NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1840277627|ref|XP_012995128|]
View 

5'-AMP-activated protein kinase subunit gamma-2 isoform X1 [Esox lucius]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 254-391 2.50e-86

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1; AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. 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: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 271.35  E-value: 2.50e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 254 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWETKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 333
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1840277627 334 WRELYLQETFKPLVNITPDASIFDAVYSLIKNKIHRLPVIDPVSGNALYILTHKRILK 391
Cdd:cd04618    81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 417-540 1.80e-76

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. 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: 341399 [Multi-domain]  Cd Length: 124  Bit Score: 244.73  E-value: 1.80e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 417 TYHDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALRHRSQYFEGVMKC 496
Cdd:cd04641     1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1840277627 497 NRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQALV 540
Cdd:cd04641    81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
PspC_subgroup_2 super family cl41463
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 551-851 2.85e-17

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


The actual alignment was detected with superfamily member NF033839:

Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 86.36  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 551 SQPQPPPEAQTSPEALVEAEPEANTEVVVV---EAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTE 627
Cdd:NF033839  179 TKPSPQPEGKKPSVPDINQEKEKAKLAVATymsKILDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIE 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 628 AEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKD-EAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSE 706
Cdd:NF033839  259 NTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKpSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEK 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 707 TEAEVmKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEA 786
Cdd:NF033839  339 PKPEV-KPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPK 417

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1840277627 787 EGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETeaEKPEAETEAEGLNSEAETEAE 851
Cdd:NF033839  418 PEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPET--PKPEVKPQPEKPKPEVKPQPE 480
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 16-215 6.78e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 6.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627   16 PRKNRMLRLNMPDLSSFAMPFLEGDASHVNKDNIPKGDGSCQSASPTKGFFSR-GPFSRPSSPKSA----PARTRNSPSS 90
Cdd:PHA03307   207 PRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRpAPITLPTRIWEAsgwnGPSSRPGPAS 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627   91 PKTifPYPSSHQDSPPKSPRRLSFSGIFRSSSRESKDSTSNSTSPVSIKLFSRARKAS-----------GVSSPPLTPPT 159
Cdd:PHA03307   287 SSS--SPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSpgpspsrspspSRPPPPADPSS 364

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1840277627  160 QVAKQPPAFLLEAYRIEPERPETRMRSYS-SPPDTGQHL--RLPCAKPATTPSAPIATS 215
Cdd:PHA03307   365 PRKRPRPSRAPSSPAASAGRPTRRRARAAvAGRARRRDAtgRFPAGRPRPSPLDAGAAS 423
 
Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 254-391 2.50e-86

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1; AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. 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: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 271.35  E-value: 2.50e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 254 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWETKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 333
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1840277627 334 WRELYLQETFKPLVNITPDASIFDAVYSLIKNKIHRLPVIDPVSGNALYILTHKRILK 391
Cdd:cd04618    81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 417-540 1.80e-76

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. 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: 341399 [Multi-domain]  Cd Length: 124  Bit Score: 244.73  E-value: 1.80e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 417 TYHDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALRHRSQYFEGVMKC 496
Cdd:cd04641     1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1840277627 497 NRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQALV 540
Cdd:cd04641    81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS COG0517
CBS domain [Signal transduction mechanisms];
420-540 3.63e-22

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 92.62  E-value: 3.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 420 DIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALRHrsqyfeGVMKCNRH 499
Cdd:COG0517    10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1840277627 500 ETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQALV 540
Cdd:COG0517    84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
344-469 7.68e-19

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 83.76  E-value: 7.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDP---VSGnalyILTHKRILKFLqlfvcEMPKPAFMKQNLEELTIGTY-- 418
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEdgrLVG----IVTERDLLRAL-----LPDRLDELEERLLDLPVEDVmt 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAE 469
Cdd:COG3448    81 RPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 551-851 2.85e-17

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 86.36  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 551 SQPQPPPEAQTSPEALVEAEPEANTEVVVV---EAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTE 627
Cdd:NF033839  179 TKPSPQPEGKKPSVPDINQEKEKAKLAVATymsKILDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIE 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 628 AEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKD-EAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSE 706
Cdd:NF033839  259 NTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKpSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEK 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 707 TEAEVmKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEA 786
Cdd:NF033839  339 PKPEV-KPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPK 417

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1840277627 787 EGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETeaEKPEAETEAEGLNSEAETEAE 851
Cdd:NF033839  418 PEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPET--PKPEVKPQPEKPKPEVKPQPE 480
growth_prot_Scy NF041483
polarized growth protein Scy;
587-850 4.09e-16

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 83.34  E-value: 4.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  587 ETEEHVAEPATTVEGIV---EADVEE-GTPEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAE--AEGMKD 660
Cdd:NF041483   470 EAVQQIEEAARTAEELLtkaKADADElRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEeqAEEVRA 549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  661 EAE--AEGMKDEAE--VEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVETDGMKP 736
Cdd:NF041483   550 AAEraARELREETEraIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQA 629

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  737 EAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPE-------AETEAE 809
Cdd:NF041483   630 QAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEaaealaaAQEEAA 709

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1840277627  810 GVKPEAETEAEGVKPEGETEAEKP----------------EAETEAEGLNSEAETEA 850
Cdd:NF041483   710 RRRREAEETLGSARAEADQERERAreqseellasarkrveEAQAEAQRLVEEADRRA 766
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 581-836 1.01e-15

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 81.35  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 581 EAFPDTETEEHVAEPATTVEGIVEADVEEGTPEEtaaEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKD 660
Cdd:NF033839  243 QALSEIDNVNTKVEIENTVHKIFADMDAVVTKFK---KGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKP 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 661 EaeaegMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGmKSETEAEVMKFEAETEAEGMKSETEVETDGMKPEAEA 740
Cdd:NF033839  320 E-----VKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKP-QPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEK 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 741 EAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAE 820
Cdd:NF033839  394 PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKP 473

                         250
                  ....*....|....*....
gi 1840277627 821 GVKPEGET---EAEKPEAE 836
Cdd:NF033839  474 EVKPQPEKpkpDNSKPQAD 492
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 569-853 1.09e-15

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 81.97  E-value: 1.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  569 AEPEANTEVVVVEAFPDTETEEHVAEpattvEGIVEADVEEGTpeETAAEGmKSEAVTEAEvMKDEAEAEGmkdEAEAEG 648
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGENGE-----ESGGEAEQEGET--ETKGEN-ESEGEIPAE-RKGEQEGEG---EIEAKE 703

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  649 MKDEAEAEGMKDEA----EAEGMKDEAEVEGmKDEAEAEGMKDEAEAEGmKDEAEAEGMKSETEaevmkFEAETEAEGMK 724
Cdd:TIGR00927  704 ADHKGETEAEEVEHegetEAEGTEDEGEIET-GEEGEEVEDEGEGEAEG-KHEVETEGDRKETE-----HEGETEAEGKE 776

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  725 SETEVETDGmkpeaeAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEgvkpEAETEAEgVKPEA 804
Cdd:TIGR00927  777 DEDEGEIQA------GEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG----EQELNAE-NQGEA 845

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1840277627  805 ETEAEGVkpEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAEVE 853
Cdd:TIGR00927  846 KQDEKGV--DGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 641-837 2.28e-15

