MULTISPECIES: betaine/proline/choline family ABC transporter ATP-binding protein [Sporosarcina]
Protein Classification
OpuBA and CBS_pair domain-containing protein( domain architecture ID 11438323)
OpuBA and CBS_pair domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| OpuBA | COG1125 | ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-306 | 0e+00 | |||||
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism]; : Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 553.16 E-value: 0e+00
|
|||||||||
| COG3448 | COG3448 | CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
249-369 | 4.78e-26 | |||||
CBS-domain-containing membrane protein [Signal transduction mechanisms]; : Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 101.48 E-value: 4.78e-26
|
|||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| OpuBA | COG1125 | ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-306 | 0e+00 | ||||||
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 553.16 E-value: 0e+00
|
||||||||||
| ABC_OpuCA_Osmoprotection | cd03295 | ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-243 | 7.05e-150 | ||||||
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 422.86 E-value: 7.05e-150
|
||||||||||
| proV | TIGR01186 | glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
13-365 | 1.25e-122 | ||||||
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines] Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 358.40 E-value: 1.25e-122
|
||||||||||
| PRK10851 | PRK10851 | sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-238 | 2.89e-75 | ||||||
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 236.90 E-value: 2.89e-75
|
||||||||||
| tungstate_WtpC | NF040840 | tungstate ABC transporter ATP-binding protein WtpC; |
1-244 | 1.02e-71 | ||||||
tungstate ABC transporter ATP-binding protein WtpC; Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 227.65 E-value: 1.02e-71
|
||||||||||
| ABC_tran | pfam00005 | ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 | 4.75e-51 | ||||||
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains. Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 167.44 E-value: 4.75e-51
|
||||||||||
| ABC_ATP_DarD | NF038007 | darobactin export ABC transporter ATP-binding protein; |
1-215 | 7.73e-48 | ||||||
darobactin export ABC transporter ATP-binding protein; Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 161.42 E-value: 7.73e-48
|
||||||||||
| ABC_ATP_SaoA | NF040729 | ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
2-217 | 1.16e-47 | ||||||
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs. Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 162.22 E-value: 1.16e-47
|
||||||||||
| AztA | NF040873 | zinc ABC transporter ATP-binding protein AztA; |
13-201 | 3.61e-32 | ||||||
zinc ABC transporter ATP-binding protein AztA; Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 119.65 E-value: 3.61e-32
|
||||||||||
| ABC2_perm_RbbA | NF033858 | ribosome-associated ATPase/putative transporter RbbA; |
5-238 | 3.61e-31 | ||||||
ribosome-associated ATPase/putative transporter RbbA; Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 125.24 E-value: 3.61e-31
|
||||||||||
| COG3448 | COG3448 | CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
249-369 | 4.78e-26 | ||||||
CBS-domain-containing membrane protein [Signal transduction mechanisms]; Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 101.48 E-value: 4.78e-26
|
||||||||||
| ABC2_perm_RbbA | NF033858 | ribosome-associated ATPase/putative transporter RbbA; |
5-225 | 3.46e-21 | ||||||
ribosome-associated ATPase/putative transporter RbbA; Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.58 E-value: 3.46e-21
|
||||||||||
| GguA | NF040905 | sugar ABC transporter ATP-binding protein; |
1-214 | 2.61e-18 | ||||||
sugar ABC transporter ATP-binding protein; Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.00 E-value: 2.61e-18
|
||||||||||
| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
256-362 | 5.89e-17 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 76.13 E-value: 5.89e-17
|
||||||||||
| 40850658_otr | NF000106 | oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-231 | 5.24e-15 | ||||||
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.54 E-value: 5.24e-15
|
||||||||||
| AAA | smart00382 | ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-209 | 4.21e-12 | ||||||
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment. Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.55 E-value: 4.21e-12
|
||||||||||
| CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
311-367 | 1.52e-07 | ||||||
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP. Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 47.59 E-value: 1.52e-07
|
||||||||||
| GguA | NF040905 | sugar ABC transporter ATP-binding protein; |
16-226 | 1.11e-06 | ||||||
sugar ABC transporter ATP-binding protein; Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 1.11e-06
|
||||||||||
| PTZ00314 | PTZ00314 | inosine-5'-monophosphate dehydrogenase; Provisional |
260-364 | 2.86e-06 | ||||||
inosine-5'-monophosphate dehydrogenase; Provisional Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 49.20 E-value: 2.86e-06
|
||||||||||
| mgtE | TIGR00400 | Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ... |
260-371 | 1.99e-04 | ||||||
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ transporter first described in Bacillus firmus. May form a homodimer. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 129495 [Multi-domain] Cd Length: 449 Bit Score: 43.27 E-value: 1.99e-04
|
||||||||||
| CBS | smart00116 | Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
322-364 | 2.77e-04 | ||||||
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease. Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 38.26 E-value: 2.77e-04
|
||||||||||
| CBS_CbpB | NF041630 | cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS ... |
285-367 | 5.89e-04 | ||||||
cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS (cystathionine beta synthase) domains (see PF00571). When levels of c-di-AMP are low, CbpB activates RelA, a bifunctional (p)ppGpp synthetase/hydrolase. Pssm-ID: 469514 [Multi-domain] Cd Length: 143 Bit Score: 39.74 E-value: 5.89e-04
|
||||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| OpuBA | COG1125 | ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-306 | 0e+00 | ||||||
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 553.16 E-value: 0e+00
|
||||||||||
| ABC_OpuCA_Osmoprotection | cd03295 | ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-243 | 7.05e-150 | ||||||
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 422.86 E-value: 7.05e-150
|
||||||||||
| ProV | COG4175 | ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-366 | 5.69e-131 | ||||||
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 380.60 E-value: 5.69e-131
|
||||||||||
| proV | TIGR01186 | glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
13-365 | 1.25e-122 | ||||||
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines] Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 358.40 E-value: 1.25e-122
|
||||||||||
| PotA | COG3842 | ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-243 | 1.80e-112 | ||||||
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 332.06 E-value: 1.80e-112
|
||||||||||
| MalK | COG3839 | ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-238 | 4.23e-103 | ||||||
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 308.16 E-value: 4.23e-103
|
||||||||||
| ABC_Pro_Gly_Betaine | cd03294 | ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-237 | 2.23e-100 | ||||||
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 298.02 E-value: 2.23e-100
|
||||||||||
| TauB | COG1116 | ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 | 9.23e-98 | ||||||
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 291.22 E-value: 9.23e-98
|
||||||||||
| CysA | COG1118 | ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-238 | 3.19e-97 | ||||||
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 292.82 E-value: 3.19e-97
|
||||||||||
| ABC_Carb_Solutes_like | cd03259 | ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-217 | 2.87e-96 | ||||||
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 285.57 E-value: 2.87e-96
|
||||||||||
| ABC_NrtD_SsuB_transporters | cd03293 | ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-210 | 8.60e-94 | ||||||
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 279.36 E-value: 8.60e-94
|
||||||||||
| ABC_PotA_N | cd03300 | ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-238 | 2.79e-88 | ||||||
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 266.02 E-value: 2.79e-88
|
||||||||||
| GsiA | COG1123 | ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 | 1.20e-86 | ||||||
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 271.39 E-value: 1.20e-86
|
||||||||||
| ABC_CysA_sulfate_importer | cd03296 | ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-238 | 3.06e-83 | ||||||
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 253.42 E-value: 3.06e-83
|
||||||||||
| 3a0106s01 | TIGR00968 | sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
5-238 | 5.82e-83 | ||||||
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 252.80 E-value: 5.82e-83
|
||||||||||
| CcmA | COG1131 | ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-227 | 3.39e-82 | ||||||
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 250.37 E-value: 3.39e-82
|
||||||||||
| GlnQ | COG1126 | ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-239 | 3.45e-82 | ||||||
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 250.68 E-value: 3.45e-82
|
||||||||||
| LolD | COG1136 | ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 | 1.14e-81 | ||||||
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 248.80 E-value: 1.14e-81
|
||||||||||
| PhnT2 | TIGR03265 | putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-299 | 1.80e-81 | ||||||
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines] Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 253.04 E-value: 1.80e-81
|
||||||||||
| ABC_MJ0796_LolCDE_FtsE | cd03255 | ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 | 7.49e-80 | ||||||
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane. Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 243.94 E-value: 7.49e-80
|
||||||||||
| AbcC | COG1135 | ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-238 | 2.90e-79 | ||||||
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 246.53 E-value: 2.90e-79
|
||||||||||
| ABC_MalK_N | cd03301 | The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-219 | 3.08e-79 | ||||||
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed. Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 242.16 E-value: 3.08e-79
|
||||||||||
| EcfA2 | COG1122 | Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-228 | 9.43e-79 | ||||||
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only]; Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 241.47 E-value: 9.43e-79
|
||||||||||
| FtsE | COG2884 | Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-215 | 9.66e-77 | ||||||
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 236.10 E-value: 9.66e-77
|
||||||||||
| MlaF | COG1127 | ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-237 | 2.61e-76 | ||||||
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 235.64 E-value: 2.61e-76
|
||||||||||
| PRK10851 | PRK10851 | sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-238 | 2.89e-75 | ||||||
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 236.90 E-value: 2.89e-75
|
||||||||||
| ABC_Class3 | cd03229 | ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-214 | 1.33e-74 | ||||||
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 229.00 E-value: 1.33e-74
|
||||||||||
| ABC_MetN_methionine_transporter | cd03258 | ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-228 | 2.06e-74 | ||||||
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 230.55 E-value: 2.06e-74
|
||||||||||
| ABC_NikE_OppD_transporters | cd03257 | ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 | 2.70e-73 | ||||||
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF. Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 227.39 E-value: 2.70e-73
|
||||||||||
| potA | PRK09452 | spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-238 | 1.34e-72 | ||||||
spermidine/putrescine ABC transporter ATP-binding protein PotA; Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 230.60 E-value: 1.34e-72
|
||||||||||
| ABC_HisP_GlnQ | cd03262 | ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 | 1.53e-72 | ||||||
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein. Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 225.10 E-value: 1.53e-72
|
||||||||||
| tungstate_WtpC | NF040840 | tungstate ABC transporter ATP-binding protein WtpC; |
1-244 | 1.02e-71 | ||||||
tungstate ABC transporter ATP-binding protein WtpC; Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 227.65 E-value: 1.02e-71
