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Conserved domains on  [gi|2496319|sp|P75586|]
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RecName: Full=UPF0053 protein MG146 homolog

Protein Classification

CNNM metal transporter family protein( domain architecture ID 1000124)

CNNM metal transporter family protein containing tandem repeats of the cystathionine beta-synthase (CBS pair) domain and a transporter-associated domain; similar to Homo sapiens metal transporter CNNM2 that is a divalent metal cation transporter

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlyC super family cl34211
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 23-349 7.95e-71

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];


The actual alignment was detected with superfamily member COG1253:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 229.62  E-value: 7.95e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   23 ISAVVSAYETAITSITSYKwsnyVKTHNKQKKLTTKIVNHFQKNYSACLITILVANNIVAILVSNILFLALDQSIKNP-- 100
Cdd:COG1253  16 LNGFFSASEFALVSLRRSR----LEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLlg 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  101 ----------AISSALNLLISGVLLLMLCEITPKTLARINIIRVLVYFAVVVYFFYILFWPITKLASII---------FA 161
Cdd:COG1253  92 slglpaalahTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGStnlllrllgIE 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  162 KYEKAPPVSRRDVYFFIDEIEQNGLFTKEDGQLIKRTLIFDQVLVDQIMIKWNRVVYCYEGDPVKTIKEKFLHGQFSRMP 241
Cdd:COG1253 172 PAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIP 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  242 VLDQTSNEVVGFIHLKDLFSSLEKsNEPFVLQELLYPAVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDI 321
Cdd:COG1253 252 VYEGDLDDIVGVVHVKDLLRALLE-GEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDI 330

                       330       340
                ....*....|....*....|....*....
gi 2496319  322 IEELVGEIYDEHDEVEA-VQTLDNNTWLV 349
Cdd:COG1253 331 LEEIVGEIRDEYDEEEPeIVKLDDGSYLV 359
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 23-349 7.95e-71

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 229.62  E-value: 7.95e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   23 ISAVVSAYETAITSITSYKwsnyVKTHNKQKKLTTKIVNHFQKNYSACLITILVANNIVAILVSNILFLALDQSIKNP-- 100
Cdd:COG1253  16 LNGFFSASEFALVSLRRSR----LEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLlg 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  101 ----------AISSALNLLISGVLLLMLCEITPKTLARINIIRVLVYFAVVVYFFYILFWPITKLASII---------FA 161
Cdd:COG1253  92 slglpaalahTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGStnlllrllgIE 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  162 KYEKAPPVSRRDVYFFIDEIEQNGLFTKEDGQLIKRTLIFDQVLVDQIMIKWNRVVYCYEGDPVKTIKEKFLHGQFSRMP 241
Cdd:COG1253 172 PAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIP 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  242 VLDQTSNEVVGFIHLKDLFSSLEKsNEPFVLQELLYPAVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDI 321
Cdd:COG1253 252 VYEGDLDDIVGVVHVKDLLRALLE-GEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDI 330

                       330       340
                ....*....|....*....|....*....
gi 2496319  322 IEELVGEIYDEHDEVEA-VQTLDNNTWLV 349
Cdd:COG1253 331 LEEIVGEIRDEYDEEEPeIVKLDDGSYLV 359
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 206-323 4.04e-35

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: 126.07  E-value: 4.04e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  206 VDQIMIKWNRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQTSNEVVGFIHLKDLFSSLEKSNEPFVLQELLYPAVLVSNT 285
Cdd:cd04590   2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRALLRPPLFVPET 81

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 2496319  286 TPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIE 323
Cdd:cd04590  82 TPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
157-349 3.52e-21

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 92.95  E-value: 3.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   157 SIIFAKYEKAPPVSRRDVYFFIDEIEQNGLFTKEDGQLIKRTL-IFDQVLVDqIMIKWNRVVYCYEGDPVKTIKEKFLHG 235
Cdd:PRK15094  20 SLLLSQLFHGEPKNRDELLALIRDSEQNDLIDEDTRDMLEGVMdIADQRVRD-IMIPRSQMITLKRNQTLDECLDVIIES 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   236 QFSRMPVLDQTSNEVVGFIHLKDLFSSLEKSNEPFVLQELLYPAVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGI 315
Cdd:PRK15094  99 AHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGL 178

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 2496319   316 VSMEDIIEELVGEIYDEHDEVE--AVQTLDNNTWLV 349
Cdd:PRK15094 179 VTIEDILELIVGEIEDEYDEEDdiDFRQLSRHTWTV 214
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 22-190 1.84e-20

Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal transporter proteins such as cyclin M 1/2 (CNNM). CNNMs are integral membrane proteins that are conserved from bacteria to humans. CNNM family members influence metal ion homeostasis through mechanisms that may not involve direct membrane transport of the ions. Structurally, CNNMs are complex proteins that contain an extracellular N-terminal domain preceding a transmembrane domain, a 'Bateman module', which consists of two cystathionine- beta-synthase (CBS) domains pfam00571, and a C-terminal cNMP (cyclic nucleotide monophosphate) binding domain. This entry describes the CNNM transmembrane domain which contains four hydrophobic regions and forms a dimer through hydrophobic contacts between TM2 and TM3, in which each chain is composed of three transmembrane helices (TM1-3), a pair of short helices exposed on the intracellular side, and a juxtamembrane (JM) helix that forms a belt-like structure. The homodimer adopts an inward-facing conformation with a negatively charged cavity containing a conserved pi-helical turn in TM3 that coordinates a Mg2 ion.


Pssm-ID: 460260  Cd Length: 183  Bit Score: 88.43  E-value: 1.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319     22 CISAVVSAYETAITSITSYKWSNYVKTHNKQkkltTKIVNHFQKNYSACLITILVANNIVAILVSNILFLALDQSIKNP- 100
Cdd:pfam01595   8 LLSAFFSAAETALVSLRRSRLEELAEKGNKG----AKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPLg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319    101 AISSALNLLISGVLLLMLCEITPKTLARINIIRVLVYFAVVVYFFYILFWPITKLASII---------FAKYEKAPPVSR 171
Cdd:pfam01595  84 ALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLanlilrlfgVKGGESEPAVTE 163

                         170
                  ....*....|....*....
gi 2496319    172 RDVYFFIDEIEQNGLFTKE 190
Cdd:pfam01595 164 EELRSLVEESAEEGVIEEE 182
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 23-349 7.95e-71

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 229.62  E-value: 7.95e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   23 ISAVVSAYETAITSITSYKwsnyVKTHNKQKKLTTKIVNHFQKNYSACLITILVANNIVAILVSNILFLALDQSIKNP-- 100
Cdd:COG1253  16 LNGFFSASEFALVSLRRSR----LEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLlg 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  101 ----------AISSALNLLISGVLLLMLCEITPKTLARINIIRVLVYFAVVVYFFYILFWPITKLASII---------FA 161
Cdd:COG1253  92 slglpaalahTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGStnlllrllgIE 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  162 KYEKAPPVSRRDVYFFIDEIEQNGLFTKEDGQLIKRTLIFDQVLVDQIMIKWNRVVYCYEGDPVKTIKEKFLHGQFSRMP 241
Cdd:COG1253 172 PAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIP 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  242 VLDQTSNEVVGFIHLKDLFSSLEKsNEPFVLQELLYPAVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDI 321
Cdd:COG1253 252 VYEGDLDDIVGVVHVKDLLRALLE-GEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDI 330

                       330       340
                ....*....|....*....|....*....
gi 2496319  322 IEELVGEIYDEHDEVEA-VQTLDNNTWLV 349
Cdd:COG1253 331 LEEIVGEIRDEYDEEEPeIVKLDDGSYLV 359
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 22-349 6.53e-49

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: 171.41  E-value: 6.53e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   22 CISAVVSAYETAITSITSYKWSNYVKTHNKQKKLTTKIVNHFQKnysacLI-TILVANNIVAILVSNI---LFLAL--DQ 95
Cdd:COG4536  18 LLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDR-----LIgTILLGNNLVNILASSLatvIAIRLfgDA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   96 SIknpAISSalnlLISGVLLLMLCEITPKTLARINIIRVLVYFAVVVYFFYILFWPITKLASII-------F---AKYEK 165
Cdd:COG4536  93 GV---AIAT----LVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIvrgllrlFgvkPDADA 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  166 APPVSRRDVYFFIDEIEQNGLFTKEDGQLIKRTLIFDQVLVDQIMIKWNRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQ 245
Cdd:COG4536 166 SDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRG 245

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  246 TSNEVVGFIHLKDLFSSLEKSN-EPFVLQELLYPAVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEE 324
Cdd:COG4536 246 DIDNIVGVLHVRDLLRALRKGDlSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILEE 325

                       330       340
                ....*....|....*....|....*.
gi 2496319  325 LVGEIYDEHDEVEA-VQTLDNNTWLV 349
Cdd:COG4536 326 IVGEITDEHDPDAEeIRPQEDGSYLV 351
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 206-323 4.04e-35

