|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
1-614 |
0e+00 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 668.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 1 MQRKIYLKKLDVSDALEKYKAELQQRGFffdESEIIQTRKSARRVLAEAVYAKRNVPAYNSAAMDGIAVRSVDTAGASKV 80
Cdd:PRK14498 1 MKRKIFLTLVSLEEAREILESLLSELPL---GTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 81 RPKILQKN----------------QFEFINTGNPMKIPFDSVIMIENVHVIDEDHVQIFESIPPFHNVRLIGEDVCEQDM 144
Cdd:PRK14498 78 NPVRLKLGgevhageapdvevepgEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 145 IFTRYHRLRPYDVALLLAAGVFEVKVLKKMKAIVIPTGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPD 224
Cdd:PRK14498 158 ILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 225 SLDLISETILKAVESYDLIFLNAGSSAGSFDYSYHALEQLGKVVVHGLNVRPGKPTILGIIRNKPVICLPGYPGSCYVIL 304
Cdd:PRK14498 238 DEEELEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 305 ENIVKPLINEKYRIITEKNLFLEASSLRRVVSSISEDEFIRVSLAKIKDRYVFVPLKRGAASMDALSKMSGTVVVQKGVE 384
Cdd:PRK14498 318 EEFVAPLLRKLAGLPPPERATVKARLARRVRSELGREEFVPVSLGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 385 LLDEGDKVTVGLNRSLEEiDKNILFVGSHDPLISIIADLLKQKDFSLnmSIVNAGSMGAVAAVAKNCAHIGGIHLFDPVS 464
Cdd:PRK14498 398 GLEAGEEVEVELFGPLVE-PPTLVIIGSHDPGLDLLLDLLARRGLRL--RSLHVGSMGGLMALKRGEADIAGIHLLDPET 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 465 GEYNVPYLKRYLP--QYILMKFVKRNQGLIVQKGNPKKIENLFDLTRKDIRFVNRQRAAGTRILLDYHLSKLGIDPSQIN 542
Cdd:PRK14498 475 GEYNIPYIKKYLLgeDAVLVKGYRREQGLVVRKGNPKGIEGIEDLVRKDVRFVNRQRGSGTRILLDYHLKELAIDPERIN 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157314953 543 GYEDEEFTHINLALKIKKGMADVGLGIAFAAKIMDLDFIPLIWEDYDLLVLEEFFNDDRFQIIMDLILSKNF 614
Cdd:PRK14498 555 GYDREEKTHMAVAAAVAQGRADAGLGIRAAAKALGLDFIPLAEEEYDLLIPKERLEKPAVRAFLEALKSPEF 626
|
|
| YvgK |
COG1910 |
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism]; |
310-633 |
8.49e-123 |
|
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
Pssm-ID: 441514 [Multi-domain] Cd Length: 328 Bit Score: 367.02 E-value: 8.49e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 310 PLINEKYRIITEKNLFLEASSLRRVVSSISEDEFIRVSLAKIKDRYVFVPLKRGAASMDALSKMSGTVVVQKGVELLDEG 389
Cdd:COG1910 1 PLLYKLLGLLAPLREKVEAALSRKLVSSLGVLEFLRVKLGLVGGLRVAEPLVRGAGVITSLVAADGLLKIPEPSEGLEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 390 DKVTVGLNRSLEEIDkNILFVGSHDPLISIIADLLKQKDFSLNMSIVNAGSMGAVAAVAKNCAHIGGIHLFDPVSGEYNV 469
Cdd:COG1910 81 LEVEVELLRPELPLL-TLVIIGSHDPLLDILLRLLEKRESGAGLASSYVGSLGGLEALARGEADIAGIHLLDEETGEYNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 470 PYLKRYLP--QYILMKFVKRNQGLIVQKGNPKKIENLFDLTRKDIRFVNRQRAAGTRILLDYHLSKLGIDPSQINGYEDE 547
Cdd:COG1910 160 PYVRRYLPgrPAVLINLARREQGLIVAKGNPKGIKGLEDLARPDLRFVNRQKGSGTRVLLDELLRRLGIDPEDINGYERE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 548 EFTHINLALKIKKGMADVGLGIAFAAKIMDLDFIPLIWEDYDLLVLEEFFNDDRFQIIMDLILSKNFCNSDLIYQGYDLS 627
Cdd:COG1910 240 EYTHLAVAAAVASGEADVGLGIEAAARAFGLDFIPLAEERYDLVIPREALFDPPVQALLEILRSPEFRERAAALGGYDLS 319
|
....*.