|
||||||||||
| PhnC | COG3638 | ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-221 | 2.46e-71 | ||||||
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 223.01 E-value: 2.46e-71
|
||||||||||
| ECF_ATPase_2 | TIGR04521 | energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-225 | 1.23e-70 | ||||||
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate] Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 222.33 E-value: 1.23e-70
|
||||||||||
| potA | TIGR01187 | spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-238 | 5.49e-70 | ||||||
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines] Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 222.37 E-value: 5.49e-70
|
||||||||||
| ABC_ModC_like | cd03299 | ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-238 | 6.03e-70 | ||||||
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 219.13 E-value: 6.03e-70
|
||||||||||
| PRK10070 | PRK10070 | proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-373 | 1.18e-69 | ||||||
proline/glycine betaine ABC transporter ATP-binding protein ProV; Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 224.14 E-value: 1.18e-69
|
||||||||||
| DppF | COG1124 | ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-238 | 3.38e-69 | ||||||
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism]; Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 217.75 E-value: 3.38e-69
|
||||||||||
| ABC_PstB_phosphate_transporter | cd03260 | ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-224 | 2.05e-68 | ||||||
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD). Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 215.12 E-value: 2.05e-68
|
||||||||||
| NatA | COG4555 | ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-225 | 9.40e-68 | ||||||
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism]; Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 213.95 E-value: 9.40e-68
|
||||||||||
| metN | PRK11153 | DL-methionine transporter ATP-binding subunit; Provisional |
1-238 | 1.19e-67 | ||||||
DL-methionine transporter ATP-binding subunit; Provisional Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 216.98 E-value: 1.19e-67
|
||||||||||
| ABC_cobalt_CbiO_domain1 | cd03225 | First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 | 3.02e-67 | ||||||
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems. Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 211.56 E-value: 3.02e-67
|
||||||||||
| ABC_PhnC_transporter | cd03256 | ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-214 | 4.08e-67 | ||||||
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 212.04 E-value: 4.08e-67
|
||||||||||
| DppD | COG0444 | ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-230 | 5.64e-67 | ||||||
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism]; Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 214.53 E-value: 5.64e-67
|
||||||||||
| ABC_Org_Solvent_Resistant | cd03261 | ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-236 | 7.69e-67 | ||||||
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 211.21 E-value: 7.69e-67
|
||||||||||
| GsiA | COG1123 | ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 | 3.71e-66 | ||||||
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 217.85 E-value: 3.71e-66
|
||||||||||
| TauB | COG4525 | ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-210 | 2.01e-64 | ||||||
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 205.87 E-value: 2.01e-64
|
||||||||||
| PstB | COG1117 | ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-237 | 4.06e-64 | ||||||
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 204.89 E-value: 4.06e-64
|
||||||||||
| 3a0107s01c2 | TIGR00972 | phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-240 | 4.62e-64 | ||||||
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions] Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 204.45 E-value: 4.62e-64
|
||||||||||
| ABC_ModC_molybdenum_transporter | cd03297 | ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-217 | 3.47e-63 | ||||||
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 200.98 E-value: 3.47e-63
|
||||||||||
| FepC | COG1120 | ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-227 | 1.58e-62 | ||||||
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism]; Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 200.66 E-value: 1.58e-62
|
||||||||||
| potG | PRK11607 | putrescine ABC transporter ATP-binding subunit PotG; |
1-270 | 4.48e-62 | ||||||
putrescine ABC transporter ATP-binding subunit PotG; Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 203.53 E-value: 4.48e-62
|
||||||||||
| ABC_subfamily_A | cd03263 | ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-224 | 5.23e-62 | ||||||
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages. Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 198.11 E-value: 5.23e-62
|
||||||||||
| ugpC | PRK11650 | sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-238 | 9.76e-62 | ||||||
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 202.00 E-value: 9.76e-62
|
||||||||||
| FtsE | TIGR02673 | cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 | 1.23e-61 | ||||||
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division] Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 197.09 E-value: 1.23e-61
|
||||||||||
| glnQ | PRK09493 | glutamine ABC transporter ATP-binding protein GlnQ; |
1-240 | 1.53e-61 | ||||||
glutamine ABC transporter ATP-binding protein GlnQ; Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 197.62 E-value: 1.53e-61
|
||||||||||
| PRK11000 | PRK11000 | maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-264 | 2.19e-61 | ||||||
maltose/maltodextrin ABC transporter ATP-binding protein MalK; Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 201.41 E-value: 2.19e-61
|
||||||||||
| ABC_phnC | TIGR02315 | phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 | 2.46e-61 | ||||||
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions] Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 197.52 E-value: 2.46e-61
|
||||||||||
| ABC_DR_subfamily_A | cd03230 | ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 | 4.54e-60 | ||||||
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 191.46 E-value: 4.54e-60
|
||||||||||
| AppF | COG4608 | ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-230 | 2.09e-59 | ||||||
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 194.95 E-value: 2.09e-59
|
||||||||||
| FetA | COG4619 | ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 | 3.26e-59 | ||||||
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 190.80 E-value: 3.26e-59
|
||||||||||
| ECF_ATPase_1 | TIGR04520 | energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-225 | 4.84e-59 | ||||||
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate] Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 192.26 E-value: 4.84e-59
|
||||||||||
| YhaQ | COG4152 | ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 | 1.09e-56 | ||||||
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 187.24 E-value: 1.09e-56
|
||||||||||
| ABCC_MRP_Like | cd03228 | ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-214 | 1.47e-56 | ||||||
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 182.58 E-value: 1.47e-56
|
||||||||||
| ABC_DrrA | cd03265 | Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-224 | 1.32e-55 | ||||||
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 181.80 E-value: 1.32e-55
|
||||||||||
| ZnuC | COG1121 | ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-237 | 2.15e-55 | ||||||
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 181.83 E-value: 2.15e-55
|
||||||||||
| cbiO | PRK13637 | energy-coupling factor transporter ATPase; |
2-227 | 2.22e-55 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 183.33 E-value: 2.22e-55
|
||||||||||
| LivG | COG0411 | ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-229 | 4.62e-54 | ||||||
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism]; Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 179.08 E-value: 4.62e-54
|
||||||||||
| ThiQ | COG3840 | ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-238 | 6.46e-54 | ||||||
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 177.64 E-value: 6.46e-54
|
||||||||||
| fbpC | PRK11432 | ferric ABC transporter ATP-binding protein; |
2-244 | 9.70e-54 | ||||||
ferric ABC transporter ATP-binding protein; Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 181.07 E-value: 9.70e-54
|
||||||||||
| ArtP | COG4161 | ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-217 | 1.01e-53 | ||||||
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 177.51 E-value: 1.01e-53
|
||||||||||
| ABC_FtsE | cd03292 | Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 | 2.28e-53 | ||||||
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 175.67 E-value: 2.28e-53
|
||||||||||
| ABC_Mj1267_LivG_branched | cd03219 | ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-229 | 3.01e-53 | ||||||
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 176.09 E-value: 3.01e-53
|
||||||||||
| SunT | COG2274 | ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-225 | 3.25e-53 | ||||||
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms]; Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 187.35 E-value: 3.25e-53
|
||||||||||
| ABC_ATPase | cd00267 | ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 | 3.40e-53 | ||||||
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 173.20 E-value: 3.40e-53
|
||||||||||
| drrA | TIGR01188 | daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-227 | 7.85e-53 | ||||||
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other] Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 177.20 E-value: 7.85e-53
|
||||||||||
| ABC_Iron-Siderophores_B12_Hemin | cd03214 | ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-216 | 3.27e-52 | ||||||
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters. Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 171.46 E-value: 3.27e-52
|
||||||||||
| CydC | COG4987 | ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-230 | 3.30e-52 | ||||||
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 182.27 E-value: 3.30e-52
|
||||||||||
| ABC_drug_resistance_like | cd03264 | ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-217 | 6.35e-52 | ||||||
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 171.99 E-value: 6.35e-52
|
||||||||||
| YejF | COG4172 | ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-230 | 8.35e-52 | ||||||
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 180.27 E-value: 8.35e-52
|
||||||||||
| ModC | COG4148 | ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-229 | 3.67e-51 | ||||||
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 174.52 E-value: 3.67e-51
|
||||||||||
| ABC_putative_ATPase | cd03269 | ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-214 | 4.67e-51 | ||||||
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 169.77 E-value: 4.67e-51
|
||||||||||
| ABC_tran | pfam00005 | ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 | 4.75e-51 | ||||||
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains. Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 167.44 E-value: 4.75e-51
|
||||||||||
| CydD | COG4988 | ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 | 2.51e-50 | ||||||
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 177.26 E-value: 2.51e-50
|
||||||||||
| SapF | COG4167 | ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-230 | 4.86e-50 | ||||||
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 168.86 E-value: 4.86e-50
|
||||||||||
| artP | PRK11124 | arginine transporter ATP-binding subunit; Provisional |
11-217 | 6.01e-50 | ||||||
arginine transporter ATP-binding subunit; Provisional Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 167.88 E-value: 6.01e-50
|
||||||||||
| PRK11264 | PRK11264 | putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-239 | 7.19e-50 | ||||||
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 168.00 E-value: 7.19e-50
|
||||||||||
| MdlB | COG1132 | ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-225 | 8.96e-49 | ||||||
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 173.04 E-value: 8.96e-49
|
||||||||||
| cbiO | PRK13634 | cobalt transporter ATP-binding subunit; Provisional |
2-229 | 1.18e-48 | ||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 165.96 E-value: 1.18e-48
|
||||||||||
| ABC_Metallic_Cations | cd03235 | ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-211 | 2.48e-48 | ||||||
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates. Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 162.70 E-value: 2.48e-48
|
||||||||||
| ABC_ATP_DarD | NF038007 | darobactin export ABC transporter ATP-binding protein; |
1-215 | 7.73e-48 | ||||||
darobactin export ABC transporter ATP-binding protein; Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 161.42 E-value: 7.73e-48
|
||||||||||
| tauB | PRK11248 | taurine ABC transporter ATP-binding subunit; |