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: 126.07  E-value: 4.04e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  206 VDQIMIKWNRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQTSNEVVGFIHLKDLFSSLEKSNEPFVLQELLYPAVLVSNT 285
Cdd:cd04590   2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRALLRPPLFVPET 81

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 2496319  286 TPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIE 323
Cdd:cd04590  82 TPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
157-349 3.52e-21

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 92.95  E-value: 3.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   157 SIIFAKYEKAPPVSRRDVYFFIDEIEQNGLFTKEDGQLIKRTL-IFDQVLVDqIMIKWNRVVYCYEGDPVKTIKEKFLHG 235
Cdd:PRK15094  20 SLLLSQLFHGEPKNRDELLALIRDSEQNDLIDEDTRDMLEGVMdIADQRVRD-IMIPRSQMITLKRNQTLDECLDVIIES 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   236 QFSRMPVLDQTSNEVVGFIHLKDLFSSLEKSNEPFVLQELLYPAVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGI 315
Cdd:PRK15094  99 AHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGL 178

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 2496319   316 VSMEDIIEELVGEIYDEHDEVE--AVQTLDNNTWLV 349
Cdd:PRK15094 179 VTIEDILELIVGEIEDEYDEEDdiDFRQLSRHTWTV 214
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 22-190 1.84e-20

Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal transporter proteins such as cyclin M 1/2 (CNNM). CNNMs are integral membrane proteins that are conserved from bacteria to humans. CNNM family members influence metal ion homeostasis through mechanisms that may not involve direct membrane transport of the ions. Structurally, CNNMs are complex proteins that contain an extracellular N-terminal domain preceding a transmembrane domain, a 'Bateman module', which consists of two cystathionine- beta-synthase (CBS) domains pfam00571, and a C-terminal cNMP (cyclic nucleotide monophosphate) binding domain. This entry describes the CNNM transmembrane domain which contains four hydrophobic regions and forms a dimer through hydrophobic contacts between TM2 and TM3, in which each chain is composed of three transmembrane helices (TM1-3), a pair of short helices exposed on the intracellular side, and a juxtamembrane (JM) helix that forms a belt-like structure. The homodimer adopts an inward-facing conformation with a negatively charged cavity containing a conserved pi-helical turn in TM3 that coordinates a Mg2 ion.


Pssm-ID: 460260  Cd Length: 183  Bit Score: 88.43  E-value: 1.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319     22 CISAVVSAYETAITSITSYKWSNYVKTHNKQkkltTKIVNHFQKNYSACLITILVANNIVAILVSNILFLALDQSIKNP- 100
Cdd:pfam01595   8 LLSAFFSAAETALVSLRRSRLEELAEKGNKG----AKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPLg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319    101 AISSALNLLISGVLLLMLCEITPKTLARINIIRVLVYFAVVVYFFYILFWPITKLASII---------FAKYEKAPPVSR 171
Cdd:pfam01595  84 ALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLanlilrlfgVKGGESEPAVTE 163

                         170
                  ....*....|....*....
gi 2496319    172 RDVYFFIDEIEQNGLFTKE 190
Cdd:pfam01595 164 EELRSLVEESAEEGVIEEE 182
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
205-332 1.01e-11

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 62.19  E-value: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  205 LVDQIMIKwnRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQtSNEVVGFIHLKDLFSSLEKSNEPFVLQELLY------- 277
Cdd:COG3448   3 TVRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDE-DGRLVGIVTERDLLRALLPDRLDELEERLLDlpvedvm 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2496319  278 --PAVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEELVGEIYDE 332
Cdd:COG3448  80 trPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
193-325 4.44e-10

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 59.13  E-value: 4.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  193 QLIKRTLIFDQVLVDQIMIKwnRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQtsNEVVGFIHLKDLFSSLEKSNEPFVL 272
Cdd:COG2524  75 VAEKELGLVLKMKVKDIMTK--DVITVSPDTTLEEALELMLEKGISGLPVVDD--GKLVGIITERDLLKALAEGRDLLDA 150

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 2496319  273 Q--ELLYPAVL-VSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEEL 325
Cdd:COG2524 151 PvsDIMTRDVVtVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
202-325 9.35e-10

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 56.46  E-value: 9.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  202 DQVLVDQIMIKwNRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDqTSNEVVGFIHLKDLFSSLEKsnepFVLQELLY-PAV 280
Cdd:COG4109  14 EILLVEDIMTL-EDVATLSEDDTVEDALELLEKTGHSRFPVVD-ENGRLVGIVTSKDILGKDDD----TPIEDVMTkNPI 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 2496319  281 LVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEEL 325
Cdd:COG4109  88 TVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKAL 132
CBS COG0517
CBS domain [Signal transduction mechanisms];
204-328 9.77e-09

