPGQIRDTNGPLLAALLREAGAEVIRYgIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVT 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1509195002 257 PKALQAEGVQK------YFHKLSQQPGKPFWFGR-----KDRNVVFALPGNPVSSFLCARRYFIPWLRQ 314
Cdd:pfam00994 75 PEALAELGGRElpgfeeLFRGVSLKPGKPVGTAPgailsRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-303 |
1.26e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 100.74 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 178 IITSGDELVPveatplPHQIRSSNVHCIATLLKPYQIEVDFIHI---PDDLATTQEAIQQALQQYDVLILCGGVSQGKKD 254
Cdd:smart00852 2 IISTGDELLS------GGQIRDSNGPMLAALLRELGIEVVRVVVvggPDDPEAIREALREALAEADVVITTGGTGPGPDD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1509195002 255 FIPKAL-QAEGVQKYFHKLSQQPGKPF-----WFGRKD----RNVVFALPGNPVSSFLC 303
Cdd:smart00852 76 LTPEALaELGGRELLGHGVAMRPGGPPgplanLSGTAPgvrgKKPVFGLPGNPVAALVM 134
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
176-303 |
2.50e-16 |
|
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: 75.07 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 176 VVIITSGDELVPVeatplphQIRSSNVHCIATLLKPYQIEVDFIHI-PDDLATTQEAIQQALQQYDVLILCGGVSQGKKD 254
Cdd:cd00758 2 VAIVTVSDELSQG-------QIEDTNGPALEALLEDLGCEVIYAGVvPDDADSIRAALIEASREADLVLTTGGTGVGRRD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1509195002 255 FIPKALQAEG-VQKYFHKLSQQPGKPFWFGRKDRNVVFALPGNPVSSFLC 303
Cdd:cd00758 75 VTPEALAELGeREAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTT 124
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
178-247 |
5.02e-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: 49.40 E-value: 5.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1509195002 178 IITSGDELvpveatpLPHQIRSSNVHCIATLLKPYQIEVDFIH-IPDDLATTQEAIQQALQQYDVLILCGG 247
Cdd:cd00885 4 IIAIGDEL-------LSGQIVDTNAAFLAKELAELGIEVYRVTvVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
136-305 |
5.81e-06 |
|
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: 47.54 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 136 GEDRM-AGSAIVPtgtlLGPPE------IAIAASVGATKVKVKKLPSVVIITSGdelvpVEATPLPHQIRSSNVhcIATL 208
Cdd:cd03522 119 EAGQMvATVKIIP----LAVPEalveraEALARDGPLLRVAPFRPLRVGLIVTG-----SEVYGGRIEDKFGPV--LRAR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509195002 209 LKPYQIEVDF-IHIPDDLATTQEAIQQALQQYDVLILC-GGVSQGKKDFIPKALQAEGVQKYFHKLSQQPGKPFWFGRKD 286
Cdd:cd03522 188 LAALGVELVEqVIVPHDEAAIAAAIAEALEAGAELLILtGGASVDPDDVTPAAIRAAGGEVIRYGMPVDPGNLLLLGYLG 267
|
170
....*....|....*....
gi 1509195002 287 RNVVFALPGnpvssflCAR 305
Cdd:cd03522 268 GVPVIGLPG-------CAR 279
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
178-247 |
1.02e-05 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 46.65 E-value: 1.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1509195002 178 IITSGDELvpveatpLPHQIRSSNVHCIATLLKPYQIEVDFIH-IPDDLATTQEAIQQALQQYDVLILCGG 247
Cdd:COG1058 4 IITIGDEL-------LSGRIVDTNAAWLARELAELGIDVYRITtVGDDPERIVEALREALARADLVITTGG 67
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
326-394 |
6.31e-05 |
|
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: 40.67 E-value: 6.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1509195002 326 AALSADYVYTSPLTYFLQVQLYQENATLMARPVMGHGSGDFANLVENQGFLELPKEQTEFKKGDIFPLW 394
Cdd:pfam03454 2 ARLARDLKSDPGRREFVRVRLHEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVI 70
|
|
| |