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 80.20  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 641 KDEAEAEGMKDEAEAEGMKDEAEAEGMKDEaevegMKDEAEAEGMKDEAEAEGMKDEAEAEgmkSETEAEVMKFEAETEA 720
Cdd:NF033839  291 KPSAPKPGMQPSPQPEKKEVKPEPETPKPE-----VKPQLEKPKPEVKPQPEKPKPEVKPQ---LETPKPEVKPQPEKPK 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 721 EGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGV 800
Cdd:NF033839  363 PEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEV 442

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1840277627 801 KPEAETEAEGVKPEAETEAEGVKPEGETE--AEKPEAET 837
Cdd:NF033839  443 KPQPEKPKPEVKPQPETPKPEVKPQPEKPkpEVKPQPEK 481
growth_prot_Scy NF041483
polarized growth protein Scy;
572-851 1.18e-14

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 78.71  E-value: 1.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  572 EANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEgtpeetaAEGMKSEAVTEAEVMKDEA---------EAEGMKD 642
Cdd:NF041483   921 EATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQ-------AEQLIAEATGEAERLRAEAaetvgsaqqHAERIRT 993

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  643 EAEAEGMKDEAEAEGMKDEA--EAEGMKDEAEVEGMKDEAEAEGMKDE------AEAEGMKDEAEAEGMKSETEAE---- 710
Cdd:NF041483   994 EAERVKAEAAAEAERLRTEAreEADRTLDEARKDANKRRSEAAEQADTliteaaAEADQLTAKAQEEALRTTTEAEaqad 1073

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  711 VMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEM-----KSETEVK--TDGMKPEAENETEEMKPEAETE-AEGVKPEA 782
Cdd:NF041483  1074 TMVGAARKEAERIVAEATVEGNSLVEKARTDADELlvgarRDATAIRerAEELRDRITGEIEELHERARREsAEQMKSAG 1153

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1840277627  783 E------TEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETeaEKPEAETEAEGLNSEAETEAE 851
Cdd:NF041483  1154 ErcdalvKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQ--KKAELVREAEKIKAEAEAEAK 1226
growth_prot_Scy NF041483
polarized growth protein Scy;
558-851 3.42e-14

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 77.17  E-value: 3.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  558 EAQTSPEALVEAEPEANTEVVvveafpdTETEEHVAEPATTVEGIVEADVEEGT----PEETAAEGMKSEAVTEAEVMKD 633
Cdd:NF041483   750 EAQAEAQRLVEEADRRATELV-------SAAEQTAQQVRDSVAGLQEQAEEEIAglrsAAEHAAERTRTEAQEEADRVRS 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  634 EAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEvegmkdeaeaegmkdeAEAEGMKDEAEAEGMKSETEAEVMK 713
Cdd:NF041483   823 DAYAERERASEDANRLRREAQEETEAAKALAERTVSEAI----------------AEAERLRSDASEYAQRVRTEASDTL 886

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  714 FEAETEAEgmKSETEVETDGMKpeaeaeaeeMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEA 793
Cdd:NF041483   887 ASAEQDAA--RTRADAREDANR---------IRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADA 955

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1840277627  794 ETEAEGVKPEAETEAEGVKPEA-ET----EAEGVKPEGETEAEKPEAETEAEGLNSEAETEAE 851
Cdd:NF041483   956 AAQAEQLIAEATGEAERLRAEAaETvgsaQQHAERIRTEAERVKAEAAAEAERLRTEAREEAD 1018
PTZ00121 PTZ00121
MAEBL; Provisional
 548-857 2.27e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.79  E-value: 2.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  548 RKSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTE 627
Cdd:PTZ00121  1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  628 AEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEvegmkdEAEAEGMKDEAEAEgmKDEAEAEGMKSET 707
Cdd:PTZ00121  1304 ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA------KAEAEAAADEAEAA--EEKAEAAEKKKEE 1375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  708 E---AEVMKFEAET--EAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKtdgmKPEAENETEEMKPEAET--EAEGVKP 780
Cdd:PTZ00121  1376 AkkkADAAKKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK----KAEEKKKADEAKKKAEEakKADEAKK 1451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  781 EAET--EAEGVKPEAET--EAEGVKPEAET-----EAEGVKPEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAE 851
Cdd:PTZ00121  1452 KAEEakKAEEAKKKAEEakKADEAKKKAEEakkadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531


                   ....*.
gi 1840277627  852 VEFKAD 857
Cdd:PTZ00121  1532 EAKKAD 1537
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 544-853 8.27e-13

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 72.11  E-value: 8.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 544 AGINRKSSQPQP---PPEAQTSPEALVEAEPEANTEVVVVeafPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGM 620
Cdd:NF033839  153 SGSSTKPETPQPenpEHQKPTTPAPDTKPSPQPEGKKPSV---PDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQ 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 621 KSEAVTEAEVMKDEAEAEgmkdeAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKD-EAEAEGMKDEAE 699
Cdd:NF033839  230 IVALIKELDELKKQALSE-----IDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKpSAPKPGMQPSPQ 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 700 AEGMKSETEAEVMKFEAETEAEGMKSETEVETDGMKPEaeaeaeemksetevktdgMKPEAENETEEMKPEAETEAEGVK 779
Cdd:NF033839  305 PEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPE------------------VKPQLETPKPEVKPQPEKPKPEVK 366

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840277627 780 PEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEaegvKPEGETEAEKPEAETEAEGLNSEAETEAEVE 853
Cdd:NF033839  367 PQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKP----KPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE 436
growth_prot_Scy NF041483
polarized growth protein Scy;
617-820 4.13e-12

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 70.24  E-value: 4.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  617 AEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEgmkdeAEAEGMKDEAEAEGMKDEAE----VEGMKDEAEAEGMKDEAEAE 692
Cdd:NF041483   904 ANRIRSDAAAQADRLIGEATSEAERLTAEAR-----AEAERLRDEARAEAERVRADaaaqAEQLIAEATGEAERLRAEAA 978

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  693 GMKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAE 772
Cdd:NF041483   979 ETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQ 1058

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1840277627  773 TEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAE 820
Cdd:NF041483  1059 EEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTDAD 1106
growth_prot_Scy NF041483
polarized growth protein Scy;
614-840 5.16e-12

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 70.24  E-value: 5.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  614 ETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAegmKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKD------ 687
Cdd:NF041483  1003 AAEAERLRTEAREEADRTLDEARKDANKRRSEA---AEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADtmvgaa 1079

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  688 EAEAEGMKDEAEAEG----MKSETEAEVMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSET--EVKTDGMKPEA- 760
Cdd:NF041483  1080 RKEAERIVAEATVEGnslvEKARTDADELLVGARRDATAIRERAEELRDRITGEIEELHERARRESaeQMKSAGERCDAl 1159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  761 ENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEaegvKPEAETEAEGVKPEGETEAEKPEAETEAE 840
Cdd:NF041483  1160 VKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQK----KAELVREAEKIKAEAEAEAKRTVEEGKRE 1235
growth_prot_Scy NF041483
polarized growth protein Scy;
586-851 5.66e-12

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 69.85  E-value: 5.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  586 TETEEHVAEPATTVEGIVEADVEEG---TPEETAAEGMKseAVTEAEVMKDEAEaegmkDEAEAEGMKDEAEAEGMKDEA 662
Cdd:NF041483   330 AEAEQALADARAEAEKLVAEAAEKArtvAAEDTAAQLAK--AARTAEEVLTKAS-----EDAKATTRAAAEEAERIRREA 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  663 EAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVETDGMKPEAEAEA 742
Cdd:NF041483   403 EAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTA 482