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 53.33  E-value: 9.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  204 VLVDQIMIKwnRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQtSNEVVGFIHLKDLFSSLEKSNEPFV---LQELLY-PA 279
Cdd:COG0517   1 MKVKDIMTT--DVVTVSPDATVREALELMSEKRIGGLPVVDE-DGKLVGIVTDRDLRRALAAEGKDLLdtpVSEVMTrPP 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 2496319  280 VLVSNTTPIKQALRQMRLHRA-HLAVVqDKHHHTIGIVSMEDIIEELVGE 328
Cdd:COG0517  78 VTVSPDTSLEEAAELMEEHKIrRLPVV-DDDGRLVGIITIKDLLKALLEP 126
PRK11573 PRK11573
hypothetical protein; Provisional
 23-328 1.41e-08

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 56.30  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319    23 ISAVVSAYETAITSITSYKWSNYVKTHNKQKKLTTKIVNHFQKnysacLIT-ILVANNIVAILVSNILFLALDQSIKNPA 101
Cdd:PRK11573   4 ISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDR-----LISlVLIGNNLVNILASALGTIVGMRLYGDAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   102 ISSALNLLIsgVLLLMLCEITPKTLARINIIRVL----VYFAVVVYFFYILFWPITKLASIIFAKYEKAPPVSRRDVyFF 177
Cdd:PRK11573  79 VAIATGVLT--FVVLVFAEVLPKTIAALYPEKVAypssFLLAPLQILMMPLVWLLNTITRLLMRLMGIKTDIVVSGA-LS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319   178 IDEI-----EQNGLFTKEDGQLIKRTLIFDQVLVDQIMIKWNRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQTSNEVVG 252
Cdd:PRK11573 156 KEELrtivhESRSQISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAIS 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2496319   253 FIHLKDLFSSLEKSNEpFVLQELLYPA---VLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEELVGE 328
Cdd:PRK11573 236 MLRVREAYRLMTEKKE-FTKENMLRAAdeiYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGD 313
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 216-322 5.20e-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: 50.71  E-value: 5.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  216 VVYCYEGDPVKTIKEKFLHGQFSRMPVLDqTSNEVVGFIHLKDLFSSLEKSNEPFVLQ--ELLYPAVL-VSNTTPIKQAL 292
Cdd:cd02205   4 VVTVDPDTTVREALELMAENGIGALPVVD-DDGKLVGIVTERDILRALVEGGLALDTPvaEVMTPDVItVSPDTDLEEAL 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 2496319  293 RQMRLHRA-HLAVVqDKHHHTIGIVSMEDII 322
Cdd:cd02205  83 ELMLEHGIrRLPVV-DDDGKLVGIVTRRDIL 112
CBS COG0517
CBS domain [Signal transduction mechanisms];
185-268 2.00e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 49.48  E-value: 2.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  185 GLFTKED--GQLIKRTLIFDQVLVDQIMIKwnRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQtSNEVVGFIHLKDLFSS 262
Cdd:COG0517  46 GIVTDRDlrRALAAEGKDLLDTPVSEVMTR--PPVTVSPDTSLEEAAELMEEHKIRRLPVVDD-DGRLVGIITIKDLLKA 122


                ....*.
gi 2496319  263 LEKSNE 268
Cdd:COG0517 123 LLEPLA 128
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 185-263 1.72e-06

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 46.75  E-value: 1.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  185 GLFTKED--GQLIKRTLIFDQVLVDQIMIKwnRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQtsNEVVGFIHLKDLFSS 262
Cdd:COG2905  44 GIITDRDlrRRVLAEGLDPLDTPVSEVMTR--PPITVSPDDSLAEALELMEEHRIRHLPVVDD--GKLVGIVSITDLLRA 119


                .
gi 2496319  263 L 263
Cdd:COG2905 120 L 120
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 277-333 4.21e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in proteobacteria; 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: 341398 [Multi-domain]  Cd Length: 133  Bit Score: 46.02  E-value: 4.21e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2496319  277 YPAVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEELVGEIYDEH 333
Cdd:cd04640   5 VPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGEKPLKIVQER 61
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 206-265 1.13e-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: 42.59  E-value: 1.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319    206 VDQIMIKwnRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQtSNEVVGFIHLKDLFSSLEK 265
Cdd:pfam00571   1 VKDIMTK--DVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRALLG 57
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 278-339 1.31e-05