gi 157314953 628 SVGKII 633
Cdd:COG1910 320 DTGKVI 325
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
32-394 |
4.71e-105 |
|
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: 324.06 E-value: 4.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 32 ESEIIQTRKSARRVLAEAVYAKRNVPAYNSAAMDGIAVRSVDTAGASK------------VRPKILQKNQFEFINTGNPM 99
Cdd:cd00887 16 GTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrvvgeipagePPDGPLGPGEAVRIMTGAPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 100 KIPFDSVIMIENVHvIDEDHVQIFESIPPFHNVRLIGEDVCEQDMIFTRYHRLRPYDVALLLAAGVFEVKVLKKMKAIVI 179
Cdd:cd00887 96 PEGADAVVMVEDTE-EEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAII 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 180 PTGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAVESYDLIFLNAGSSAGSFDYSYH 259
Cdd:cd00887 175 STGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 260 ALEQL-GKVVVHGLNVRPGKPTILGIIRNKPVICLPGYPGSCYVILENIVKPLINEKYRIITEKNLFLEASSLRRVVSSI 338
Cdd:cd00887 255 VLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLAEDLKSKP 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 157314953 339 SEDEFIRVSLAKIKDRYVFVPL-KRGAASMDALSKMSGTVVVQKGVELLDEGDKVTV 394
Cdd:cd00887 335 GRREFLRVRLERDEGGLVVAPPgGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEV 391
|
|
| PBP_like |
pfam12727 |
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ... |
421-609 |
4.56e-83 |
|
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain.
Pssm-ID: 463683 [Multi-domain] Cd Length: 192 Bit Score: 259.43 E-value: 4.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 421 ADLLKQKDFSLNMSIVNAGSMGAVAAVAKNCAHIGGIHLFDPVSGEYNVPYLKRYLP--QYILMKFVKRNQGLIVQKGNP 498
Cdd:pfam12727 1 AEELARKHPGVRLAVAYVGSLGGLAALRRGEAHIAGIHLLDPETGEYNLPFLRRLLPgiPVVLINLAYREQGLVVAPGNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 499 KKIENLFDLTRKDIRFVNRQRAAGTRILLDYHLSKLGIDPSQINGYEDEEFTHINLALKIKKGMADVGLGIAFAAK-IMD 577
Cdd:pfam12727 81 KGITGWEDLARPGLRFVNRQRGSGTRVLLDELLRKAGIDPSDINGYDREERSHLAVAAAVASGRADAGLGIEAAARaLGG 160
|
170 180 190
....*....|....*....|....*....|..
gi 157314953 578 LDFIPLIWEDYDLLVLEEFFNDDRFQIIMDLI 609
Cdd:pfam12727 161 LDFIPLARERYDLVIPKEALDDPAVQALLEVL 192
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
174-310 |
4.15e-29 |
|
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: 112.80 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 174 MKAIVIPTGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAVESYDLIFLNAGSSAGS 253
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157314953 254 FDYSYHALEQLGKVVVHGL-----------NVRPGKPTILGIIRNKPVICLPGYPGSCYVILENIVKP 310
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFgefrmlsslpvLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-307 |
6.25e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 103.44 E-value: 6.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 178 VIPTGGEVVQPedeidvGAIPETNSVMIKAYLEEL--DVDVNVNDVVPDSLDLISETILKAVESYDLIFLNAGSSAGSFD 255
Cdd:smart00852 2 IISTGDELLSG------GQIRDSNGPMLAALLRELgiEVVRVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPDD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157314953 256 YSYHALEQLG--KVVVHGLNVRPGKPTIL---------GIIRNKPVICLPGYPGSCYVILENI 307