1-219 | 9.00e-48 | ||||||
taurine ABC transporter ATP-binding subunit; Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 162.56 E-value: 9.00e-48
|
||||||||||
| ABC_ATP_SaoA | NF040729 | ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
2-217 | 1.16e-47 | ||||||
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs. Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 162.22 E-value: 1.16e-47
|
||||||||||
| MglA | COG1129 | ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-215 | 1.55e-47 | ||||||
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 168.27 E-value: 1.55e-47
|
||||||||||
| YnjD | COG4136 | ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-209 | 2.45e-47 | ||||||
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only]; Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 159.95 E-value: 2.45e-47
|
||||||||||
| cbiO | PRK13632 | cobalt transporter ATP-binding subunit; Provisional |
1-242 | 3.85e-47 | ||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 161.31 E-value: 3.85e-47
|
||||||||||
| ABC_NatA_sodium_exporter | cd03266 | ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 | 7.31e-47 | ||||||
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein. Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 159.07 E-value: 7.31e-47
|
||||||||||
| YejF | COG4172 | ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-230 | 1.20e-46 | ||||||
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 166.40 E-value: 1.20e-46
|
||||||||||
| PRK14239 | PRK14239 | phosphate transporter ATP-binding protein; Provisional |
1-239 | 7.73e-46 | ||||||
phosphate transporter ATP-binding protein; Provisional Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 157.63 E-value: 7.73e-46
|
||||||||||
| L_ocin_972_ABC | TIGR03608 | putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-207 | 1.46e-45 | ||||||
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate] Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 155.08 E-value: 1.46e-45
|
||||||||||
| modC_ABC | TIGR02142 | molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
13-229 | 2.89e-45 | ||||||
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions] Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 159.12 E-value: 2.89e-45
|
||||||||||
| CcmA | COG4133 | ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-196 | 6.18e-45 | ||||||
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 153.40 E-value: 6.18e-45
|
||||||||||
| ABC_BcrA_bacitracin_resist | cd03268 | ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 | 6.91e-45 | ||||||
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein. Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 153.53 E-value: 6.91e-45
|
||||||||||
| ABC_ThiQ_thiamine_transporter | cd03298 | ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-215 | 2.79e-44 | ||||||
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 152.26 E-value: 2.79e-44
|
||||||||||
| ABC_TM1139_LivF_branched | cd03224 | ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-227 | 3.20e-44 | ||||||
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 152.20 E-value: 3.20e-44
|
||||||||||
| LolD_lipo_ex | TIGR02211 | lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-215 | 3.65e-44 | ||||||
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 152.12 E-value: 3.65e-44
|
||||||||||
| ModF | COG1119 | ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-214 | 3.71e-44 | ||||||
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism]; Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 152.93 E-value: 3.71e-44
|
||||||||||
| PRK14243 | PRK14243 | phosphate transporter ATP-binding protein; Provisional |
2-237 | 6.05e-44 | ||||||
phosphate transporter ATP-binding protein; Provisional Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 153.01 E-value: 6.05e-44
|
||||||||||
| ABCC_Glucan_exporter_like | cd03254 | ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-225 | 3.14e-43 | ||||||
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 150.07 E-value: 3.14e-43
|
||||||||||
| YbbA | COG4181 | Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 | 3.57e-43 | ||||||
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 149.89 E-value: 3.57e-43
|
||||||||||
| HisP | COG4598 | ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-241 | 5.25e-43 | ||||||
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 150.34 E-value: 5.25e-43
|
||||||||||
| ABCC_ATM1_transporter | cd03253 | ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-225 | 5.28e-43 | ||||||
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 149.69 E-value: 5.28e-43
|
||||||||||
| ABC_Carb_Monos_I | cd03216 | First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 | 5.91e-43 | ||||||
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter. Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 146.80 E-value: 5.91e-43
|
||||||||||
| ntrCD | TIGR01184 | nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-213 | 6.87e-43 | ||||||
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other] Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 149.15 E-value: 6.87e-43
|
||||||||||
| ABCC_Protease_Secretion | cd03246 | ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 | 7.64e-43 | ||||||
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA. Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 146.98 E-value: 7.64e-43
|
||||||||||
| cbiO | PRK13635 | energy-coupling factor ABC transporter ATP-binding protein; |
16-224 | 1.67e-42 | ||||||
energy-coupling factor ABC transporter ATP-binding protein; Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 149.40 E-value: 1.67e-42
|
||||||||||
| PRK14247 | PRK14247 | phosphate ABC transporter ATP-binding protein; Provisional |
9-237 | 1.98e-42 | ||||||
phosphate ABC transporter ATP-binding protein; Provisional Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 148.52 E-value: 1.98e-42
|
||||||||||
| cbiO | PRK13650 | energy-coupling factor transporter ATPase; |
18-224 | 3.03e-42 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 148.73 E-value: 3.03e-42
|
||||||||||
| LptB | COG1137 | ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-228 | 3.36e-42 | ||||||
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 147.48 E-value: 3.36e-42
|
||||||||||
| cbiO | PRK13641 | energy-coupling factor transporter ATPase; |
2-240 | 3.94e-42 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 148.82 E-value: 3.94e-42
|
||||||||||
| ABC_YhbG | cd03218 | ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-225 | 6.72e-42 | ||||||
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium. Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 146.53 E-value: 6.72e-42
|
||||||||||
| PRK13651 | PRK13651 | cobalt transporter ATP-binding subunit; Provisional |
2-216 | 1.11e-41 | ||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 148.31 E-value: 1.11e-41
|
||||||||||
| LivF | COG0410 | ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-229 | 4.60e-41 | ||||||
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism]; Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 144.35 E-value: 4.60e-41
|
||||||||||
| PRK10261 | PRK10261 | glutathione transporter ATP-binding protein; Provisional |
17-230 | 5.80e-41 | ||||||
glutathione transporter ATP-binding protein; Provisional Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 152.32 E-value: 5.80e-41
|
||||||||||
| cbiO | PRK13645 | energy-coupling factor transporter ATPase; |
15-221 | 1.12e-40 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 145.15 E-value: 1.12e-40
|
||||||||||
| ArpD | COG4618 | ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-215 | 1.34e-40 | ||||||
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 150.67 E-value: 1.34e-40
|
||||||||||
| PRK13633 | PRK13633 | energy-coupling factor transporter ATPase; |
17-227 | 5.85e-40 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 142.92 E-value: 5.85e-40
|
||||||||||
| type_I_sec_LssB | TIGR03375 | type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-216 | 1.05e-39 | ||||||
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis] Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 149.63 E-value: 1.05e-39
|
||||||||||
| NupO | COG3845 | ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-215 | 1.07e-39 | ||||||
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism]; Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 147.10 E-value: 1.07e-39
|
||||||||||
| PRK14267 | PRK14267 | phosphate ABC transporter ATP-binding protein; Provisional |
9-237 | 1.10e-39 | ||||||
phosphate ABC transporter ATP-binding protein; Provisional Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 141.52 E-value: 1.10e-39
|
||||||||||
| ABCC_bacteriocin_exporters | cd03245 | ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-215 | 1.11e-39 | ||||||
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane. Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 140.42 E-value: 1.11e-39
|
||||||||||
| ABCC_MsbA | cd03251 | ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-225 | 1.62e-39 | ||||||
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 140.44 E-value: 1.62e-39
|
||||||||||
| PRK10908 | PRK10908 | cell division ATP-binding protein FtsE; |
1-215 | 1.72e-39 | ||||||
cell division ATP-binding protein FtsE; Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 140.01 E-value: 1.72e-39
|
||||||||||
| PRK10619 | PRK10619 | histidine ABC transporter ATP-binding protein HisP; |
13-237 | 2.48e-39 | ||||||
histidine ABC transporter ATP-binding protein HisP; Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 140.49 E-value: 2.48e-39
|
||||||||||
| dppF | PRK11308 | dipeptide transporter ATP-binding subunit; Provisional |
16-230 | 2.56e-39 | ||||||
dipeptide transporter ATP-binding subunit; Provisional Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 142.41 E-value: 2.56e-39
|
||||||||||
| cbiO | PRK13647 | cobalt transporter ATP-binding subunit; Provisional |
5-227 | 6.30e-39 | ||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 139.87 E-value: 6.30e-39
|
||||||||||
| PRK15079 | PRK15079 | oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-230 | 2.53e-38 | ||||||
oligopeptide ABC transporter ATP-binding protein OppF; Provisional Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 139.84 E-value: 2.53e-38
|
||||||||||
| cbiO | TIGR01166 | cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-200 | 2.68e-38 | ||||||
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 135.63 E-value: 2.68e-38
|
||||||||||
| thiQ | PRK10771 | thiamine ABC transporter ATP-binding protein ThiQ; |
1-215 | 3.09e-38 | ||||||
thiamine ABC transporter ATP-binding protein ThiQ; Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 137.02 E-value: 3.09e-38
|
||||||||||
| thiQ | TIGR01277 | thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-218 | 9.88e-38 | ||||||
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other] Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 134.99 E-value: 9.88e-38
|
||||||||||
| cbiO | PRK13646 | energy-coupling factor transporter ATPase; |
2-224 | 1.03e-37 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 137.22 E-value: 1.03e-37
|
||||||||||
| ABC_MTABC3_MDL1_MDL2 | cd03249 | ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-225 | 1.33e-37 | ||||||
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another. Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 135.36 E-value: 1.33e-37
|
||||||||||
| cbiO | PRK13649 | energy-coupling factor transporter ATPase; |
4-235 | 1.70e-37 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 136.41 E-value: 1.70e-37
|
||||||||||
| cbiO | PRK13644 | energy-coupling factor transporter ATPase; |
1-229 | 1.78e-37 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 136.27 E-value: 1.78e-37
|
||||||||||
| PRK14246 | PRK14246 | phosphate ABC transporter ATP-binding protein; Provisional |
18-237 | 1.91e-37 | ||||||
phosphate ABC transporter ATP-binding protein; Provisional Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 135.56 E-value: 1.91e-37
|
||||||||||
| CydD | TIGR02857 | thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 | 2.69e-37 | ||||||
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 140.88 E-value: 2.69e-37
|
||||||||||
| nickel_nikE | TIGR02769 | nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-224 | 3.40e-37 | ||||||
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 135.32 E-value: 3.40e-37
|
||||||||||
| met_CoM_red_A2 | TIGR03269 | methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-227 | 4.76e-37 | ||||||
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis] Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 140.32 E-value: 4.76e-37
|
||||||||||
| CeuD | COG4604 | ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-222 | 7.18e-37 | ||||||
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 133.67 E-value: 7.18e-37
|
||||||||||
| fecE | PRK11231 | Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-227 | 1.12e-36 | ||||||