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: 44.16  E-value: 1.31e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496319  278 PAVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEELVGEIYDEHDEVEAV 339
Cdd:cd02205   3 DVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEV 64
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 206-325 2.28e-05

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 43.66  E-value: 2.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  206 VDQIMIKwnRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDQtSNEVVGFIHLKDLFSSLEKSNEPFV---LQELL-YPAVL 281
Cdd:COG2905   1 VKDIMSR--DVVTVSPDATVREAARLMTEKGVGSLVVVDD-DGRLVGIITDRDLRRRVLAEGLDPLdtpVSEVMtRPPIT 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 2496319  282 VSNTTPIKQALRQMRLHRA-HLAVVQDKhhHTIGIVSMEDIIEEL 325
Cdd:COG2905  78 VSPDDSLAEALELMEEHRIrHLPVVDDG--KLVGIVSITDLLRAL 120
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 278-327 3.87e-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: 41.04  E-value: 3.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2496319    278 PAVLVSNTTPIKQALRQMRLHR-AHLAVVqDKHHHTIGIVSMEDIIEELVG 327
Cdd:pfam00571   8 DVVTVSPDTTLEEALELMREHGiSRLPVV-DEDGKLVGIVTLKDLLRALLG 57
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04589
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 276-341 7.04e-05

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: 341365 [Multi-domain]  Cd Length: 113  Bit Score: 41.79  E-value: 7.04e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2496319  276 LYPAVLVSNTTPIKQALRQMRLHRAHLAVVQDkHHHTIGIVSMEDIIEELVGEIYDEHDEVEAVQT 341
Cdd:cd04589   2 LHPPLFVDAETSIREATRLMKENGADSLLVRD-GDGRVGIVTRTDLRDAVVLDGQPVDTPVGEIAT 66
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 185-260 7.60e-05

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: 41.85  E-value: 7.60e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496319  185 GLFTKED-GQLIKRTLIFDQVLVDQIMIKwnRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDqTSNEVVGFIHLKDLF 260
Cdd:cd02205  39 GIVTERDiLRALVEGGLALDTPVAEVMTP--DVITVSPDTDLEEALELMLEHGIRRLPVVD-DDGKLVGIVTRRDIL 112
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 278-341 9.50e-05

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 41.74  E-value: 9.50e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2496319  278 PAVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEELVGEIYDEHDE-VEAVQT 341
Cdd:COG2905   8 DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMT 72
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
280-342 2.17e-04

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 41.00  E-value: 2.17e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2496319  280 VLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEELVGEIYDEHDEVEAVQTL 342
Cdd:COG3448  13 VTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDLPV 75
CBS COG0517
CBS domain [Signal transduction mechanisms];
280-334 3.45e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 40.23  E-value: 3.45e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 2496319  280 VLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEELVGEIYDEHD 334
Cdd:COG0517  12 VTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLD 66
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 ...
 279-343 5.74e-04

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: 39.22  E-value: 5.74e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2496319  279 AVLVSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDIIEELVGEIYDEHDEVEAVQTLD 343
Cdd:cd17771   6 PVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQIDLDAPISEVMTPD 70
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 206-322 1.14e-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: 38.85  E-value: 1.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496319  206 VDQIMIKwnRVVYCYEGDPVKTIKEKFLHGQFSRMPVLDqtSNEVVGFIHLKDL---FSSLEKSNEPF----------VL 272
Cdd:cd17778   2 VKEFMTT--PVVTIYPDDTLKEAMELMVTRGFRRLPVVS--GGKLVGIVTAMDIvkyFGSHEAKKRLTtgdideaystPV 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 2496319  273 QELLYPAVL-VSNTTPIKQALRQMRLHRAHLAVVQDKHHHTIGIVSMEDII 322
Cdd:cd17778  78 EEIMSKEVVtIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 280-322 5.93e-03

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: 36.77  E-value: 5.93e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 2496319  280 VLVSNTTPIKQALRQMRLHRAH-LAVVqDKHHHTIGIVSMEDII 322
Cdd:cd04600   6 VTVTPDTSLEEAWRLLRRHRIKaLPVV-DRARRLVGIVTLADLL 48
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 278-325 6.16e-03

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: 36.37  E-value: 6.16e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 2496319  278 PAVLVSNTTPIKQALRQMRLHRA-HLAVVqDKHHHTIGIVSMEDIIEEL 325
Cdd:cd17775  70 DLITAREDDGLFEALERMREKGVrRLPVV-DDDGELVGIVTLDDILELL 117
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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