Cdd:smart00852 76 LTPEALAELGgrELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
1-614 |
0e+00 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 668.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 1 MQRKIYLKKLDVSDALEKYKAELQQRGFffdESEIIQTRKSARRVLAEAVYAKRNVPAYNSAAMDGIAVRSVDTAGASKV 80
Cdd:PRK14498 1 MKRKIFLTLVSLEEAREILESLLSELPL---GTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 81 RPKILQKN----------------QFEFINTGNPMKIPFDSVIMIENVHVIDEDHVQIFESIPPFHNVRLIGEDVCEQDM 144
Cdd:PRK14498 78 NPVRLKLGgevhageapdvevepgEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 145 IFTRYHRLRPYDVALLLAAGVFEVKVLKKMKAIVIPTGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPD 224
Cdd:PRK14498 158 ILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 225 SLDLISETILKAVESYDLIFLNAGSSAGSFDYSYHALEQLGKVVVHGLNVRPGKPTILGIIRNKPVICLPGYPGSCYVIL 304
Cdd:PRK14498 238 DEEELEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 305 ENIVKPLINEKYRIITEKNLFLEASSLRRVVSSISEDEFIRVSLAKIKDRYVFVPLKRGAASMDALSKMSGTVVVQKGVE 384
Cdd:PRK14498 318 EEFVAPLLRKLAGLPPPERATVKARLARRVRSELGREEFVPVSLGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 385 LLDEGDKVTVGLNRSLEEiDKNILFVGSHDPLISIIADLLKQKDFSLnmSIVNAGSMGAVAAVAKNCAHIGGIHLFDPVS 464
Cdd:PRK14498 398 GLEAGEEVEVELFGPLVE-PPTLVIIGSHDPGLDLLLDLLARRGLRL--RSLHVGSMGGLMALKRGEADIAGIHLLDPET 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 465 GEYNVPYLKRYLP--QYILMKFVKRNQGLIVQKGNPKKIENLFDLTRKDIRFVNRQRAAGTRILLDYHLSKLGIDPSQIN 542
Cdd:PRK14498 475 GEYNIPYIKKYLLgeDAVLVKGYRREQGLVVRKGNPKGIEGIEDLVRKDVRFVNRQRGSGTRILLDYHLKELAIDPERIN 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157314953 543 GYEDEEFTHINLALKIKKGMADVGLGIAFAAKIMDLDFIPLIWEDYDLLVLEEFFNDDRFQIIMDLILSKNF 614
Cdd:PRK14498 555 GYDREEKTHMAVAAAVAQGRADAGLGIRAAAKALGLDFIPLAEEEYDLLIPKERLEKPAVRAFLEALKSPEF 626
|
|
| YvgK |
COG1910 |
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism]; |
310-633 |
8.49e-123 |
|
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
Pssm-ID: 441514 [Multi-domain] Cd Length: 328 Bit Score: 367.02 E-value: 8.49e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 310 PLINEKYRIITEKNLFLEASSLRRVVSSISEDEFIRVSLAKIKDRYVFVPLKRGAASMDALSKMSGTVVVQKGVELLDEG 389
Cdd:COG1910 1 PLLYKLLGLLAPLREKVEAALSRKLVSSLGVLEFLRVKLGLVGGLRVAEPLVRGAGVITSLVAADGLLKIPEPSEGLEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 390 DKVTVGLNRSLEEIDkNILFVGSHDPLISIIADLLKQKDFSLNMSIVNAGSMGAVAAVAKNCAHIGGIHLFDPVSGEYNV 469
Cdd:COG1910 81 LEVEVELLRPELPLL-TLVIIGSHDPLLDILLRLLEKRESGAGLASSYVGSLGGLEALARGEADIAGIHLLDEETGEYNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 470 PYLKRYLP--QYILMKFVKRNQGLIVQKGNPKKIENLFDLTRKDIRFVNRQRAAGTRILLDYHLSKLGIDPSQINGYEDE 547
Cdd:COG1910 160 PYVRRYLPgrPAVLINLARREQGLIVAKGNPKGIKGLEDLARPDLRFVNRQKGSGTRVLLDELLRRLGIDPEDINGYERE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 548 EFTHINLALKIKKGMADVGLGIAFAAKIMDLDFIPLIWEDYDLLVLEEFFNDDRFQIIMDLILSKNFCNSDLIYQGYDLS 627
Cdd:COG1910 240 EYTHLAVAAAVASGEADVGLGIEAAARAFGLDFIPLAEERYDLVIPREALFDPPVQALLEILRSPEFRERAAALGGYDLS 319
|
....*.