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  743 EEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAE-------TEAEGVKPEAETEAEGVKPEAETEAEGVKPEA 815
Cdd:NF041483   483 EELLTKAKADADELRSTATAESERVRTEAIERATTLRRQAEetlertrAEAERLRAEAEEQAEEVRAAAERAARELREET 562

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1840277627  816 ETEAEGVKPEGETEAEKPEAETE-----AEGLNSEAETEAE 851
Cdd:NF041483   563 ERAIAARQAEAAEELTRLHTEAEerltaAEEALADARAEAE 603
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
663-846 5.30e-11

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 65.66  E-value: 5.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 663 EAEGMKDEAEV--EGMKDEAEAEGMKDEAEAEGMKDEAEAEgMKSETEAEVMKF-EAETEAEGMKSETEVETDgmkpeae 739
Cdd:COG2268   187 DALGRRKIAEIirDARIAEAEAERETEIAIAQANREAEEAE-LEQEREIETARIaEAEAELAKKKAEERREAE------- 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 740 aeaeemksETEVKTDGMKPEAENETEEmkpEAETEAEGVKPEAETE---AEGVKPEAETEAEGVKPeAETEAEGVKPEAE 816
Cdd:COG2268   259 --------TARAEAEAAYEIAEANAER---EVQRQLEIAEREREIElqeKEAEREEAELEADVRKP-AEAEKQAAEAEAE 326

                         170       180       190
                  ....*....|....*....|....*....|
gi 1840277627 817 TEAEGVKPEGETEAEKPEAETEAEGLNSEA 846
Cdd:COG2268   327 AEAEAIRAKGLAEAEGKRALAEAWNKLGDA 356
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 420-468 1.78e-10

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: 56.75  E-value: 1.78e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1840277627  420 DIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAA 468
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
growth_prot_Scy NF041483
polarized growth protein Scy;
560-851 2.68e-10

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 64.46  E-value: 2.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  560 QTSPEALVEAEPEAntEVVVVEAfpdtetEEHVAEPATTVEGIVEADVEegTPEETAAEgMKSEAVTEAEVMKdeaeaeg 639
Cdd:NF041483   268 QEAEEALREARAEA--EKVVAEA------KEAAAKQLASAESANEQRTR--TAKEEIAR-LVGEATKEAEALK------- 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  640 mkdeAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEgmkdEAEAEGMKDEAEAEGM----KDEAEAEGMKSETEAEVMKFE 715
Cdd:NF041483   330 ----AEAEQALADARAEAEKLVAEAAEKARTVAAE----DTAAQLAKAARTAEEVltkaSEDAKATTRAAAEEAERIRRE 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  716 AETEAEGMKSETEVETDGMKPEAEAEAEemksETEVKTDGMKPEA---ENETEEMKPEAETEAEGVKPEAETEAEGVKPE 792
Cdd:NF041483   402 AEAEADRLRGEAADQAEQLKGAAKDDTK----EYRAKTVELQEEArrlRGEAEQLRAEAVAEGERIRGEARREAVQQIEE 477

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1840277627  793 AETEAEGVKPEAETEAEGVKPEAETEAEGVKPE--------------------GETEAEKPEAETEAEGLNSEAETEAE 851
Cdd:NF041483   478 AARTAEELLTKAKADADELRSTATAESERVRTEaierattlrrqaeetlertrAEAERLRAEAEEQAEEVRAAAERAAR 556
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 419-469 1.19e-08

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: 51.83  E-value: 1.19e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAE 469
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 345-394 1.37e-07

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: 48.66  E-value: 1.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1840277627  345 PLVNITPDASIFDAVYSLIKNKIHRLPVIDPVsGNALYILTHKRILKFLQ 394
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIKALA 49
growth_prot_Scy NF041483
polarized growth protein Scy;
613-850 1.01e-06

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 52.91  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  613 EETAAEGMKS--EAVTEAEVMKDEA------EAEGMKDEAEAEGMKDEAEAEGM-----------KDEAE---------- 663
Cdd:NF041483   170 DESRAEAEQAlaAARAEAERLAEEArqrlgsEAESARAEAEAILRRARKDAERLlnaastqaqeaTDHAEqlrsstaaes 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  664 -------------AEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSE----TEAEVMKF--EAETEAEGMK 724
Cdd:NF041483   250 dqarrqaaelsraAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQrtrtAKEEIARLvgEATKEAEALK 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  725 SETE-------VETDGMKPEAEAEAEEMKSEtevKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEA 797
Cdd:NF041483   330 AEAEqaladarAEAEKLVAEAAEKARTVAAE---DTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEA 406

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1840277627  798 EGVKPEAETEAEGVKPEA------------ETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEA 850
Cdd:NF041483   407 DRLRGEAADQAEQLKGAAkddtkeyraktvELQEEARRLRGEAEQLRAEAVAEGERIRGEARREA 471
growth_prot_Scy NF041483
polarized growth protein Scy;
627-850 4.23e-06

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 50.98  E-value: 4.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  627 EAEVMKDEAEAEGMK--DEAEAEGMKDEAEAEGMKD----EAEAEGMKDEAEvegMKDEAEAEGMKDEAEAEGMKDEAEA 700
Cdd:NF041483   144 ESHVNENVAWAEQLRarTESQARRLLDESRAEAEQAlaaaRAEAERLAEEAR---QRLGSEAESARAEAEAILRRARKDA 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  701 EGMKseTEAEVMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEvktdgmkpeaenETEEMKPEAETEAEGVKP 780
Cdd:NF041483   221 ERLL--NAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ------------EAEEALREARAEAEKVVA 286

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  781 EAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEkpEAETEAEGLNSEAETEA 850
Cdd:NF041483   287 EAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALA--DARAEAEKLVAEAAEKA 354
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 344-393 2.15e-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: 2.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFL 393
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRAL 55
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 16-215 6.78e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 6.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627   16 PRKNRMLRLNMPDLSSFAMPFLEGDASHVNKDNIPKGDGSCQSASPTKGFFSR-GPFSRPSSPKSA----PARTRNSPSS 90
Cdd:PHA03307   207 PRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRpAPITLPTRIWEAsgwnGPSSRPGPAS 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627   91 PKTifPYPSSHQDSPPKSPRRLSFSGIFRSSSRESKDSTSNSTSPVSIKLFSRARKAS-----------GVSSPPLTPPT 159
Cdd:PHA03307   287 SSS--SPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSpgpspsrspspSRPPPPADPSS 364

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1840277627  160 QVAKQPPAFLLEAYRIEPERPETRMRSYS-SPPDTGQHL--RLPCAKPATTPSAPIATS 215
Cdd:PHA03307   365 PRKRPRPSRAPSSPAASAGRPTRRRARAAvAGRARRRDAtgRFPAGRPRPSPLDAGAAS 423
Med26_M pfam15694
Mediator complex subunit 26 middle domain; Med26_M is the middle domain of subunit 26 of ...
 72-243 1.29e-04

Mediator complex subunit 26 middle domain; Med26_M is the middle domain of subunit 26 of Mediator. Med19 and Med26 act synergistically to mediate the interaction between REST (a Kruppel-type zinc finger transcription factor that binds to a 21-bp RE1 silencing element present in over 900 human genes) and Mediator.