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 133.60 E-value: 1.12e-36
|
||||||||||
| COG4559 | COG4559 | ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-225 | 2.87e-36 | ||||||
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 132.55 E-value: 2.87e-36
|
||||||||||
| nickel_nikD | TIGR02770 | nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
17-240 | 5.06e-36 | ||||||
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 130.95 E-value: 5.06e-36
|
||||||||||
| ABC_KpsT_Wzt | cd03220 | ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-215 | 6.34e-36 | ||||||
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2. Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 130.73 E-value: 6.34e-36
|
||||||||||
| ssuB | PRK11247 | aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-221 | 8.37e-36 | ||||||
aliphatic sulfonates transport ATP-binding subunit; Provisional Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 131.34 E-value: 8.37e-36
|
||||||||||
| ABC_cobalt_CbiO_domain2 | cd03226 | Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-215 | 1.28e-35 | ||||||
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems. Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 129.30 E-value: 1.28e-35
|
||||||||||
| type_I_sec_PrtD | TIGR01842 | type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-225 | 1.96e-35 | ||||||
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 135.94 E-value: 1.96e-35
|
||||||||||
| cbiO | PRK13639 | cobalt transporter ATP-binding subunit; Provisional |
1-228 | 2.43e-35 | ||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 130.58 E-value: 2.43e-35
|
||||||||||
| PRK13536 | PRK13536 | nodulation factor ABC transporter ATP-binding protein NodI; |
2-227 | 2.51e-35 | ||||||
nodulation factor ABC transporter ATP-binding protein NodI; Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 132.26 E-value: 2.51e-35
|
||||||||||
| PRK14258 | PRK14258 | phosphate ABC transporter ATP-binding protein; Provisional |
2-237 | 2.71e-35 | ||||||
phosphate ABC transporter ATP-binding protein; Provisional Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 130.16 E-value: 2.71e-35
|
||||||||||
| modC | PRK11144 | molybdenum ABC transporter ATP-binding protein ModC; |
21-229 | 3.88e-35 | ||||||
molybdenum ABC transporter ATP-binding protein ModC; Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 131.92 E-value: 3.88e-35
|
||||||||||
| PhnL | COG4778 | Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 | 6.56e-35 | ||||||
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism]; Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 127.94 E-value: 6.56e-35
|
||||||||||
| cbiO | PRK13652 | cobalt transporter ATP-binding subunit; Provisional |
1-228 | 7.48e-35 | ||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 129.15 E-value: 7.48e-35
|
||||||||||
| cbiO | PRK13640 | energy-coupling factor transporter ATPase; |
2-228 | 8.69e-35 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 129.15 E-value: 8.69e-35
|
||||||||||
| nikE | PRK10419 | nickel ABC transporter ATP-binding protein NikE; |
16-217 | 1.15e-34 | ||||||
nickel ABC transporter ATP-binding protein NikE; Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 128.65 E-value: 1.15e-34
|
||||||||||
| cbiO | PRK13648 | cobalt transporter ATP-binding subunit; Provisional |
1-222 | 1.30e-34 | ||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 128.33 E-value: 1.30e-34
|
||||||||||
| PRK14271 | PRK14271 | phosphate ABC transporter ATP-binding protein; Provisional |
13-238 | 2.55e-34 | ||||||
phosphate ABC transporter ATP-binding protein; Provisional Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 127.90 E-value: 2.55e-34
|
||||||||||
| PRK13537 | PRK13537 | nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 | 2.71e-34 | ||||||
nodulation factor ABC transporter ATP-binding protein NodI; Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 128.38 E-value: 2.71e-34
|
||||||||||
| hmuV | PRK13548 | hemin importer ATP-binding subunit; Provisional |
1-227 | 6.58e-34 | ||||||
hemin importer ATP-binding subunit; Provisional Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.04 E-value: 6.58e-34
|
||||||||||
| PRK10535 | PRK10535 | macrolide ABC transporter ATP-binding protein/permease MacB; |
1-230 | 8.70e-34 | ||||||
macrolide ABC transporter ATP-binding protein/permease MacB; Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 132.16 E-value: 8.70e-34
|
||||||||||
| TagH | COG1134 | ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-227 | 1.53e-33 | ||||||
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism]; Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 124.81 E-value: 1.53e-33
|
||||||||||
| PhnK | COG1101 | ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-227 | 2.75e-33 | ||||||
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 124.81 E-value: 2.75e-33
|
||||||||||
| MsbA_lipidA | TIGR02203 | lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-225 | 5.72e-33 | ||||||
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other] Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 129.45 E-value: 5.72e-33
|
||||||||||
| cbiO | PRK13642 | energy-coupling factor transporter ATPase; |
1-225 | 9.15e-33 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 123.66 E-value: 9.15e-33
|
||||||||||
| lolD | PRK11629 | lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-217 | 1.17e-32 | ||||||
lipoprotein-releasing ABC transporter ATP-binding protein LolD; Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 122.23 E-value: 1.17e-32
|
||||||||||
| rim_protein | TIGR01257 | retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-245 | 1.27e-32 | ||||||
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other] Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 129.75 E-value: 1.27e-32
|
||||||||||
| PRK09700 | PRK09700 | D-allose ABC transporter ATP-binding protein AlsA; |
1-213 | 1.91e-32 | ||||||
D-allose ABC transporter ATP-binding protein AlsA; Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 127.21 E-value: 1.91e-32
|
||||||||||
| PRK11160 | PRK11160 | cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 | 2.11e-32 | ||||||
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 127.63 E-value: 2.11e-32
|
||||||||||
| galliderm_ABC | TIGR03740 | gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-215 | 2.28e-32 | ||||||
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes. Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 120.97 E-value: 2.28e-32
|
||||||||||
| urea_trans_UrtE | TIGR03410 | urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-213 | 3.19e-32 | ||||||
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines] Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 120.71 E-value: 3.19e-32
|
||||||||||
| cbiO | PRK13643 | energy-coupling factor transporter ATPase; |
1-227 | 3.33e-32 | ||||||
energy-coupling factor transporter ATPase; Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 122.53 E-value: 3.33e-32
|
||||||||||
| AztA | NF040873 | zinc ABC transporter ATP-binding protein AztA; |
13-201 | 3.61e-32 | ||||||
zinc ABC transporter ATP-binding protein AztA; Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 119.65 E-value: 3.61e-32
|
||||||||||
| cbiO | PRK13631 | cobalt transporter ATP-binding subunit; Provisional |
1-268 | 3.66e-32 | ||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 123.04 E-value: 3.66e-32
|
||||||||||
| ABCC_Hemolysin | cd03252 | ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-227 | 5.24e-32 | ||||||
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy. Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 120.67 E-value: 5.24e-32
|
||||||||||
| ABCC_MRP_domain1 | cd03250 | ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-214 | 6.49e-32 | ||||||
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate. Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 119.11 E-value: 6.49e-32
|
||||||||||
| ABCG_EPDR | cd03213 | Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-216 | 9.54e-32 | ||||||
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus. Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 118.42 E-value: 9.54e-32
|
||||||||||
| ABC_Carb_Monos_II | cd03215 | Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-215 | 1.02e-31 | ||||||
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter. Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 117.92 E-value: 1.02e-31
|
||||||||||
| CydC | TIGR02868 | thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 | 2.72e-31 | ||||||
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 124.40 E-value: 2.72e-31
|
||||||||||
| PRK13657 | PRK13657 | glucan ABC transporter ATP-binding protein/ permease; |
4-176 | 3.13e-31 | ||||||
glucan ABC transporter ATP-binding protein/ permease; Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 124.69 E-value: 3.13e-31
|
||||||||||
| ABC2_perm_RbbA | NF033858 | ribosome-associated ATPase/putative transporter RbbA; |
5-238 | 3.61e-31 | ||||||
ribosome-associated ATPase/putative transporter RbbA; Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 125.24 E-value: 3.61e-31
|
||||||||||
| PRK10584 | PRK10584 | putative ABC transporter ATP-binding protein YbbA; Provisional |
28-215 | 5.66e-31 | ||||||
putative ABC transporter ATP-binding protein YbbA; Provisional Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.57 E-value: 5.66e-31
|
||||||||||
| PRK15134 | PRK15134 | microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-237 | 1.60e-30 | ||||||
microcin C ABC transporter ATP-binding protein YejF; Provisional Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.12 E-value: 1.60e-30
|
||||||||||
| PRK15112 | PRK15112 | peptide ABC transporter ATP-binding protein SapF; |
1-240 | 1.79e-30 | ||||||
peptide ABC transporter ATP-binding protein SapF; Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 117.20 E-value: 1.79e-30
|
||||||||||
| PRK10895 | PRK10895 | lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-225 | 1.92e-30 | ||||||
lipopolysaccharide ABC transporter ATP-binding protein; Provisional Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.53 E-value: 1.92e-30
|
||||||||||
| PRK15134 | PRK15134 | microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-237 | 1.64e-29 | ||||||
microcin C ABC transporter ATP-binding protein YejF; Provisional Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 119.04 E-value: 1.64e-29
|
||||||||||
| ABCC_cytochrome_bd | cd03247 | ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-215 | 3.02e-29 | ||||||
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism. Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 111.25 E-value: 3.02e-29
|
||||||||||
| dppD | PRK11022 | dipeptide transporter ATP-binding subunit; Provisional |
1-250 | 3.95e-29 | ||||||
dipeptide transporter ATP-binding subunit; Provisional Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 115.22 E-value: 3.95e-29
|
||||||||||
| ABCC_MRP_domain2 | cd03244 | ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-221 | 8.40e-29 | ||||||
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate. Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 111.43 E-value: 8.40e-29
|
||||||||||
| araG | PRK11288 | L-arabinose ABC transporter ATP-binding protein AraG; |
2-217 | 8.60e-29 | ||||||
L-arabinose ABC transporter ATP-binding protein AraG; Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 116.93 E-value: 8.60e-29
|
||||||||||
| MsbA_rel | TIGR02204 | ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
17-225 | 1.76e-28 | ||||||
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins. Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 116.72 E-value: 1.76e-28
|
||||||||||
| PRK10575 | PRK10575 | Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-225 | 2.41e-28 | ||||||
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 111.42 E-value: 2.41e-28
|
||||||||||
| PRK11174 | PRK11174 | cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-228 | 2.58e-28 | ||||||
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 116.10 E-value: 2.58e-28
|
||||||||||
| ABC_NatA_like | cd03267 | ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-216 | 2.68e-28 | ||||||
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein. Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 110.50 E-value: 2.68e-28
|
||||||||||
| type_I_sec_HlyB | TIGR01846 | type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
21-227 | 3.39e-28 | ||||||
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 116.00 E-value: 3.39e-28
|
||||||||||
| PRK10261 | PRK10261 | glutathione transporter ATP-binding protein; Provisional |
15-230 | 3.82e-28 | ||||||
glutathione transporter ATP-binding protein; Provisional Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 115.72 E-value: 3.82e-28
|
||||||||||
| PRK11176 | PRK11176 | lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-225 | 8.00e-28 | ||||||
lipid A ABC transporter ATP-binding protein/permease MsbA; Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 114.73 E-value: 8.00e-28
|
||||||||||