gi 157314953 628 SVGKII 633
Cdd:COG1910 320 DTGKVI 325
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
32-394 |
4.71e-105 |
|
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: 324.06 E-value: 4.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 32 ESEIIQTRKSARRVLAEAVYAKRNVPAYNSAAMDGIAVRSVDTAGASK------------VRPKILQKNQFEFINTGNPM 99
Cdd:cd00887 16 GTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrvvgeipagePPDGPLGPGEAVRIMTGAPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 100 KIPFDSVIMIENVHvIDEDHVQIFESIPPFHNVRLIGEDVCEQDMIFTRYHRLRPYDVALLLAAGVFEVKVLKKMKAIVI 179
Cdd:cd00887 96 PEGADAVVMVEDTE-EEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAII 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 180 PTGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAVESYDLIFLNAGSSAGSFDYSYH 259
Cdd:cd00887 175 STGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 260 ALEQL-GKVVVHGLNVRPGKPTILGIIRNKPVICLPGYPGSCYVILENIVKPLINEKYRIITEKNLFLEASSLRRVVSSI 338
Cdd:cd00887 255 VLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLAEDLKSKP 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 157314953 339 SEDEFIRVSLAKIKDRYVFVPL-KRGAASMDALSKMSGTVVVQKGVELLDEGDKVTV 394
Cdd:cd00887 335 GRREFLRVRLERDEGGLVVAPPgGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEV 391
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
10-394 |
1.56e-92 |
|
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: 291.61 E-value: 1.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 10 LDVSDALEKYKAELQQRGfffdeSEIIQTRKSARRVLAEAVYAKRNVPAYNSAAMDGIAVRSVDTAGASKVR-------- 81
Cdd:COG0303 2 ISVEEALALILAAVRPLG-----TETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTlrvvgeia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 82 -----PKILQKNQFEFINTGNPMKIPFDSVIMIENVHViDEDHVQIFESIPPFHNVRLIGEDVCEQDMIFTRYHRLRPYD 156
Cdd:COG0303 77 agsppPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER-EGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 157 VALLLAAGVFEVKVLKKMKAIVIPTGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKA 236
Cdd:COG0303 156 LGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 237 VESYDLIFLNAGSSAGSFDYSYHALEQLG-KVVVHGLNVRPGKPTILGIIRNKPVICLPGYPGSCYVILENIVKPLINEK 315
Cdd:COG0303 236 LAEADLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 316 YRIITEKNLFLEASSLRRVVSSISEDEFIRVSLAKIKDRYVFVPLKRGAASMdaLSKMSGT---VVVQKGVELLDEGDKV 392
Cdd:COG0303 316 AGLPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQGSGL--LSSLAEAdglIVLPEGVEGVEAGEEV 393
|
..
gi 157314953 393 TV 394
Cdd:COG0303 394 EV 395
|
|
| PBP_like |
pfam12727 |
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ... |
421-609 |
4.56e-83 |
|
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain.
Pssm-ID: 463683 [Multi-domain] Cd Length: 192 Bit Score: 259.43 E-value: 4.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 421 ADLLKQKDFSLNMSIVNAGSMGAVAAVAKNCAHIGGIHLFDPVSGEYNVPYLKRYLP--QYILMKFVKRNQGLIVQKGNP 498
Cdd:pfam12727 1 AEELARKHPGVRLAVAYVGSLGGLAALRRGEAHIAGIHLLDPETGEYNLPFLRRLLPgiPVVLINLAYREQGLVVAPGNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 499 KKIENLFDLTRKDIRFVNRQRAAGTRILLDYHLSKLGIDPSQINGYEDEEFTHINLALKIKKGMADVGLGIAFAAK-IMD 577
Cdd:pfam12727 81 KGITGWEDLARPGLRFVNRQRGSGTRVLLDELLRKAGIDPSDINGYDREERSHLAVAAAVASGRADAGLGIEAAARaLGG 160
|
170 180 190
....*....|....*....|....*....|..