Pssm-ID: 464807 [Multi-domain]  Cd Length: 255  Bit Score: 44.48  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  72 SRPSSPksAPARTRNSPSSPKTIFPYPSSHQDS-----PPKSPRRLSFS------GIF--RSSSRESKDSTSnstSPVSI 138
Cdd:pfam15694  51 PHTSSP--GLGKPPSTSSLLKAAVLQQQARLDEtggppQPKSPRCSSFSprnsrhETFarRSSTYAPKGSVP---SPSPR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 139 KLFSRARKASGVSSP-PLTPPTQVAK--QPPAFLLEAYRIEPERPETrmRSYSSPPDTGQHLRLPCAKP-ATTPSAPIAT 214
Cdd:pfam15694 126 SQVLDAQVPSPLPLSqPSTPPVQAKRleKPPQSSPESSQHWLEQSDS--ESHQRHQDGSATLLSQSVSPgCKTPLHPGEN 203

                         170       180
                  ....*....|....*....|....*....
gi 1840277627 215 SRSRTVhglTEGMLEKLDLEDEAVEESES 243
Cdd:pfam15694 204 SLPHLG---FSPDSSKADSDGAASSGSDS 229
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 641-840 7.02e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.00  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 641 KDEAEAEGMKDEAE--AEGMKDEAE---AEGMKDEAEVEgmkdEAEAEGMKDEAEAEGMKDEAEaegmKSETEAEVMKFE 715
Cdd:NF033838  304 KKVAEAEKKVEEAKkkAKDQKEEDRrnyPTNTYKTLELE----IAESDVKVKEAELELVKEEAK----EPRNEEKIKQAK 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 716 AETEAEgmKSE-TEVEtdgmkpeaeaeaeemksetEVKTDGMKP--EAENETEEMKPEAETEAEGVKPEAETEAEGVKPE 792
Cdd:NF033838  376 AKVESK--KAEaTRLE-------------------KIKTDRKKAeeEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPK 434

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1840277627 793 AETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKPEAETEAE 840
Cdd:NF033838  435 PEKPAEQPKAEKPADQQAEEDYARRSEEEYNRLTQQQPPKTEKPAQPS 482
 
Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 254-391 2.50e-86

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1; AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. 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: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 271.35  E-value: 2.50e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 254 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWETKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 333
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1840277627 334 WRELYLQETFKPLVNITPDASIFDAVYSLIKNKIHRLPVIDPVSGNALYILTHKRILK 391
Cdd:cd04618    81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 417-540 1.80e-76

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. 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: 341399 [Multi-domain]  Cd Length: 124  Bit Score: 244.73  E-value: 1.80e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 417 TYHDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALRHRSQYFEGVMKC 496
Cdd:cd04641     1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1840277627 497 NRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQALV 540
Cdd:cd04641    81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 419-537 2.59e-22

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: 92.69  E-value: 2.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKtYNNLDITVTQALRhrsqyfEGVMKCNR 498
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG-GLALDTPVAEVMT------PDVITVSP 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1840277627 499 HETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQ 537
Cdd:cd02205    75 DTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
420-540 3.63e-22

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 92.62  E-value: 3.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 420 DIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALRHrsqyfeGVMKCNRH 499
Cdd:COG0517    10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1840277627 500 ETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQALV 540
Cdd:COG0517    84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
419-540 1.72e-21

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 91.08  E-value: 1.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNL-----DITVTQALRHRsqyfegV 493
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELeerllDLPVEDVMTRP------V 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1840277627 494 MKCNRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQALV 540
Cdd:COG3448    84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
344-469 7.68e-19

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 83.76  E-value: 7.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDP---VSGnalyILTHKRILKFLqlfvcEMPKPAFMKQNLEELTIGTY-- 418
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEdgrLVG----IVTERDLLRAL-----LPDRLDELEERLLDLPVEDVmt 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAE 469
Cdd:COG3448    81 RPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
419-539 5.14e-18

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 83.39  E-value: 5.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVINLAAEKTYNnLDITVTQALRhrsqyfEGVMKCNR 498
Cdd:COG2524    94 KDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDL-LDAPVSDIMT------RDVVTVSE 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1840277627 499 HETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQAL 539
Cdd:COG2524   166 DDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 551-851 2.85e-17

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 86.36  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 551 SQPQPPPEAQTSPEALVEAEPEANTEVVVV---EAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTE 627
Cdd:NF033839  179 TKPSPQPEGKKPSVPDINQEKEKAKLAVATymsKILDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIE 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 628 AEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKD-EAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSE 706
Cdd:NF033839  259 NTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKpSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEK 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 707 TEAEVmKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEA 786
Cdd:NF033839  339 PKPEV-KPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPK 417

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1840277627 787 EGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETeaEKPEAETEAEGLNSEAETEAE 851
Cdd:NF033839  418 PEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPET--PKPEVKPQPEKPKPEVKPQPE 480
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 419-539 4.00e-17

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 78.33  E-value: 4.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALRHRsqyfegVMKCNR 498
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRP------PITVSP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1840277627 499 HETLETIVDRIVKAEVHRLVVVDENaRIVGIVSLSDILQAL 539
Cdd:COG2905    81 DDSLAEALELMEEHRIRHLPVVDDG-KLVGIVSITDLLRAL 120
growth_prot_Scy NF041483
polarized growth protein Scy;
587-850 4.09e-16

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 83.34  E-value: 4.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  587 ETEEHVAEPATTVEGIV---EADVEE-GTPEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAE--AEGMKD 660
Cdd:NF041483   470 EAVQQIEEAARTAEELLtkaKADADElRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEeqAEEVRA 549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  661 EAE--AEGMKDEAE--VEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVETDGMKP 736
Cdd:NF041483   550 AAEraARELREETEraIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQA 629

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  737 EAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPE-------AETEAE 809
Cdd:NF041483   630 QAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEaaealaaAQEEAA 709

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1840277627  810 GVKPEAETEAEGVKPEGETEAEKP----------------EAETEAEGLNSEAETEA 850
Cdd:NF041483   710 RRRREAEETLGSARAEADQERERAreqseellasarkrveEAQAEAQRLVEEADRRA 766
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 424-538 8.60e-16

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: 74.77  E-value: 8.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKT----YNNLDITVTQALRHRSQYF-------EG 492
Cdd:cd04586     8 VTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRREEPGTeprrVWWLDALLESPERLAEEYVkahgrtvGD 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1840277627 493 VMK-----CNRHETLETIVDRIVKAEVHRLVVVDENaRIVGIVSLSDILQA 538
Cdd:cd04586    88 VMTrpvvtVSPDTPLEEAARLMERHRIKRLPVVDDG-KLVGIVSRADLLRA 137
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 581-836 1.01e-15

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 81.35  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 581 EAFPDTETEEHVAEPATTVEGIVEADVEEGTPEEtaaEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKD 660
Cdd:NF033839  243 QALSEIDNVNTKVEIENTVHKIFADMDAVVTKFK---KGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKP 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 661 EaeaegMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGmKSETEAEVMKFEAETEAEGMKSETEVETDGMKPEAEA 740
Cdd:NF033839  320 E-----VKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKP-QPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEK 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 741 EAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAE 820
Cdd:NF033839  394 PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKP 473

                         250
                  ....*....|....*....
gi 1840277627 821 GVKPEGET---EAEKPEAE 836
Cdd:NF033839  474 EVKPQPEKpkpDNSKPQAD 492
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 569-853 1.09e-15

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 81.97  E-value: 1.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  569 AEPEANTEVVVVEAFPDTETEEHVAEpattvEGIVEADVEEGTpeETAAEGmKSEAVTEAEvMKDEAEAEGmkdEAEAEG 648
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGENGE-----ESGGEAEQEGET--ETKGEN-ESEGEIPAE-RKGEQEGEG---EIEAKE 703

