MULTISPECIES: CNNM family magnesium/cobalt transport protein CorC [Klebsiella]
Protein Classification
HlyC/CorC family transporter( domain architecture ID 11487637)
HlyC/CorC family transporter similar to magnesium and cobalt efflux protein CorC and hemolysin C; the precise transport mechanism is unknown
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PRK15094 | PRK15094 | magnesium/cobalt transporter CorC; |
1-292 | 0e+00 | |||||
magnesium/cobalt transporter CorC; : Pssm-ID: 185050 [Multi-domain] Cd Length: 292 Bit Score: 557.50 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| PRK15094 | PRK15094 | magnesium/cobalt transporter CorC; |
1-292 | 0e+00 | |||||
magnesium/cobalt transporter CorC; Pssm-ID: 185050 [Multi-domain] Cd Length: 292 Bit Score: 557.50 E-value: 0e+00
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| CorC | COG4535 | Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ... |
1-291 | 4.84e-170 | |||||
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion transport and metabolism]; Pssm-ID: 443601 [Multi-domain] Cd Length: 288 Bit Score: 471.90 E-value: 4.84e-170
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| CBS_pair_CorC_HlyC_assoc | cd04590 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ... |
68-186 | 1.19e-50 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. 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: 341366 [Multi-domain] Cd Length: 119 Bit Score: 162.67 E-value: 1.19e-50
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| CorC_HlyC | smart01091 | Transporter associated domain; This small domain is found in a family of proteins with the ... |
205-282 | 2.48e-26 | |||||
Transporter associated domain; This small domain is found in a family of proteins with the DUF21 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates. Pssm-ID: 215020 [Multi-domain] Cd Length: 78 Bit Score: 98.67 E-value: 2.48e-26
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| CorC_HlyC | pfam03471 | Transporter associated domain; This small domain is found in a family of proteins with the ... |
205-283 | 4.39e-21 | |||||
Transporter associated domain; This small domain is found in a family of proteins with the pfam01595 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates. Pssm-ID: 460935 [Multi-domain] Cd Length: 81 Bit Score: 84.90 E-value: 4.39e-21
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| Name | Accession | Description | Interval | E-value | |||||
| PRK15094 | PRK15094 | magnesium/cobalt transporter CorC; |
1-292 | 0e+00 | |||||
magnesium/cobalt transporter CorC; Pssm-ID: 185050 [Multi-domain] Cd Length: 292 Bit Score: 557.50 E-value: 0e+00
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| CorC | COG4535 | Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ... |
1-291 | 4.84e-170 | |||||
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion transport and metabolism]; Pssm-ID: 443601 [Multi-domain] Cd Length: 288 Bit Score: 471.90 E-value: 4.84e-170
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| TlyC | COG1253 | Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ... |
22-289 | 3.23e-94 | |||||
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only]; Pssm-ID: 440865 [Multi-domain] Cd Length: 435 Bit Score: 285.09 E-value: 3.23e-94
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| CorB | COG4536 | Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ... |
18-283 | 8.98e-66 | |||||
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion transport and metabolism]; Pssm-ID: 443602 [Multi-domain] Cd Length: 420 Bit Score: 211.47 E-value: 8.98e-66
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| CBS_pair_CorC_HlyC_assoc | cd04590 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ... |
68-186 | 1.19e-50 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. 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: 341366 [Multi-domain] Cd Length: 119 Bit Score: 162.67 E-value: 1.19e-50
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| CorC_HlyC | smart01091 | Transporter associated domain; This small domain is found in a family of proteins with the ... |
205-282 | 2.48e-26 | |||||
Transporter associated domain; This small domain is found in a family of proteins with the DUF21 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates. Pssm-ID: 215020 [Multi-domain] Cd Length: 78 Bit Score: 98.67 E-value: 2.48e-26
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| PRK11573 | PRK11573 | hypothetical protein; Provisional |
34-280 | 1.51e-25 | |||||
hypothetical protein; Provisional Pssm-ID: 236933 [Multi-domain] Cd Length: 413 Bit Score: 104.83 E-value: 1.51e-25
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| CorC_HlyC | pfam03471 | Transporter associated domain; This small domain is found in a family of proteins with the ... |
205-283 | 4.39e-21 | |||||
Transporter associated domain; This small domain is found in a family of proteins with the pfam01595 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates. Pssm-ID: 460935 [Multi-domain] Cd Length: 81 Bit Score: 84.90 E-value: 4.39e-21
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| COG2524 | COG2524 | Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
61-188 | 7.32e-13 | |||||
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 66.06 E-value: 7.32e-13
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| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
68-189 | 6.16e-11 | |||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 58.72 E-value: 6.16e-11
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| YtoI | COG4109 | Predicted transcriptional regulator containing CBS domains [Transcription]; |
68-186 | 2.44e-10 | |||||
Predicted transcriptional regulator containing CBS domains [Transcription]; Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 57.23 E-value: 2.44e-10
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| COG3448 | COG3448 | CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
68-189 | 4.14e-10 | |||||
CBS-domain-containing membrane protein [Signal transduction mechanisms]; Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 56.80 E-value: 4.14e-10
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| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
80-185 | 1.27e-09 | |||||
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: 54.94 E-value: 1.27e-09
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| CBS_pair_peptidase_M50 | cd04639 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ... |
71-188 | 5.27e-07 | |||||
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: 341397 [Multi-domain] Cd Length: 120 Bit Score: 47.57 E-value: 5.27e-07
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| COG2905 | COG2905 | Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
69-188 | 4.34e-06 | |||||
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms]; Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 45.21 E-value: 4.34e-06
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| CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
69-123 | 6.15e-06 | |||||
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: 42.97 E-value: 6.15e-06
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| CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
140-190 | 8.52e-05 | |||||
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: 39.50 E-value: 8.52e-05
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| COG3448 | COG3448 | CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
46-123 | 1.01e-04 | |||||
CBS-domain-containing membrane protein [Signal transduction mechanisms]; Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 41.39 E-value: 1.01e-04
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| CBS_pair_IMPDH | cd04601 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
66-123 | 1.79e-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: 40.09 E-value: 1.79e-04
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| CBS_archAMPK_gamma-repeat1 | cd17779 | signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ... |
69-126 | 3.17e-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: 39.91 E-value: 3.17e-04
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| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
55-123 | 6.65e-04 | |||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 39.08 E-value: 6.65e-04
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| PRK07107 | PRK07107 | IMP dehydrogenase; |
54-121 | 1.87e-03 | |||||
IMP dehydrogenase; Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 39.68 E-value: 1.87e-03
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| COG2524 | COG2524 | Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
51-123 | 3.54e-03 | |||||
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 37.94 E-value: 3.54e-03
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| IMPDH | pfam00478 | IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
80-188 | 8.42e-03 | |||||
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: 37.37 E-value: 8.42e-03
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| CBS_arch_repeat2 | cd17778 | CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ... |
68-185 | 8.75e-03 | |||||
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: 35.77 E-value: 8.75e-03
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| COG2905 | COG2905 | Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
55-123 | 8.86e-03 | |||||
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms]; Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 35.58 E-value: 8.86e-03
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