gi 157314953 578 LDFIPLIWEDYDLLVLEEFFNDDRFQIIMDLI 609
Cdd:pfam12727 161 LDFIPLARERYDLVIPKEALDDPAVQALLEVL 192
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
14-417 |
4.89e-58 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 204.66 E-value: 4.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 14 DALEKYKAELQqrgfFFDESEIIQTRKSARRVLAEAVYAKRNVPAYNSAAMDGIAVRSVDTAGASKVRPKIlQKNQFEFI 93
Cdd:PRK14497 15 EAIKVFLSSLN----FKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKI-GIGEFKEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 94 ----------NTGNPMKIPFDSVIMIENVHVIDEDHVQIFESIPPFHNVRLIGEDVCEQDMIFTRYHRLRPYDVALLLAA 163
Cdd:PRK14497 90 hikeceavevDTGSMIPMGADAVIKVENTKVINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 164 GVFEVKVLKKMKAIVIPTGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAVESYDLI 243
Cdd:PRK14497 170 GISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 244 FLNAGSSAGSFDYSYHALEQLGKVVVHGLNVRPGKPTILGIIRNKPVICLPGYPGSCYVILENIVKPLINEKYRIITEKN 323
Cdd:PRK14497 250 ILTGGTSAGEKDFVHQAIRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSRKEIL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 324 LF--LEASSLRRVVSSISEDEFIRVSLAKIKDRYVFVPLKRGAASMDALSKMSGTVVVQKGVElLDEGDKVTVGLNRsle 401
Cdd:PRK14497 330 GLgkIKARLALRVKADEHRNTLIPVYLFKSDNSYYALPVPFDSYMVGTFSLTDGYIMLGPNEE-IEEGKEVEVDLKK--- 405
|
410
....*....|....*.
gi 157314953 402 eIDKNILFVGSHDPLI 417
Cdd:PRK14497 406 -LDDRPSIIGEEDKRI 420
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
8-394 |
3.71e-42 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 161.32 E-value: 3.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 8 KKLDVSDALEKYKAELQQrgffFDESEIIQTRKSARRVLAEAVYAKRNVPAYNSAAMDGIAVRSVD------------TA 75
Cdd:PRK14491 197 AFLSVSQGLDKILSLVTP----VTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDlepesytlvgevLA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 76 GASkvRPKILQKNQFEFINTGNPMKIPFDSVIMIENVHViDEDHVQIFESIPPFHNVRLIGEDVCEQDMIFTRYHRLRPY 155
Cdd:PRK14491 273 GHQ--YDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQ-DGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAP 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 156 DVALLLAAGVFEVKVLKKMKAIVIPTGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILK 235
Cdd:PRK14491 350 EQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQ 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 236 AVESYDLIFLNAGSSAGSFDYSYHALEQLGKVVVHGLNVRPGKPTILGIIRNKPVICLPGYPGSCYVILENIVKPLINEK 315
Cdd:PRK14491 430 AAAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 316 YRIITEKNLFLEASSLRRVVSSISEDEFIR--VSLAKIKDRYVFVPLKRGAASMDALSKMSGTVVVQKGVELLDEGDKVT 393
Cdd:PRK14491 510 AGEQNWQPLLFPAIADETLRSRQGRTEFSRgiYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGETVT 589
|
.
gi 157314953 394 V 394
Cdd:PRK14491 590 I 590
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
44-164 |
1.00e-36 |
|
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: 134.23 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 44 RVLAEAVYAKRNVPAYNSAAMDGIAVRSVDTAGASKVRP--------KILQKNQFEFINTGNPMKIPFDSVIMIENVHVI 115
Cdd:pfam03453 19 RVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPiaageppgPLLPGGEAVRIMTGAPLPEGADAVVMVEDTEEG 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 157314953 116 DEDHVQIFESIPPFHNVRLIGEDVCEQDMIFTRYHRLRPYDVALLLAAG 164
Cdd:pfam03453 99 GGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
32-312 |
4.64e-30 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 122.89 E-value: 4.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 32 ESEIIQTRKSARRVLAEAVYAKRNVPAYNSAAMDGIAVRSVDTAG--ASKVRPKILQKNQFE---------FINTGNPMK 100
Cdd:PRK10680 26 ATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASgqPLPVAGKAFAGQPFHgewpagtciRIMTGAPVP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 101 IPFDSVIMIENVHViDEDHVQIFESIPPFHNVRLIGEDVCEQDMIFTRYHRLRPYDVALLLAAGVFEVKVLKKMKAIVIP 180
Cdd:PRK10680 106 EGCEAVVMQEQTEQ-TDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALFS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 181 TGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAVESYDLIFLNAGSSAGSFDYSYHA 260
Cdd:PRK10680 185 TGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKTI 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 157314953 261 LEQLGKVVVHGLNVRPGKPTILGIIRNKPVICLPGYPGSCYVILENIVKPLI 312