| bacteriocin_ABC | TIGR01193 | ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-237 | 9.99e-28 | ||||||
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other] Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 114.84 E-value: 9.99e-28
|
||||||||||
| ABCG_White | cd03234 | White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-216 | 1.81e-27 | ||||||
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners. Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 108.13 E-value: 1.81e-27
|
||||||||||
| livF | PRK11614 | high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-229 | 3.98e-27 | ||||||
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 107.66 E-value: 3.98e-27
|
||||||||||
| btuD | PRK09536 | corrinoid ABC transporter ATPase; Reviewed |
1-258 | 8.44e-27 | ||||||
corrinoid ABC transporter ATPase; Reviewed Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.93 E-value: 8.44e-27
|
||||||||||
| COG4586 | COG4586 | ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 | 1.21e-26 | ||||||
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 108.25 E-value: 1.21e-26
|
||||||||||
| PRK09984 | PRK09984 | phosphonate ABC transporter ATP-binding protein; |
1-216 | 1.54e-26 | ||||||
phosphonate ABC transporter ATP-binding protein; Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 106.64 E-value: 1.54e-26
|
||||||||||
| Uup | COG0488 | ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-215 | 4.35e-26 | ||||||
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only]; Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.38 E-value: 4.35e-26
|
||||||||||
| COG3448 | COG3448 | CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
249-369 | 4.78e-26 | ||||||
CBS-domain-containing membrane protein [Signal transduction mechanisms]; Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 101.48 E-value: 4.78e-26
|
||||||||||
| PRK11831 | PRK11831 | phospholipid ABC transporter ATP-binding protein MlaF; |
21-237 | 5.15e-26 | ||||||
phospholipid ABC transporter ATP-binding protein MlaF; Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 105.23 E-value: 5.15e-26
|
||||||||||
| ATM1 | COG5265 | ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-178 | 7.84e-26 | ||||||
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 108.75 E-value: 7.84e-26
|
||||||||||
| MglA | COG1129 | ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-215 | 8.24e-26 | ||||||
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.18 E-value: 8.24e-26
|
||||||||||
| cbiO | PRK13636 | cobalt transporter ATP-binding subunit; Provisional |
1-227 | 8.25e-26 | ||||||
cobalt transporter ATP-binding subunit; Provisional Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.93 E-value: 8.25e-26
|
||||||||||
| nikD | PRK10418 | nickel transporter ATP-binding protein NikD; Provisional |
18-250 | 8.80e-26 | ||||||
nickel transporter ATP-binding protein NikD; Provisional Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 104.40 E-value: 8.80e-26
|
||||||||||
| rim_protein | TIGR01257 | retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-233 | 1.44e-25 | ||||||
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other] Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 108.95 E-value: 1.44e-25
|
||||||||||
| livG | PRK11300 | leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-228 | 1.58e-25 | ||||||
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 103.53 E-value: 1.58e-25
|
||||||||||
| CP_lyasePhnK | TIGR02323 | phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-234 | 2.83e-25 | ||||||
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds] Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 102.99 E-value: 2.83e-25
|
||||||||||
| phnK | PRK11701 | phosphonate C-P lyase system protein PhnK; Provisional |
1-230 | 5.35e-25 | ||||||
phosphonate C-P lyase system protein PhnK; Provisional Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 102.31 E-value: 5.35e-25
|
||||||||||
| ABCC_TAP | cd03248 | ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 | 1.48e-24 | ||||||
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes. Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 100.24 E-value: 1.48e-24
|
||||||||||
| 3a01208 | TIGR00958 | Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-228 | 2.88e-24 | ||||||
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.42 E-value: 2.88e-24
|
||||||||||
| PRK09700 | PRK09700 | D-allose ABC transporter ATP-binding protein AlsA; |
15-227 | 6.06e-24 | ||||||
D-allose ABC transporter ATP-binding protein AlsA; Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.94 E-value: 6.06e-24
|
||||||||||
| PRK10253 | PRK10253 | iron-enterobactin ABC transporter ATP-binding protein; |
13-225 | 1.52e-23 | ||||||
iron-enterobactin ABC transporter ATP-binding protein; Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.52 E-value: 1.52e-23
|
||||||||||
| PRK15093 | PRK15093 | peptide ABC transporter ATP-binding protein SapD; |
12-237 | 1.93e-23 | ||||||
peptide ABC transporter ATP-binding protein SapD; Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 99.49 E-value: 1.93e-23
|
||||||||||
| NHLM_micro_ABC1 | TIGR03796 | NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
22-230 | 3.52e-23 | ||||||
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products] Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 101.17 E-value: 3.52e-23
|
||||||||||
| PRK10247 | PRK10247 | putative ABC transporter ATP-binding protein YbbL; Provisional |
14-199 | 5.95e-23 | ||||||
putative ABC transporter ATP-binding protein YbbL; Provisional Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.94 E-value: 5.95e-23
|
||||||||||
| PRK13549 | PRK13549 | xylose transporter ATP-binding subunit; Provisional |
1-214 | 1.04e-22 | ||||||
xylose transporter ATP-binding subunit; Provisional Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.23 E-value: 1.04e-22
|
||||||||||
| NupO | COG3845 | ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-215 | 1.14e-22 | ||||||
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism]; Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.95 E-value: 1.14e-22
|
||||||||||
| PRK13539 | PRK13539 | cytochrome c biogenesis protein CcmA; Provisional |
1-195 | 1.77e-22 | ||||||
cytochrome c biogenesis protein CcmA; Provisional Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.79 E-value: 1.77e-22
|
||||||||||
| MK0520 | COG2401 | ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-198 | 2.37e-22 | ||||||
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only]; Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 93.87 E-value: 2.37e-22
|
||||||||||
| met_CoM_red_A2 | TIGR03269 | methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-224 | 3.68e-22 | ||||||
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis] Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 97.57 E-value: 3.68e-22
|
||||||||||
| SapD | COG4170 | ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-230 | 5.19e-22 | ||||||
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 95.36 E-value: 5.19e-22
|
||||||||||
| ABCD_peroxisomal_ALDP | cd03223 | ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-195 | 5.77e-22 | ||||||
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic). Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 91.45 E-value: 5.77e-22
|
||||||||||
| PRK15439 | PRK15439 | autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-215 | 9.49e-22 | ||||||
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.66 E-value: 9.49e-22
|
||||||||||
| YddA | COG4178 | ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-195 | 1.01e-21 | ||||||
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only]; Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.41 E-value: 1.01e-21
|
||||||||||
| ABCC_SUR1_N | cd03290 | ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-213 | 2.00e-21 | ||||||
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity. Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 91.24 E-value: 2.00e-21
|
||||||||||
| oppD | PRK09473 | oligopeptide transporter ATP-binding component; Provisional |
12-230 | 2.56e-21 | ||||||
oligopeptide transporter ATP-binding component; Provisional Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 93.25 E-value: 2.56e-21
|
||||||||||
| ABC2_perm_RbbA | NF033858 | ribosome-associated ATPase/putative transporter RbbA; |
5-225 | 3.46e-21 | ||||||
ribosome-associated ATPase/putative transporter RbbA; Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.58 E-value: 3.46e-21
|
||||||||||
| PRK03695 | PRK03695 | vitamin B12-transporter ATPase; Provisional |
20-228 | 5.42e-21 | ||||||
vitamin B12-transporter ATPase; Provisional Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.76 E-value: 5.42e-21
|
||||||||||
| xylG | TIGR02633 | D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-214 | 5.77e-21 | ||||||
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids] Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 94.12 E-value: 5.77e-21
|
||||||||||
| Uup | COG0488 | ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-215 | 7.15e-21 | ||||||
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only]; Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 7.15e-21
|
||||||||||
| ccmA | TIGR01189 | heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-169 | 8.59e-21 | ||||||
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other] Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 88.95 E-value: 8.59e-21
|
||||||||||
| BtuD | COG4138 | ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-225 | 1.05e-20 | ||||||
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.90 E-value: 1.05e-20
|
||||||||||
| ABCF_EF-3 | cd03221 | ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-196 | 1.08e-20 | ||||||
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions. Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 87.12 E-value: 1.08e-20
|
||||||||||
| COG2524 | COG2524 | Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
239-365 | 1.13e-20 | ||||||
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 89.17 E-value: 1.13e-20
|
||||||||||
| YtoI | COG4109 | Predicted transcriptional regulator containing CBS domains [Transcription]; |
247-366 | 1.20e-20 | ||||||
Predicted transcriptional regulator containing CBS domains [Transcription]; Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 86.89 E-value: 1.20e-20
|
||||||||||
| 3a01204 | TIGR00955 | The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-225 | 2.05e-20 | ||||||
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.80 E-value: 2.05e-20
|
||||||||||
| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
249-368 | 6.16e-20 | ||||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 84.53 E-value: 6.16e-20
|
||||||||||
| PRK11147 | PRK11147 | ABC transporter ATPase component; Reviewed |
23-215 | 1.39e-19 | ||||||
ABC transporter ATPase component; Reviewed Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 90.39 E-value: 1.39e-19
|
||||||||||
| ABCC_CFTR2 | cd03289 | ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-230 | 2.78e-19 | ||||||
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2. Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 86.83 E-value: 2.78e-19
|
||||||||||
| PRK10762 | PRK10762 | D-ribose transporter ATP binding protein; Provisional |
1-214 | 4.88e-19 | ||||||
D-ribose transporter ATP binding protein; Provisional Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.52 E-value: 4.88e-19
|
||||||||||
| PRK15056 | PRK15056 | manganese/iron ABC transporter ATP-binding protein; |
5-211 | 7.49e-19 | ||||||
manganese/iron ABC transporter ATP-binding protein; Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.32 E-value: 7.49e-19
|
||||||||||
| ABCC_NFT1 | cd03369 | ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-221 | 8.37e-19 | ||||||
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate. Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 83.62 E-value: 8.37e-19
|
||||||||||
| PRK10522 | PRK10522 | multidrug transporter membrane component/ATP-binding component; Provisional |
2-225 | 1.58e-18 | ||||||
multidrug transporter membrane component/ATP-binding component; Provisional Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 86.95 E-value: 1.58e-18
|
||||||||||
| PRK10789 | PRK10789 | SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-228 | 1.67e-18 | ||||||
SmdA family multidrug ABC transporter permease/ATP-binding protein; Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.08 E-value: 1.67e-18
|
||||||||||
| PRK10762 | PRK10762 | D-ribose transporter ATP binding protein; Provisional |
18-215 | 2.08e-18 | ||||||
D-ribose transporter ATP binding protein; Provisional Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 2.08e-18
|
||||||||||
| GguA | NF040905 | sugar ABC transporter ATP-binding protein; |
1-214 | 2.61e-18 | ||||||
sugar ABC transporter ATP-binding protein; Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.00 E-value: 2.61e-18
|
||||||||||
| PLN03211 | PLN03211 | ABC transporter G-25; Provisional |