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  649 MKDEAEAEGMKDEA----EAEGMKDEAEVEGmKDEAEAEGMKDEAEAEGmKDEAEAEGMKSETEaevmkFEAETEAEGMK 724
Cdd:TIGR00927  704 ADHKGETEAEEVEHegetEAEGTEDEGEIET-GEEGEEVEDEGEGEAEG-KHEVETEGDRKETE-----HEGETEAEGKE 776

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  725 SETEVETDGmkpeaeAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEgvkpEAETEAEgVKPEA 804
Cdd:TIGR00927  777 DEDEGEIQA------GEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG----EQELNAE-NQGEA 845

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1840277627  805 ETEAEGVkpEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAEVE 853
Cdd:TIGR00927  846 KQDEKGV--DGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 641-837 2.28e-15

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 80.20  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 641 KDEAEAEGMKDEAEAEGMKDEAEAEGMKDEaevegMKDEAEAEGMKDEAEAEGMKDEAEAEgmkSETEAEVMKFEAETEA 720
Cdd:NF033839  291 KPSAPKPGMQPSPQPEKKEVKPEPETPKPE-----VKPQLEKPKPEVKPQPEKPKPEVKPQ---LETPKPEVKPQPEKPK 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 721 EGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGV 800
Cdd:NF033839  363 PEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEV 442

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1840277627 801 KPEAETEAEGVKPEAETEAEGVKPEGETE--AEKPEAET 837
Cdd:NF033839  443 KPQPEKPKPEVKPQPETPKPEVKPQPEKPkpEVKPQPEK 481
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 628-856 2.49e-15

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 80.81  E-value: 2.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  628 AEVMKDEAEAEGMKDEAEAEG------MKDEAEAEGMKDEAEAEGMKDEAEVEGmKDEAEAEGmkdEAEAEGmKDEAEAE 701
Cdd:TIGR00927  622 AKVMALGDLSKGDVAEAEHTGertgeeGERPTEAEGENGEESGGEAEQEGETET-KGENESEG---EIPAER-KGEQEGE 696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  702 GmksETEAEVMKFEAETEAEGMKSETEVETDGMKPeaeaeaeemKSETEVKTDGMKPEAENETE-EMKPEAETEAEGVKP 780
Cdd:TIGR00927  697 G---EIEAKEADHKGETEAEEVEHEGETEAEGTED---------EGEIETGEEGEEVEDEGEGEaEGKHEVETEGDRKET 764

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  781 EAETEAEGVKPEAETEAE-----GVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAEVEFK 855
Cdd:TIGR00927  765 EHEGETEAEGKEDEDEGEiqageDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGE 844


                   .
gi 1840277627  856 A 856
Cdd:TIGR00927  845 A 845
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 612-853 4.45e-15

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 80.04  E-value: 4.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  612 PEETAAEGMKSEAVTEAEVMKDEAEAEGmKDEAEAEGMKDEAEAEGMKDEAEAEGmKDEAEVEGmkdEAEAEGmKDEAEA 691
Cdd:TIGR00927  622 AKVMALGDLSKGDVAEAEHTGERTGEEG-ERPTEAEGENGEESGGEAEQEGETET-KGENESEG---EIPAER-KGEQEG 695

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  692 EGmKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVETDG---MKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMK 768
Cdd:TIGR00927  696 EG-EIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEegeEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEG 774

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  769 PEAETEAE-----GVKPEAETEAEGVKPEAETEAEGVKPE----AETEAEGVKPEAETEAEGVKPEGETEAEKPE--AET 837
Cdd:TIGR00927  775 KEDEDEGEiqageDGEMKGDEGAEGKVEHEGETEAGEKDEhegqSETQADDTEVKDETGEQELNAENQGEAKQDEkgVDG 854

                          250
                   ....*....|....*.
gi 1840277627  838 EAEGLNSEAETEAEVE 853
Cdd:TIGR00927  855 GGGSDGGDSEEEEEEE 870
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 419-538 4.50e-15

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: 72.09  E-value: 4.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNLD-ITVTQALRHrsqyfeGVMKCN 497
Cdd:cd04629     3 RNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPgGTVADYMST------EVLTVS 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1840277627 498 RHETLETIVDRIVKAEVHRLVVVDENaRIVGIVSLSDILQA 538
Cdd:cd04629    77 PDTSIVDLAQLFLKNKPRRYPVVEDG-KLVGQISRRDVLRA 116
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 344-467 6.12e-15

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: 72.07  E-value: 6.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDpvsGNALY-ILTHKRILK-----FLQLFVCEmpkpafMKQNLEELTIgt 417
Cdd:cd04584     8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVD---DGKLVgIVTDRDLLRaspskATSLSIYE------LNYLLSKIPV-- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1840277627 418 yHDI-----AFIHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVINLA 467
Cdd:cd04584    77 -KDImtkdvITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAF 129
growth_prot_Scy NF041483
polarized growth protein Scy;
572-851 1.18e-14

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 78.71  E-value: 1.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  572 EANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEgtpeetaAEGMKSEAVTEAEVMKDEA---------EAEGMKD 642
Cdd:NF041483   921 EATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQ-------AEQLIAEATGEAERLRAEAaetvgsaqqHAERIRT 993

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  643 EAEAEGMKDEAEAEGMKDEA--EAEGMKDEAEVEGMKDEAEAEGMKDE------AEAEGMKDEAEAEGMKSETEAE---- 710
Cdd:NF041483   994 EAERVKAEAAAEAERLRTEAreEADRTLDEARKDANKRRSEAAEQADTliteaaAEADQLTAKAQEEALRTTTEAEaqad 1073

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  711 VMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEM-----KSETEVK--TDGMKPEAENETEEMKPEAETE-AEGVKPEA 782
Cdd:NF041483  1074 TMVGAARKEAERIVAEATVEGNSLVEKARTDADELlvgarRDATAIRerAEELRDRITGEIEELHERARREsAEQMKSAG 1153

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1840277627  783 E------TEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETeaEKPEAETEAEGLNSEAETEAE 851
Cdd:NF041483  1154 ErcdalvKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQ--KKAELVREAEKIKAEAEAEAK 1226
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
344-465 2.17e-14

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 72.99  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDpvSGNALYILTHKRILKFLqlfvcempkpaFMKQNLEELTIGTY--HDI 421
Cdd:COG2524    94 KDVITVSPDTTLEEALELMLEKGISGLPVVD--DGKLVGIITERDLLKAL-----------AEGRDLLDAPVSDImtRDV 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1840277627 422 AFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVIN 465
Cdd:COG2524   161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204
CBS COG0517
CBS domain [Signal transduction mechanisms];
344-469 2.49e-14

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 70.28  E-value: 2.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDpvSGNALY-ILTHKRILKFLqlfvcempkpAFMKQNLEELTIGTY--HD 420
Cdd:COG0517     9 TDVVTVSPDATVREALELMSEKRIGGLPVVD--EDGKLVgIVTDRDLRRAL----------AAEGKDLLDTPVSEVmtRP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1840277627 421 IAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAE 469
Cdd:COG0517    77 PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125
growth_prot_Scy NF041483
polarized growth protein Scy;
558-851 3.42e-14