Cdd:PRK10680 265 LEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLL 316
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
174-310 |
4.15e-29 |
|
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: 112.80 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 174 MKAIVIPTGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAVESYDLIFLNAGSSAGS 253
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157314953 254 FDYSYHALEQLGKVVVHGL-----------NVRPGKPTILGIIRNKPVICLPGYPGSCYVILENIVKP 310
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFgefrmlsslpvLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-307 |
6.25e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 103.44 E-value: 6.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 178 VIPTGGEVVQPedeidvGAIPETNSVMIKAYLEEL--DVDVNVNDVVPDSLDLISETILKAVESYDLIFLNAGSSAGSFD 255
Cdd:smart00852 2 IISTGDELLSG------GQIRDSNGPMLAALLRELgiEVVRVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPDD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157314953 256 YSYHALEQLG--KVVVHGLNVRPGKPTIL---------GIIRNKPVICLPGYPGSCYVILENI 307
Cdd:smart00852 76 LTPEALAELGgrELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
44-302 |
2.04e-25 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 109.24 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 44 RVLAEAVYAKRNVPAYNSAAMDGIAVRSVDTAGAsKVRPKI-------------LQKNQFEFINTGNPMKIPFDSVIMIE 110
Cdd:PRK14690 53 HVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGA-QVLPLIegraaagvpfsgrVPEGMALRILTGAALPEGVDTVVLEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 111 NVhVIDEDHVQIFESIPPFHNVRLIGEDVCEQDMIFTRYHRLRPYDVALLLAAGVFEVKVLKKMKAIVIPTGGEVVQPED 190
Cdd:PRK14690 132 DV-AGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 191 EIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAVESYDLIFLNAGSSAGSFDYSYHALEQLGKVVVH 270
Cdd:PRK14690 211 LAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHVSALLREAGAMQSW 290
|
250 260 270
....*....|....*....|....*....|..
gi 157314953 271 GLNVRPGKPTILGIIRNKPVICLPGYPGSCYV 302
Cdd:PRK14690 291 RIALKPGRPLALGLWQGVPVFGLPGNPVAALV 322
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-312 |
5.16e-24 |
|
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: 98.09 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 178 VIPTGgevvqpeDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAVESYDLIFLNAGSSAGSFDYS 257
Cdd:pfam00994 2 IITTG-------DELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVT 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157314953 258 YHALEQLG-------KVVVHGLNVRPGKPTILGII-----RNKPVICLPGYPGSCYVILENIVKPLI 312
Cdd:pfam00994 75 PEALAELGgrelpgfEELFRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLL 141
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
44-312 |
2.63e-21 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 98.35 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 44 RVLAEAVYAKRNVPAYNSAAMDGIAVRSVDTAGASKVRPK----------ILQKNQFEFINTGNPMKIPFDSVIMIENVH 113
Cdd:PLN02699 37 KVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITEsragndglgvTLTPGTVAYVTTGGPIPDGADAVVQVEDTE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 114 VI-----DEDHVQIFESIPPFHNVRLIGEDVCEQDMIFTRYHRLRPYDVALLLAAGVFEVKVLKKMKAIVIPTGGEVVQP 188
Cdd:PLN02699 117 VVedpldGSKRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 189 EDE-IDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAVES-YDLIFLNAGSSAGSFDYSYHALEQLGK 266
Cdd:PLN02699 197 TTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAISSgVDILLTSGGVSMGDRDFVKPLLEKRGT 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 157314953 267 VVVHGLNVRPGKPTILGIIRNKP---------VICLPGYPGSCYVILENIVKPLI 312
Cdd:PLN02699 277 VYFSKVLMKPGKPLTFAEIDAKSapsnskkmlAFGLPGNPVSCLVCFNLFVVPAI 331
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
190-312 |
9.65e-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: 9.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 190 DEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAVESYDLIFLNAGSSAGSFDYSYHALEQLGKVVV 269
Cdd:cd00758 9 DELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALAELGEREA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 157314953 270 HG--LNVRPGKPTILGIIRNKPVICLPGYPGSCYVILENIVKPLI 312