28-216 | 7.40e-18 | ||||||
ABC transporter G-25; Provisional Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 85.32 E-value: 7.40e-18
|
||||||||||
| ABC_CcmA_heme_exporter | cd03231 | Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-195 | 1.46e-17 | ||||||
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE. Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.23 E-value: 1.46e-17
|
||||||||||
| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
256-362 | 5.89e-17 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 76.13 E-value: 5.89e-17
|
||||||||||
| PTZ00265 | PTZ00265 | multidrug resistance protein (mdr1); Provisional |
37-225 | 9.09e-17 | ||||||
multidrug resistance protein (mdr1); Provisional Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.38 E-value: 9.09e-17
|
||||||||||
| SufC | COG0396 | Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-227 | 1.00e-16 | ||||||
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.57 E-value: 1.00e-16
|
||||||||||
| PRK10982 | PRK10982 | galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-214 | 1.26e-16 | ||||||
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 80.93 E-value: 1.26e-16
|
||||||||||
| cbiO | PRK13638 | energy-coupling factor ABC transporter ATP-binding protein; |
16-221 | 1.63e-16 | ||||||
energy-coupling factor ABC transporter ATP-binding protein; Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 1.63e-16
|
||||||||||
| CFTR_protein | TIGR01271 | cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-230 | 2.14e-16 | ||||||
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions] Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 81.11 E-value: 2.14e-16
|
||||||||||
| COG2905 | COG2905 | Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
251-368 | 2.96e-16 | ||||||
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms]; Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 74.48 E-value: 2.96e-16
|
||||||||||
| PRK15439 | PRK15439 | autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-215 | 5.70e-16 | ||||||
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 5.70e-16
|
||||||||||
| CFTR_protein | TIGR01271 | cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-213 | 1.20e-15 | ||||||
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions] Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 78.80 E-value: 1.20e-15
|
||||||||||
| ABCC_CFTR1 | cd03291 | ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-213 | 2.54e-15 | ||||||
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2. Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 75.28 E-value: 2.54e-15
|
||||||||||
| CBS_pair_ABC_OpuCA_assoc | cd04583 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
271-365 | 3.11e-15 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341360 [Multi-domain] Cd Length: 110 Bit Score: 71.01 E-value: 3.11e-15
|
||||||||||
| MRP_assoc_pro | TIGR00957 | multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-225 | 3.15e-15 | ||||||
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other] Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 77.68 E-value: 3.15e-15
|
||||||||||
| PTZ00243 | PTZ00243 | ABC transporter; Provisional |
2-234 | 3.22e-15 | ||||||
ABC transporter; Provisional Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.51 E-value: 3.22e-15
|
||||||||||
| PLN03232 | PLN03232 | ABC transporter C family member; Provisional |
1-232 | 4.41e-15 | ||||||
ABC transporter C family member; Provisional Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.94 E-value: 4.41e-15
|
||||||||||
| 40850658_otr | NF000106 | oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-231 | 5.24e-15 | ||||||
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.54 E-value: 5.24e-15
|
||||||||||
| hmuV | PRK13547 | heme ABC transporter ATP-binding protein; |
18-230 | 7.39e-15 | ||||||
heme ABC transporter ATP-binding protein; Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.09 E-value: 7.39e-15
|
||||||||||
| ABCG_PDR_domain1 | cd03233 | First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-214 | 3.32e-14 | ||||||
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 70.75 E-value: 3.32e-14
|
||||||||||
| PRK13546 | PRK13546 | teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-244 | 3.45e-14 | ||||||
teichoic acids export ABC transporter ATP-binding subunit TagH; Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.77 E-value: 3.45e-14
|
||||||||||
| PLN03130 | PLN03130 | ABC transporter C family member; Provisional |
21-226 | 9.78e-14 | ||||||
ABC transporter C family member; Provisional Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 9.78e-14
|
||||||||||
| ABC_FeS_Assembly | cd03217 | ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-232 | 9.81e-14 | ||||||
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet. Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 69.09 E-value: 9.81e-14
|
||||||||||
| PRK10982 | PRK10982 | galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-215 | 1.43e-13 | ||||||
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 1.43e-13
|
||||||||||
| PRK10790 | PRK10790 | SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-225 | 1.95e-13 | ||||||
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.67 E-value: 1.95e-13
|
||||||||||
| ABCC_SUR2 | cd03288 | ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-225 | 2.68e-13 | ||||||
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity. Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 69.17 E-value: 2.68e-13
|
||||||||||
| znuC | PRK09544 | high-affinity zinc transporter ATPase; Reviewed |
1-197 | 3.46e-13 | ||||||
high-affinity zinc transporter ATPase; Reviewed Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 3.46e-13
|
||||||||||
| PTZ00243 | PTZ00243 | ABC transporter; Provisional |
4-215 | 5.80e-13 | ||||||
ABC transporter; Provisional Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.58 E-value: 5.80e-13
|
||||||||||
| PLN03130 | PLN03130 | ABC transporter C family member; Provisional |
2-225 | 6.75e-13 | ||||||
ABC transporter C family member; Provisional Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.15 E-value: 6.75e-13
|
||||||||||
| araG | PRK11288 | L-arabinose ABC transporter ATP-binding protein AraG; |
21-215 | 9.02e-13 | ||||||
L-arabinose ABC transporter ATP-binding protein AraG; Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 9.02e-13
|
||||||||||
| PRK13543 | PRK13543 | heme ABC exporter ATP-binding protein CcmA; |
23-195 | 9.33e-13 | ||||||
heme ABC exporter ATP-binding protein CcmA; Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 9.33e-13
|
||||||||||
| CBS_pair_Mg_transporter | cd04606 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ... |
254-357 | 1.49e-12 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341380 [Multi-domain] Cd Length: 121 Bit Score: 63.89 E-value: 1.49e-12
|
||||||||||
| PRK13538 | PRK13538 | cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-195 | 1.49e-12 | ||||||
cytochrome c biogenesis heme-transporting ATPase CcmA; Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 1.49e-12
|
||||||||||
| ABC_RNaseL_inhibitor_domain2 | cd03237 | The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-214 | 2.71e-12 | ||||||
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology. Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.89 E-value: 2.71e-12
|
||||||||||
| ABCG_PDR_domain2 | cd03232 | Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-168 | 3.79e-12 | ||||||
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 64.57 E-value: 3.79e-12
|
||||||||||
| CBS_pair_HPP_assoc | cd04600 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
255-365 | 4.14e-12 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 62.96 E-value: 4.14e-12
|
||||||||||
| AAA | smart00382 | ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-209 | 4.21e-12 | ||||||
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment. Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.55 E-value: 4.21e-12
|
||||||||||
| MgtE | COG2239 | Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism]; |
254-357 | 4.74e-12 | ||||||
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism]; Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 67.01 E-value: 4.74e-12
|
||||||||||
| CBS_pair_AcuB_like | cd04584 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
251-365 | 4.78e-12 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 62.82 E-value: 4.78e-12
|
||||||||||
| PLN03232 | PLN03232 | ABC transporter C family member; Provisional |
21-224 | 6.72e-12 | ||||||
ABC transporter C family member; Provisional Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 6.72e-12
|
||||||||||
| ycf16 | CHL00131 | sulfate ABC transporter protein; Validated |
1-216 | 1.06e-11 | ||||||
sulfate ABC transporter protein; Validated Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 1.06e-11
|
||||||||||
| PTZ00265 | PTZ00265 | multidrug resistance protein (mdr1); Provisional |
2-197 | 1.09e-11 | ||||||
multidrug resistance protein (mdr1); Provisional Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 1.09e-11
|
||||||||||
| xylG | TIGR02633 | D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-215 | 1.84e-11 | ||||||
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids] Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.23 E-value: 1.84e-11
|
||||||||||
| PvdE | COG4615 | ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
12-222 | 2.64e-11 | ||||||
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism]; Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 64.82 E-value: 2.64e-11
|
||||||||||
| PRK10938 | PRK10938 | putative molybdenum transport ATP-binding protein ModF; Provisional |
22-200 | 3.18e-11 | ||||||
putative molybdenum transport ATP-binding protein ModF; Provisional Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 3.18e-11
|
||||||||||
| 3a01203 | TIGR00954 | Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-195 | 3.40e-11 | ||||||
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids] Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.77 E-value: 3.40e-11
|
||||||||||
| CBS_pair_DRTGG_assoc | cd04596 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
285-364 | 3.72e-11 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341371 [Multi-domain] Cd Length: 108 Bit Score: 59.41 E-value: 3.72e-11
|
||||||||||
| tagH | PRK13545 | teichoic acids export protein ATP-binding subunit; Provisional |
2-199 | 5.97e-11 | ||||||
teichoic acids export protein ATP-binding subunit; Provisional Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.76 E-value: 5.97e-11
|
||||||||||
| PRK13540 | PRK13540 | cytochrome c biogenesis protein CcmA; Provisional |
18-195 | 6.70e-11 | ||||||
cytochrome c biogenesis protein CcmA; Provisional Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.12 E-value: 6.70e-11
|
||||||||||
| CBS_pair_plant_CBSX | cd17789 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ... |
256-364 | 8.63e-11 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341425 [Multi-domain] Cd Length: 141 Bit Score: 59.41 E-value: 8.63e-11
|
||||||||||
| CBS_pair_bac | cd04629 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ... |
255-364 | 1.67e-10 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 57.83 E-value: 1.67e-10
|
||||||||||
| CBS_pair_arch_MET2_assoc | cd04605 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
251-357 | 1.82e-10 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 57.63 E-value: 1.82e-10
|
||||||||||
| ABC_ABC_ChvD | TIGR03719 | ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-168 | 2.59e-10 | ||||||
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown. Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 2.59e-10
|
||||||||||
| PRK13549 | PRK13549 | xylose transporter ATP-binding subunit; Provisional |
18-215 | 3.07e-10 | ||||||
xylose transporter ATP-binding subunit; Provisional Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 3.07e-10
|
||||||||||
| CBS_pair_ACT | cd17787 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Thermatoga ... |
269-365 | 4.10e-10 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Thermatoga in combination with an ACT domain; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341423 [Multi-domain] Cd Length: 111 Bit Score: 56.66 E-value: 4.10e-10
|
||||||||||
| PRK15064 | PRK15064 | ABC transporter ATP-binding protein; Provisional |
2-215 | 4.81e-10 | ||||||
ABC transporter ATP-binding protein; Provisional Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 4.81e-10
|
||||||||||
| CBS_pair_arch | cd09836 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ... |
255-357 | 5.07e-10 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 56.38 E-value: 5.07e-10
|
||||||||||
| COG2905 | COG2905 | Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
245-307 | 5.98e-10 | ||||||
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms]; Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 56.38 E-value: 5.98e-10
|
||||||||||
| ABC_ABC_ChvD | TIGR03719 | ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-196 | 1.05e-09 | ||||||