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 77.17  E-value: 3.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  558 EAQTSPEALVEAEPEANTEVVvveafpdTETEEHVAEPATTVEGIVEADVEEGT----PEETAAEGMKSEAVTEAEVMKD 633
Cdd:NF041483   750 EAQAEAQRLVEEADRRATELV-------SAAEQTAQQVRDSVAGLQEQAEEEIAglrsAAEHAAERTRTEAQEEADRVRS 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  634 EAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEvegmkdeaeaegmkdeAEAEGMKDEAEAEGMKSETEAEVMK 713
Cdd:NF041483   823 DAYAERERASEDANRLRREAQEETEAAKALAERTVSEAI----------------AEAERLRSDASEYAQRVRTEASDTL 886

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  714 FEAETEAEgmKSETEVETDGMKpeaeaeaeeMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEA 793
Cdd:NF041483   887 ASAEQDAA--RTRADAREDANR---------IRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADA 955

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1840277627  794 ETEAEGVKPEAETEAEGVKPEA-ET----EAEGVKPEGETEAEKPEAETEAEGLNSEAETEAE 851
Cdd:NF041483   956 AAQAEQLIAEATGEAERLRAEAaETvgsaQQHAERIRTEAERVKAEAAAEAERLRTEAREEAD 1018
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
410-539 1.48e-13

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 68.40  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 410 LEELTIG---TYHDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNLD----ITVTQa 482
Cdd:COG4109    13 KEILLVEdimTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDTPIEDVMtknpITVTP- 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1840277627 483 lrhrsqyfegvmkcnrHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQAL 539
Cdd:COG4109    92 ----------------DTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKAL 132
PTZ00121 PTZ00121
MAEBL; Provisional
 548-857 2.27e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.79  E-value: 2.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  548 RKSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTE 627
Cdd:PTZ00121  1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  628 AEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEvegmkdEAEAEGMKDEAEAEgmKDEAEAEGMKSET 707
Cdd:PTZ00121  1304 ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA------KAEAEAAADEAEAA--EEKAEAAEKKKEE 1375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  708 E---AEVMKFEAET--EAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKtdgmKPEAENETEEMKPEAET--EAEGVKP 780
Cdd:PTZ00121  1376 AkkkADAAKKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK----KAEEKKKADEAKKKAEEakKADEAKK 1451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  781 EAET--EAEGVKPEAET--EAEGVKPEAET-----EAEGVKPEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAE 851
Cdd:PTZ00121  1452 KAEEakKAEEAKKKAEEakKADEAKKKAEEakkadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531


                   ....*.
gi 1840277627  852 VEFKAD 857
Cdd:PTZ00121  1532 EAKKAD 1537
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 544-853 8.27e-13

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 72.11  E-value: 8.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 544 AGINRKSSQPQP---PPEAQTSPEALVEAEPEANTEVVVVeafPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGM 620
Cdd:NF033839  153 SGSSTKPETPQPenpEHQKPTTPAPDTKPSPQPEGKKPSV---PDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQ 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 621 KSEAVTEAEVMKDEAEAEgmkdeAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKD-EAEAEGMKDEAE 699
Cdd:NF033839  230 IVALIKELDELKKQALSE-----IDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKpSAPKPGMQPSPQ 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 700 AEGMKSETEAEVMKFEAETEAEGMKSETEVETDGMKPEaeaeaeemksetevktdgMKPEAENETEEMKPEAETEAEGVK 779
Cdd:NF033839  305 PEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPE------------------VKPQLETPKPEVKPQPEKPKPEVK 366

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840277627 780 PEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEaegvKPEGETEAEKPEAETEAEGLNSEAETEAEVE 853
Cdd:NF033839  367 PQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKP----KPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE 436
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 262-391 1.10e-12

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: 65.34  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 262 SSKLVVFDTTLQVKKAFFALVANGVRAAPLWEtKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETwrelylqe 341
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVD-DDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVIT-------- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1840277627 342 tfkplvnITPDASIFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILK 391
Cdd:cd02205    72 -------VSPDTDLEEALELMLEHGIRRLPVVDD-DGKLVGIVTRRDILR 113
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 419-539 2.19e-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: 64.89  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALRHRSQyfegvmkcnR 498
Cdd:cd04600     3 RDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLGLRRD---------R 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1840277627 499 HETLETIVDRIVK-----------------AEVHRLVVVDENARIVGIVSLSDILQAL 539
Cdd:cd04600    74 PETVGDIMTRPVVtvrpdtpiaelvplfsdGGLHHIPVVDADGRLVGIVTQSDLIAAL 131
PTZ00121 PTZ00121
MAEBL; Provisional
 548-857 3.30e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 70.94  E-value: 3.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  548 RKSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTE 627
Cdd:PTZ00121  1200 RKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  628 AEVMKdeaEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEA---EAEGMK 704
Cdd:PTZ00121  1280 ADELK---KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAakaEAEAAA 1356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  705 SETEAEVMKFEAeteAEGMKSETEVETDGMKPeaeaeaeemKSETEVKTDGMKPEAENE---TEEMK--PEAETEAEGVK 779
Cdd:PTZ00121  1357 DEAEAAEEKAEA---AEKKKEEAKKKADAAKK---------KAEEKKKADEAKKKAEEDkkkADELKkaAAAKKKADEAK 1424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  780 PEAET--EAEGVKPEAET--EAEGVKPEAET--EAEGVKPEAET--EAEGVKPEGETEAEKPEAETEAEGLNSEAE---T 848
Cdd:PTZ00121  1425 KKAEEkkKADEAKKKAEEakKADEAKKKAEEakKAEEAKKKAEEakKADEAKKKAEEAKKADEAKKKAEEAKKKADeakK 1504


                   ....*....
gi 1840277627  849 EAEVEFKAD 857
Cdd:PTZ00121  1505 AAEAKKKAD 1513
growth_prot_Scy NF041483
polarized growth protein Scy;
617-820 4.13e-12

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 70.24  E-value: 4.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  617 AEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEgmkdeAEAEGMKDEAEAEGMKDEAE----VEGMKDEAEAEGMKDEAEAE 692
Cdd:NF041483   904 ANRIRSDAAAQADRLIGEATSEAERLTAEAR-----AEAERLRDEARAEAERVRADaaaqAEQLIAEATGEAERLRAEAA 978

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  693 GMKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAE 772
Cdd:NF041483   979 ETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQ 1058

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1840277627  773 TEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAE 820
Cdd:NF041483  1059 EEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTDAD 1106
growth_prot_Scy NF041483
polarized growth protein Scy;
614-840 5.16e-12

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 70.24  E-value: 5.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  614 ETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAegmKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKD------ 687
Cdd:NF041483  1003 AAEAERLRTEAREEADRTLDEARKDANKRRSEA---AEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADtmvgaa 1079

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  688 EAEAEGMKDEAEAEG----MKSETEAEVMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSET--EVKTDGMKPEA- 760
Cdd:NF041483  1080 RKEAERIVAEATVEGnslvEKARTDADELLVGARRDATAIRERAEELRDRITGEIEELHERARRESaeQMKSAGERCDAl 1159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  761 ENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEaegvKPEAETEAEGVKPEGETEAEKPEAETEAE 840
Cdd:NF041483  1160 VKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQK----KAELVREAEKIKAEAEAEAKRTVEEGKRE 1235
growth_prot_Scy NF041483
polarized growth protein Scy;
586-851 5.66e-12

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 69.85  E-value: 5.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  586 TETEEHVAEPATTVEGIVEADVEEG---TPEETAAEGMKseAVTEAEVMKDEAEaegmkDEAEAEGMKDEAEAEGMKDEA 662
Cdd:NF041483   330 AEAEQALADARAEAEKLVAEAAEKArtvAAEDTAAQLAK--AARTAEEVLTKAS-----EDAKATTRAAAEEAERIRREA 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  663 EAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVETDGMKPEAEAEA 742
Cdd:NF041483   403 EAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTA 482