Cdd:cd00758 89 HGkgVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
157-295 |
1.01e-07 |
|
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: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 157 VALLLAAGVFEVKVLKKMKAIVIPTGGEVVQPEDEIDVGAIpetnsvmIKAYLEELDVDVNVNDVVPDSLDLISETILKA 236
Cdd:cd03522 143 EALARDGPLLRVAPFRPLRVGLIVTGSEVYGGRIEDKFGPV-------LRARLAALGVELVEQVIVPHDEAAIAAAIAEA 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157314953 237 VESY-DLIFLNAGSSAGSFDYSYHALEQLGKVVVH-GLNVRPGKPTILGIIRNKPVICLPG 295
Cdd:cd03522 216 LEAGaELLILTGGASVDPDDVTPAAIRAAGGEVIRyGMPVDPGNLLLLGYLGGVPVIGLPG 276
|
|
| PBP2_PEB3_AcfC |
cd13519 |
Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a ... |
487-528 |
1.41e-03 |
|
Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a member of the type 2 periplasmic binding fold superfamily; PEB3 is a glycoprotein adhesion from Campylobacter jejuni whose structure suggests a functional role in transport, and resembles PEB1a, an Asp/Glu transporter and an adhesin. The overall structure of PEB3 is a dimer and is similar to that of other type 2 periplasmic transport proteins such as the molybdate/tungstate, sulfate, and ferric iron transporters. PEB3 has high sequence identity to Paa, an Escherichia coli adhesin, and to AcfC, an accessory colonization factor from Vibrio cholera.
Pssm-ID: 270237 [Multi-domain] Cd Length: 227 Bit Score: 40.76 E-value: 1.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 157314953 487 RNQGLIVQKGNPKKIENLFDLTRKDIRFVNRQRAAGTRILLD 528
Cdd:cd13519 80 RPSAILVRKGNPKKIKGLKDLLKPGVKILVVNGAGQTGLWED 121
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
342-394 |
1.83e-03 |
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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: 37.21 E-value: 1.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 157314953 342 EFIRVSLAKIKDRYVFVPL-KRGAASMDALSKMSGTVVVQKGVELLDEGDKVTV 394
Cdd:pfam03454 16 EFVRVRLHEEDGRYYAEPIgKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEV 69
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| PBP2_ModA_like_1 |
cd13538 |
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ... |
491-567 |
1.91e-03 |
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Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270256 [Multi-domain] Cd Length: 230 Bit Score: 40.36 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 491 LIVQKGNPKKIENLFDLTRKDIRFVNRQRA--AG--TRILLDyhlsKLGIDPSqiNGYED--------EEFTHINLALKI 558
Cdd:cd13538 84 VIVPKDNPAKITSLADLAKPGVKIVIGAPEvpVGtyTRRVLD----KAGNDYA--YGYKEavlanvvsEETNVRDVVTKV 157
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....*....
gi 157314953 559 KKGMADVGL 567
Cdd:cd13538 158 ALGEADAGF 166
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| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
180-298 |
3.32e-03 |
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bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 39.92 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157314953 180 PTGGEVVQPEDEIDVGAIPETNSVMIKAYLEELDVDVNVNDVVPDSLDLISETILKAV-ESYDLIFLNAGSSAGSFDYSY 258
Cdd:PRK03604 155 RTSAAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIaEGYALIITTGGTGLGPRDVTP 234
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 157314953 259 HALEQLGKVVVHGL-----NVRPGK-PT------ILGIIRNKPVICLPGYPG 298
Cdd:PRK03604 235 EALAPLLERRLPGIaealrSWGQGRtPTamlsrlVAGMIGNSLVVALPGSPG 286
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| PBP2_ModA3_like |
cd13517 |
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 ... |
491-515 |
8.72e-03 |
|
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 periplasmic binding fold superfamily; This subfamily contains molybdate binding protein-like (ModA3) domain of an ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. ModA transporters import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arrangted around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270235 [Multi-domain] Cd Length: 223 Bit Score: 38.36 E-value: 8.72e-03
10 20
....*....|....*....|....*
gi 157314953 491 LIVQKGNPKKIENLFDLTRKDIRFV 515
Cdd:cd13517 82 IAVPKGNPKNITSLEDLAKPGVKVA 106
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