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown. Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.95 E-value: 1.05e-09
|
||||||||||
| CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
251-307 | 1.53e-09 | ||||||
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP. Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 53.37 E-value: 1.53e-09
|
||||||||||
| CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc | cd17771 | CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ... |
254-363 | 1.76e-09 | ||||||
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341407 [Multi-domain] Cd Length: 115 Bit Score: 55.02 E-value: 1.76e-09
|
||||||||||
| CBS_arch_repeat1 | cd17777 | CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ... |
270-363 | 4.25e-09 | ||||||
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341413 [Multi-domain] Cd Length: 137 Bit Score: 54.27 E-value: 4.25e-09
|
||||||||||
| CBS_pair_bact_arch | cd17775 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
245-305 | 5.09e-09 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 53.70 E-value: 5.09e-09
|
||||||||||
| CBS_pair_SIS_assoc | cd04604 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
250-303 | 5.17e-09 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341378 [Multi-domain] Cd Length: 124 Bit Score: 53.92 E-value: 5.17e-09
|
||||||||||
| PRK10938 | PRK10938 | putative molybdenum transport ATP-binding protein ModF; Provisional |
113-227 | 7.21e-09 | ||||||
putative molybdenum transport ATP-binding protein ModF; Provisional Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 7.21e-09
|
||||||||||
| PRK11819 | PRK11819 | putative ABC transporter ATP-binding protein; Reviewed |
2-168 | 9.32e-09 | ||||||
putative ABC transporter ATP-binding protein; Reviewed Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 9.32e-09
|
||||||||||
| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
250-303 | 1.35e-08 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 52.25 E-value: 1.35e-08
|
||||||||||
| Rli1 | COG1245 | Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-168 | 1.50e-08 | ||||||
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.33 E-value: 1.50e-08
|
||||||||||
| PRK13409 | PRK13409 | ribosome biogenesis/translation initiation ATPase RLI; |
1-168 | 1.70e-08 | ||||||
ribosome biogenesis/translation initiation ATPase RLI; Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.70e-08
|
||||||||||
| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
311-375 | 1.79e-08 | ||||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 52.56 E-value: 1.79e-08
|
||||||||||
| CBS_pair_BON_assoc | cd04586 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
255-364 | 1.96e-08 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 52.43 E-value: 1.96e-08
|
||||||||||
| CBS_pair_arch1_repeat2 | cd04632 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ... |
256-364 | 2.02e-08 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341395 [Multi-domain] Cd Length: 127 Bit Score: 52.33 E-value: 2.02e-08
|
||||||||||
| CBS_pair_Euryarchaeota | cd17784 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ... |
259-366 | 2.63e-08 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341420 [Multi-domain] Cd Length: 120 Bit Score: 51.65 E-value: 2.63e-08
|
||||||||||
| CBS_pair_HRP1_like | cd04622 | CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ... |
245-301 | 2.99e-08 | ||||||
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341390 [Multi-domain] Cd Length: 115 Bit Score: 51.27 E-value: 2.99e-08
|
||||||||||
| CBS_pair_peptidase_M50 | cd04801 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ... |
253-364 | 5.09e-08 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341401 [Multi-domain] Cd Length: 113 Bit Score: 50.64 E-value: 5.09e-08
|
||||||||||
| ABC_UvrA_I | cd03270 | ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-207 | 6.02e-08 | ||||||
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases. Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 53.03 E-value: 6.02e-08
|
||||||||||
| PRK13409 | PRK13409 | ribosome biogenesis/translation initiation ATPase RLI; |
33-168 | 7.49e-08 | ||||||
ribosome biogenesis/translation initiation ATPase RLI; Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 7.49e-08
|
||||||||||
| CBS_pair_ABC_Gly_Pro_assoc | cd09831 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
267-364 | 7.53e-08 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341402 [Multi-domain] Cd Length: 116 Bit Score: 50.25 E-value: 7.53e-08
|
||||||||||
| PRK11147 | PRK11147 | ABC transporter ATPase component; Reviewed |
5-196 | 1.06e-07 | ||||||
ABC transporter ATPase component; Reviewed Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 1.06e-07
|
||||||||||
| CBS_pair_bac | cd17783 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ... |
267-363 | 1.37e-07 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341419 [Multi-domain] Cd Length: 108 Bit Score: 49.49 E-value: 1.37e-07
|
||||||||||
| 3a01205 | TIGR00956 | Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-168 | 1.40e-07 | ||||||
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 1.40e-07
|
||||||||||
| Rli1 | COG1245 | Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-168 | 1.41e-07 | ||||||
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.25 E-value: 1.41e-07
|
||||||||||
| CBS_pair_NTP_transferase_assoc | cd04607 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ... |
250-303 | 1.42e-07 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341381 [Multi-domain] Cd Length: 112 Bit Score: 49.37 E-value: 1.42e-07
|
||||||||||
| CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
311-367 | 1.52e-07 | ||||||
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP. Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 47.59 E-value: 1.52e-07
|
||||||||||
| CBS_pair_AcuB_like | cd04584 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
249-305 | 2.67e-07 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 48.96 E-value: 2.67e-07
|
||||||||||
| CBS_pair_MUG70_1 | cd17781 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ... |
276-355 | 3.58e-07 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341417 [Multi-domain] Cd Length: 118 Bit Score: 48.35 E-value: 3.58e-07
|
||||||||||
| CBS_pair_BON_assoc | cd04586 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
249-303 | 3.98e-07 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 48.58 E-value: 3.98e-07
|
||||||||||
| ABC_RNaseL_inhibitor_domain1 | cd03236 | The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-197 | 4.20e-07 | ||||||
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology. Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.83 E-value: 4.20e-07
|
||||||||||
| CBS_pair_bact_arch | cd17775 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
255-357 | 4.47e-07 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 48.31 E-value: 4.47e-07
|
||||||||||
| CBS_pair_arch | cd09836 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ... |
250-305 | 5.18e-07 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 47.90 E-value: 5.18e-07
|
||||||||||
| CBS_archAMPK_gamma-repeat2 | cd04631 | CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ... |
251-365 | 5.51e-07 | ||||||
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341394 [Multi-domain] Cd Length: 130 Bit Score: 48.38 E-value: 5.51e-07
|
||||||||||
| CBS_pair_inorgPPase | cd04597 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ... |
264-363 | 7.32e-07 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341372 [Multi-domain] Cd Length: 106 Bit Score: 47.34 E-value: 7.32e-07
|
||||||||||
| CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc | cd04587 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
276-357 | 7.53e-07 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341363 [Multi-domain] Cd Length: 114 Bit Score: 47.42 E-value: 7.53e-07
|
||||||||||
| CBS_pair_SIS_assoc | cd04604 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
284-356 | 8.52e-07 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341378 [Multi-domain] Cd Length: 124 Bit Score: 47.38 E-value: 8.52e-07
|
||||||||||
| PLN03140 | PLN03140 | ABC transporter G family member; Provisional |
10-168 | 9.31e-07 | ||||||
ABC transporter G family member; Provisional Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 9.31e-07
|
||||||||||
| CBS_arch_repeat2 | cd17778 | CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ... |
250-365 | 9.90e-07 | ||||||
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 47.33 E-value: 9.90e-07
|
||||||||||
| GguA | NF040905 | sugar ABC transporter ATP-binding protein; |
16-226 | 1.11e-06 | ||||||
sugar ABC transporter ATP-binding protein; Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 1.11e-06
|
||||||||||
| ABC_RNaseL_inhibitor | cd03222 | ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-209 | 1.19e-06 | ||||||
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology. Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 1.19e-06
|
||||||||||
| CBS_pair_archHTH_assoc | cd04588 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ... |
277-362 | 1.31e-06 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341364 [Multi-domain] Cd Length: 111 Bit Score: 46.76 E-value: 1.31e-06
|
||||||||||
| CBS_pair_bac_euk | cd04623 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
249-303 | 1.37e-06 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 46.64 E-value: 1.37e-06
|
||||||||||
| 3a01205 | TIGR00956 | Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-214 | 2.51e-06 | ||||||
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 2.51e-06
|
||||||||||
| CBS_arch_repeat2 | cd17778 | CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ... |
206-305 | 2.62e-06 | ||||||
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 46.17 E-value: 2.62e-06
|
||||||||||
| PTZ00314 | PTZ00314 | inosine-5'-monophosphate dehydrogenase; Provisional |
260-364 | 2.86e-06 | ||||||
inosine-5'-monophosphate dehydrogenase; Provisional Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 49.20 E-value: 2.86e-06
|
||||||||||
| MRP_assoc_pro | TIGR00957 | multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-227 | 3.46e-06 | ||||||
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other] Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.17 E-value: 3.46e-06
|
||||||||||
| CBS_pair_arch2_repeat1 | cd04638 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ... |
255-364 | 4.05e-06 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341396 [Multi-domain] Cd Length: 109 Bit Score: 45.03 E-value: 4.05e-06
|
||||||||||
| PRK07807 | PRK07807 | GuaB1 family IMP dehydrogenase-related protein; |
271-364 | 5.07e-06 | ||||||
GuaB1 family IMP dehydrogenase-related protein; Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 48.36 E-value: 5.07e-06
|
||||||||||
| CBS_pair_IMPDH | cd04601 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
257-358 | 5.30e-06 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 44.71 E-value: 5.30e-06
|
||||||||||
| PLN03073 | PLN03073 | ABC transporter F family; Provisional |
112-195 | 5.36e-06 | ||||||
ABC transporter F family; Provisional Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 5.36e-06
|
||||||||||
| PRK13541 | PRK13541 | cytochrome c biogenesis protein CcmA; Provisional |
35-177 | 6.53e-06 | ||||||
cytochrome c biogenesis protein CcmA; Provisional Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 6.53e-06
|
||||||||||
| IMPDH | pfam00478 | IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
255-358 | 6.68e-06 | ||||||
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family. Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 47.77 E-value: 6.68e-06
|
||||||||||
| CBS_pair_Mg_transporter | cd04606 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ... |
241-302 | 7.83e-06 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341380 [Multi-domain] Cd Length: 121 Bit Score: 44.63 E-value: 7.83e-06
|
||||||||||
| ABC_UvrA | cd03238 | ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
137-207 | 8.40e-06 | ||||||
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases. Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 8.40e-06
|
||||||||||
| PRK11819 | PRK11819 | putative ABC transporter ATP-binding protein; Reviewed |
6-196 | 1.36e-05 | ||||||
putative ABC transporter ATP-binding protein; Reviewed Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 1.36e-05
|
||||||||||
| CBS_pair_voltage-gated_CLC_archaea | cd04594 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
269-364 | 1.97e-05 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in archaea; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in archaea. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341369 [Multi-domain] Cd Length: 107 Bit Score: 43.10 E-value: 1.97e-05
|
||||||||||
| CBS_pair_MUG70_2 | cd17782 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ... |