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  743 EEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAE-------TEAEGVKPEAETEAEGVKPEAETEAEGVKPEA 815
Cdd:NF041483   483 EELLTKAKADADELRSTATAESERVRTEAIERATTLRRQAEetlertrAEAERLRAEAEEQAEEVRAAAERAARELREET 562

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1840277627  816 ETEAEGVKPEGETEAEKPEAETE-----AEGLNSEAETEAE 851
Cdd:NF041483   563 ERAIAARQAEAAEELTRLHTEAEerltaAEEALADARAEAE 603
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 424-538 1.71e-11

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: 62.35  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNN------------LDITVtqalrhRSQYFE 491
Cdd:cd04632     7 VNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTrggdrggekermLDLPV------YDIMSS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1840277627 492 GVMKCNRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQA 538
Cdd:cd04632    81 PVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 494-813 1.96e-11

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 68.10  E-value: 1.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  494 MKCNRHetletiVDRIVKAEVHRLVVvdenARIVGIVSLSDILQALVLTPAGINRKSSQPQPPPEAQTSPEALVEAEPEA 573
Cdd:TIGR00927  602 MKWNKQ------IELWVKEQLSRRPV----AKVMALGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEG 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  574 NTEVVVvEAFPDTETEehvAEPATTVEGIVEADVEEGTPE-ETAAEGMKSEAVTEAEVMKDEAEAEGmKDEAEAEGMKDE 652
Cdd:TIGR00927  672 ETETKG-ENESEGEIP---AERKGEQEGEGEIEAKEADHKgETEAEEVEHEGETEAEGTEDEGEIET-GEEGEEVEDEGE 746

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  653 AEAEGmKDEAEAEGMKDEAEVEGmkdEAEAEGMKDEAEAEgmkDEAEAEG-MKSETEAevmkfEAETEAEGMKSETEVET 731
Cdd:TIGR00927  747 GEAEG-KHEVETEGDRKETEHEG---ETEAEGKEDEDEGE---IQAGEDGeMKGDEGA-----EGKVEHEGETEAGEKDE 814

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  732 DGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEgvkPEAETEAEGVKPEAETEAEGV 811
Cdd:TIGR00927  815 HEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEE---EEEEEEEEEEEEEEEEEEENE 891


                   ..
gi 1840277627  812 KP 813
Cdd:TIGR00927  892 EP 893
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 691-857 2.95e-11

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 67.71  E-value: 2.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  691 AEGMKDEAEAEGMKSETEAEvmkfeAETEAEGMKSEtEVETDGMKPEAEAEAEEMKSETEvktdgMKPEAENETEEmkpE 770
Cdd:TIGR00927  631 SKGDVAEAEHTGERTGEEGE-----RPTEAEGENGE-ESGGEAEQEGETETKGENESEGE-----IPAERKGEQEG---E 696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  771 AETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEG----VKPEAETEAEGvKPEGETEAEKPEAETEAEglnsea 846
Cdd:TIGR00927  697 GEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEegeeVEDEGEGEAEG-KHEVETEGDRKETEHEGE------ 769

                          170
                   ....*....|.
gi 1840277627  847 eTEAEVEFKAD 857
Cdd:TIGR00927  770 -TEAEGKEDED 779
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
663-846 5.30e-11

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 65.66  E-value: 5.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 663 EAEGMKDEAEV--EGMKDEAEAEGMKDEAEAEGMKDEAEAEgMKSETEAEVMKF-EAETEAEGMKSETEVETDgmkpeae 739
Cdd:COG2268   187 DALGRRKIAEIirDARIAEAEAERETEIAIAQANREAEEAE-LEQEREIETARIaEAEAELAKKKAEERREAE------- 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 740 aeaeemksETEVKTDGMKPEAENETEEmkpEAETEAEGVKPEAETE---AEGVKPEAETEAEGVKPeAETEAEGVKPEAE 816
Cdd:COG2268   259 --------TARAEAEAAYEIAEANAER---EVQRQLEIAEREREIElqeKEAEREEAELEADVRKP-AEAEKQAAEAEAE 326

                         170       180       190
                  ....*....|....*....|....*....|
gi 1840277627 817 TEAEGVKPEGETEAEKPEAETEAEGLNSEA 846
Cdd:COG2268   327 AEAEAIRAKGLAEAEGKRALAEAWNKLGDA 356
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 344-466 8.42e-11

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: 59.85  E-value: 8.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDpvSGNALYILTHKRILKFLQlfvcempkpafmkQNLEELTIGTY--HDI 421
Cdd:cd04588     2 KDLITLKPDATIKDAAKLLSENNIHGAPVVD--DGKLVGIVTLTDIAKALA-------------EGKENAKVKDImtKDV 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1840277627 422 AFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINL 466
Cdd:cd04588    67 ITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 424-539 9.63e-11

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: 59.84  E-value: 9.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTynNLDITVTQALRhrsqyfEGVMKCNRHETLE 503
Cdd:cd09836     8 VPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGI--DLDTPVEEIMT------KNLVTVSPDESIY 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1840277627 504 TIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQAL 539
Cdd:cd09836    80 EAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
617-798 1.39e-10

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 64.51  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 617 AEGMK--SEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGM 694
Cdd:COG2268   188 ALGRRkiAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAA 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 695 KDEAEAEGMKS-ETEAEVMKFEAETEAEgmksETEVEtdgmkpeaeaeaeemKSETEVKTDGMKPeAENETEEMKPEAET 773
Cdd:COG2268   268 YEIAEANAEREvQRQLEIAEREREIELQ----EKEAE---------------REEAELEADVRKP-AEAEKQAAEAEAEA 327

                         170       180
                  ....*....|....*....|....*
gi 1840277627 774 EAEGVKPEAETEAEGVKPEAETEAE 798
Cdd:COG2268   328 EAEAIRAKGLAEAEGKRALAEAWNK 352
PTZ00121 PTZ00121
MAEBL; Provisional
 581-857 1.40e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.55  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  581 EAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKD 660
Cdd:PTZ00121  1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  661 EAEAEGMKDEAEVEGmKDEAEAEGMKDEAE----AEGMKDEAE----AEGMKSETEAEVMKFEAETEAEGMKSETEVETD 732
Cdd:PTZ00121  1413 AAAAKKKADEAKKKA-EEKKKADEAKKKAEeakkADEAKKKAEeakkAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  733 GMKPEAEAEAEEMKSETEVKTDGM-KPEAENETEEMKP--EAETEAEGVKPEAETEAEGVKPEAET-EAEGV-KPEAETE 807
Cdd:PTZ00121  1492 AEEAKKKADEAKKAAEAKKKADEAkKAEEAKKADEAKKaeEAKKADEAKKAEEKKKADELKKAEELkKAEEKkKAEEAKK 1571

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1840277627  808 AEGVKPEAETEAEGVK--PEGETEAEKPEAETEAEGLNSEAETEAEVEFKAD 857
Cdd:PTZ00121  1572 AEEDKNMALRKAEEAKkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 419-535 1.70e-10

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: 58.97  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDEsGKVV------DIyskfdVINLAAEKTyNNLDITVTQALRHrsqyfeG 492
Cdd:cd04622     3 RDVVTVSPDTTLREAARLMRDLDIGALPVCEG-DRLVgmvtdrDI-----VVRAVAEGK-DPNTTTVREVMTG------D 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1840277627 493 VMKCNRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDI 535
Cdd:cd04622    70 VVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 420-468 1.78e-10