270-357 | 1.97e-05 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341418 [Multi-domain] Cd Length: 118 Bit Score: 43.39 E-value: 1.97e-05
|
||||||||||
| uvra | TIGR00630 | excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
109-228 | 2.09e-05 | ||||||
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 2.09e-05
|
||||||||||
| CBS_pair_voltage-gated_CLC_bac | cd04613 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
278-364 | 2.59e-05 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341385 [Multi-domain] Cd Length: 119 Bit Score: 42.95 E-value: 2.59e-05
|
||||||||||
| CBS_pair_arch1_repeat2 | cd04632 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ... |
249-303 | 2.61e-05 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341395 [Multi-domain] Cd Length: 127 Bit Score: 43.47 E-value: 2.61e-05
|
||||||||||
| CBS_pair_HRP1_like | cd04622 | CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ... |
255-361 | 2.79e-05 | ||||||
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341390 [Multi-domain] Cd Length: 115 Bit Score: 42.79 E-value: 2.79e-05
|
||||||||||
| YtoI | COG4109 | Predicted transcriptional regulator containing CBS domains [Transcription]; |
242-305 | 2.93e-05 | ||||||
Predicted transcriptional regulator containing CBS domains [Transcription]; Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 43.36 E-value: 2.93e-05
|
||||||||||
| CBS_pair_NTP_transferase_assoc | cd04607 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ... |
284-363 | 3.46e-05 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341381 [Multi-domain] Cd Length: 112 Bit Score: 42.43 E-value: 3.46e-05
|
||||||||||
| sufC | PRK09580 | cysteine desulfurase ATPase component; Reviewed |
1-195 | 3.64e-05 | ||||||
cysteine desulfurase ATPase component; Reviewed Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 3.64e-05
|
||||||||||
| CBS_pair_bac_euk | cd04623 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
259-356 | 3.78e-05 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 42.40 E-value: 3.78e-05
|
||||||||||
| CBS_pair_ParBc_assoc | cd04610 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ... |
286-357 | 4.07e-05 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341383 [Multi-domain] Cd Length: 108 Bit Score: 42.31 E-value: 4.07e-05
|
||||||||||
| CBS_pair_arch_MET2_assoc | cd04605 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
253-301 | 4.18e-05 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 42.61 E-value: 4.18e-05
|
||||||||||
| IMPDH | pfam00478 | IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
250-306 | 4.21e-05 | ||||||
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family. Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 45.46 E-value: 4.21e-05
|
||||||||||
| CBS | smart00116 | Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
259-305 | 4.66e-05 | ||||||
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease. Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 40.57 E-value: 4.66e-05
|
||||||||||
| PRK15064 | PRK15064 | ABC transporter ATP-binding protein; Provisional |
4-196 | 4.80e-05 | ||||||
ABC transporter ATP-binding protein; Provisional Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 4.80e-05
|
||||||||||
| ABC_Class2 | cd03227 | ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-211 | 7.14e-05 | ||||||
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins. Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 7.14e-05
|
||||||||||
| CBS_archAMPK_gamma-repeat1 | cd17779 | signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ... |
251-365 | 1.00e-04 | ||||||
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341415 [Multi-domain] Cd Length: 136 Bit Score: 41.83 E-value: 1.00e-04
|
||||||||||
| COG2524 | COG2524 | Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
291-370 | 1.49e-04 | ||||||
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 42.56 E-value: 1.49e-04
|
||||||||||
| ABC_UvrA_II | cd03271 | ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-198 | 1.57e-04 | ||||||
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases. Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.99 E-value: 1.57e-04
|
||||||||||
| CBS_pair_AcuB_like | cd04584 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
310-368 | 1.79e-04 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 40.87 E-value: 1.79e-04
|
||||||||||
| mgtE | TIGR00400 | Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ... |
260-371 | 1.99e-04 | ||||||
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ transporter first described in Bacillus firmus. May form a homodimer. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 129495 [Multi-domain] Cd Length: 449 Bit Score: 43.27 E-value: 1.99e-04
|
||||||||||
| CBS_pair_DHH_polyA_Pol_assoc | cd04595 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
256-364 | 2.30e-04 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341370 [Multi-domain] Cd Length: 110 Bit Score: 40.17 E-value: 2.30e-04
|
||||||||||
| CBS_pair_peptidase_M50 | cd04801 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ... |
247-303 | 2.43e-04 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341401 [Multi-domain] Cd Length: 113 Bit Score: 40.24 E-value: 2.43e-04
|
||||||||||
| CBS_pair_bac | cd04643 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ... |
285-366 | 2.61e-04 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341400 [Multi-domain] Cd Length: 130 Bit Score: 40.56 E-value: 2.61e-04
|
||||||||||
| CBS | smart00116 | Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
322-364 | 2.77e-04 | ||||||
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease. Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 38.26 E-value: 2.77e-04
|
||||||||||
| CBS_pair_archHTH_assoc | cd04588 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ... |
209-304 | 3.27e-04 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341364 [Multi-domain] Cd Length: 111 Bit Score: 39.82 E-value: 3.27e-04
|
||||||||||
| CBS_two-component_sensor_histidine_kinase_repeat1 | cd04620 | 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ... |
233-364 | 3.31e-04 | ||||||
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341389 [Multi-domain] Cd Length: 136 Bit Score: 40.21 E-value: 3.31e-04
|
||||||||||
| PRK14869 | PRK14869 | putative manganese-dependent inorganic diphosphatase; |
246-317 | 3.33e-04 | ||||||
putative manganese-dependent inorganic diphosphatase; Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 42.51 E-value: 3.33e-04
|
||||||||||
| CBS_pair_ParBc_assoc | cd04610 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ... |
223-303 | 5.39e-04 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341383 [Multi-domain] Cd Length: 108 Bit Score: 39.23 E-value: 5.39e-04
|
||||||||||
| CBS_pair_IMPDH | cd04601 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
249-303 | 5.60e-04 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 38.93 E-value: 5.60e-04
|
||||||||||
| CBS_CbpB | NF041630 | cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS ... |
285-367 | 5.89e-04 | ||||||
cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS (cystathionine beta synthase) domains (see PF00571). When levels of c-di-AMP are low, CbpB activates RelA, a bifunctional (p)ppGpp synthetase/hydrolase. Pssm-ID: 469514 [Multi-domain] Cd Length: 143 Bit Score: 39.74 E-value: 5.89e-04
|
||||||||||
| PilT | COG2805 | Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
31-75 | 6.32e-04 | ||||||
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures]; Pssm-ID: 442056 Cd Length: 342 Bit Score: 41.23 E-value: 6.32e-04
|
||||||||||
| ABC_Rad50 | cd03240 | ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
15-213 | 7.76e-04 | ||||||
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence. Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.28 E-value: 7.76e-04
|
||||||||||
| CBS_pair_GGDEF_PAS_repeat1 | cd09833 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ... |
250-304 | 8.32e-04 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341403 [Multi-domain] Cd Length: 116 Bit Score: 38.74 E-value: 8.32e-04
|
||||||||||
| gutQ | PRK11543 | arabinose-5-phosphate isomerase GutQ; |
250-301 | 8.45e-04 | ||||||
arabinose-5-phosphate isomerase GutQ; Pssm-ID: 183186 [Multi-domain] Cd Length: 321 Bit Score: 40.91 E-value: 8.45e-04
|
||||||||||
| CBS_two-component_sensor_histidine_kinase_repeat2 | cd17774 | 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ... |
250-310 | 8.60e-04 | ||||||
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 2; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341410 [Multi-domain] Cd Length: 137 Bit Score: 39.06 E-value: 8.60e-04
|
||||||||||
| PRK00635 | PRK00635 | excinuclease ABC subunit A; Provisional |
111-207 | 9.51e-04 | ||||||
excinuclease ABC subunit A; Provisional Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 9.51e-04
|
||||||||||
| CBS_pair_voltage-gated_CLC_euk_bac | cd04592 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
255-361 | 1.02e-03 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341368 [Multi-domain] Cd Length: 128 Bit Score: 38.89 E-value: 1.02e-03
|
||||||||||
| UvrA | COG0178 | Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-43 | 1.05e-03 | ||||||
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 1.05e-03
|
||||||||||
| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
320-369 | 1.08e-03 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 38.38 E-value: 1.08e-03
|
||||||||||
| MgtE | COG2239 | Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism]; |
241-313 | 1.24e-03 | ||||||
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism]; Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 40.82 E-value: 1.24e-03
|
||||||||||
| SbcC | COG0419 | DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-196 | 1.31e-03 | ||||||
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 1.31e-03
|
||||||||||
| CBS_pair_CcpN | cd04617 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ... |
283-358 | 1.40e-03 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341387 [Multi-domain] Cd Length: 125 Bit Score: 38.24 E-value: 1.40e-03
|
||||||||||
| CBS_pair_SIS_assoc | cd04604 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
311-361 | 1.46e-03 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341378 [Multi-domain] Cd Length: 124 Bit Score: 38.13 E-value: 1.46e-03
|
||||||||||
| PRK10636 | PRK10636 | putative ABC transporter ATP-binding protein; Provisional |
111-198 | 1.52e-03 | ||||||
putative ABC transporter ATP-binding protein; Provisional Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 1.52e-03
|
||||||||||
| CBS_archAMPK_gamma-repeat1 | cd17779 | signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ... |
250-305 | 1.74e-03 | ||||||
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341415 [Multi-domain] Cd Length: 136 Bit Score: 38.37 E-value: 1.74e-03
|
||||||||||
| CBS_pair_arch2_repeat1 | cd04638 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ... |
237-302 | 1.86e-03 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341396 [Multi-domain] Cd Length: 109 Bit Score: 37.71 E-value: 1.86e-03
|
||||||||||
| ABC_sbcCD | cd03279 | ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
13-213 | 1.98e-03 | ||||||
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini. Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.17 E-value: 1.98e-03
|
||||||||||
| COG4938 | COG4938 | Predicted ATPase [General function prediction only]; |
14-195 | 2.38e-03 | ||||||
Predicted ATPase [General function prediction only]; Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.18 E-value: 2.38e-03
|
||||||||||
| CBS_pair_GGDEF_assoc | cd04599 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
255-364 | 4.37e-03 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 36.55 E-value: 4.37e-03
|
||||||||||
| PilT | cd01131 | Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
31-61 | 6.08e-03 | ||||||
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility. Pssm-ID: 410875 [Multi-domain] Cd Length: 223 Bit Score: 37.90 E-value: 6.08e-03
|
||||||||||
| CBS_pair_CBS | cd04608 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
327-367 | 6.31e-03 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 36.36 E-value: 6.31e-03
|
||||||||||
| CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc | cd04587 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
250-302 | 6.94e-03 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341363 [Multi-domain] Cd Length: 114 Bit Score: 35.86 E-value: 6.94e-03
|
||||||||||
| CBS_pair_GGDEF_assoc | cd04599 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
251-302 | 8.05e-03 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 35.78 E-value: 8.05e-03
|
||||||||||
| YbjD | COG3593 | Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
14-195 | 8.23e-03 | ||||||
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair]; Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.06 E-value: 8.23e-03
|
||||||||||
| Blast search parameters | ||||
|