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: 56.75  E-value: 1.78e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1840277627  420 DIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAA 468
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 344-464 2.30e-10

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: 59.17  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDPVSGNALYILTHKRILKFL-----QLFVCEMPKPAFMKQNLEELTIGTY 418
Cdd:cd17779     8 KDVITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLgggskYNLVEKKHNGNLLAAINEPVREIMT 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVI 464
Cdd:cd17779    88 RDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFL 133
PTZ00121 PTZ00121
MAEBL; Provisional
 589-855 2.38e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 2.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  589 EEHVAEPATTVEGIVEADVEEGTPEET-AAEGMK---SEAVTEAEVMKDEAEAEGMKDEA---EAEGMKDEAEAEGMKDE 661
Cdd:PTZ00121  1288 EKKKADEAKKAEEKKKADEAKKKAEEAkKADEAKkkaEEAKKKADAAKKKAEEAKKAAEAakaEAEAAADEAEAAEEKAE 1367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  662 AeAEGMKDEAE--VEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVETdgmKPEAE 739
Cdd:PTZ00121  1368 A-AEKKKEEAKkkADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK---KAEEA 1443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  740 AEAEEMKSETEVKTDG----MKPEAENETEEMKPEAET--EAEGVKPEAEtEAEGVKPEAETEAEGVKPEAETEAEGVKP 813
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAeeakKKAEEAKKADEAKKKAEEakKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKAEEAK 1522

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1840277627  814 EAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAEVEFK 855
Cdd:PTZ00121  1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
growth_prot_Scy NF041483
polarized growth protein Scy;
560-851 2.68e-10

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 64.46  E-value: 2.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  560 QTSPEALVEAEPEAntEVVVVEAfpdtetEEHVAEPATTVEGIVEADVEegTPEETAAEgMKSEAVTEAEVMKdeaeaeg 639
Cdd:NF041483   268 QEAEEALREARAEA--EKVVAEA------KEAAAKQLASAESANEQRTR--TAKEEIAR-LVGEATKEAEALK------- 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  640 mkdeAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEgmkdEAEAEGMKDEAEAEGM----KDEAEAEGMKSETEAEVMKFE 715
Cdd:NF041483   330 ----AEAEQALADARAEAEKLVAEAAEKARTVAAE----DTAAQLAKAARTAEEVltkaSEDAKATTRAAAEEAERIRRE 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  716 AETEAEGMKSETEVETDGMKPEAEAEAEemksETEVKTDGMKPEA---ENETEEMKPEAETEAEGVKPEAETEAEGVKPE 792
Cdd:NF041483   402 AEAEADRLRGEAADQAEQLKGAAKDDTK----EYRAKTVELQEEArrlRGEAEQLRAEAVAEGERIRGEARREAVQQIEE 477

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1840277627  793 AETEAEGVKPEAETEAEGVKPEAETEAEGVKPE--------------------GETEAEKPEAETEAEGLNSEAETEAE 851
Cdd:NF041483   478 AARTAEELLTKAKADADELRSTATAESERVRTEaierattlrrqaeetlertrAEAERLRAEAEEQAEEVRAAAERAAR 556
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 496-539 8.67e-10

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: 54.83  E-value: 8.67e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1840277627  496 CNRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQAL 539
Cdd:smart00116   5 VSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 344-469 1.03e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 57.15  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFLQLfvcempkpafMKQNLEELTIGTY--HDI 421
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDD-DGRLVGIITDRDLRRRVLA----------EGLDPLDTPVSEVmtRPP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1840277627 422 AFIHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVINLAAE 469
Cdd:COG2905    76 ITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALSE 122
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 420-538 3.96e-09

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: 55.94  E-value: 3.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 420 DIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAA----EKTYNNLDITVT--------QALRHRS 487
Cdd:cd17789     4 KLHVVKPNTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLALDSisgrSQTDNNFPPADStwktfnevQKLLSKT 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1840277627 488 --QYFEGVMKCN----RHET-LETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQA 538
Cdd:cd17789    84 ngKVVGDVMTPSplvvREKTnLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVVRA 141
PTZ00121 PTZ00121
MAEBL; Provisional
 558-857 5.47e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 5.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  558 EAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEAD----VEEGTPEETA---AEGMKSEAVTEAEV 630
Cdd:PTZ00121  1113 EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEdarkAEEARKAEDAkkaEAARKAEEVRKAEE 1192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  631 MKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEgmKDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEAE 710
Cdd:PTZ00121  1193 LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAK--KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  711 VMKFEAETEAEGMKSETEVEtdgmkpeaeAEAEEMKSETEVKTDGMKPEAEN--ETEEMKPEAE---TEAEGVKPEAE-- 783
Cdd:PTZ00121  1271 AIKAEEARKADELKKAEEKK---------KADEAKKAEEKKKADEAKKKAEEakKADEAKKKAEeakKKADAAKKKAEea 1341

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  784 -TEAEGVKPEAETEAEGVKPEAETE--AEGVKPEAETEAEGVKPEGE----TEAEKPEAEtEAEGLNSEAETEAEVEFKA 856
Cdd:PTZ00121  1342 kKAAEAAKAEAEAAADEAEAAEEKAeaAEKKKEEAKKKADAAKKKAEekkkADEAKKKAE-EDKKKADELKKAAAAKKKA 1420


                   .
gi 1840277627  857 D 857
Cdd:PTZ00121  1421 D 1421
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 419-537 6.12e-09

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: 54.46  E-value: 6.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVINLAAEktyNNLDITVTQALRHRsqyfegVMKCNR 498
Cdd:cd04588     2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDD-GKLVGIVTLTDIAKALAE---GKENAKVKDIMTKD------VITIDK 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1840277627 499 HETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQ 537
Cdd:cd04588    72 DEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
262-393 6.88e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 56.82  E-value: 6.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 262 SSKLVVFDTTLQVKKAFFALVANGVRAAPLweTKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEhkietwrelylqe 341
Cdd:COG2524    93 TKDVITVSPDTTLEEALELMLEKGISGLPV--VDDGKLVGIITERDLLKALAEGRDLLDAPVSDIMT------------- 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1840277627 342 tfKPLVNITPDASIFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFL 393
Cdd:COG2524   158 --RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDD-DGKLVGIITRTDILRAL 206
PTZ00121 PTZ00121
MAEBL; Provisional
 558-857 7.17e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 7.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  558 EAQTSPEALVEAEPEANTEVV---VVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEET--AAEGMKSEAVTEAEVMK 632
Cdd:PTZ00121  1455 EAKKAEEAKKKAEEAKKADEAkkkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkkAEEAKKADEAKKAEEAK 1534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  633 DEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGM--KDEAEAEGMKDEAEAEGMKDEAEAEGMKSET--E 708
Cdd:PTZ00121  1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakK 1614

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  709 AEvmkfEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSEtEVKTDGMKPEAENETEEMKPEAET-EAEGVKPEAETE-- 785
Cdd:PTZ00121  1615 AE----EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENKIKAAEEAKKAEEDKkKAEEAKKAEEDEkk 1689

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  786 -AEGVKPEAET--EAEGVKPEAETE---AEGVKPEAE---TEAEGVKPEGETEAEKP-EAETEAEGLNSEAETEAEVEFK 855
Cdd:PTZ00121  1690 aAEALKKEAEEakKAEELKKKEAEEkkkAEELKKAEEenkIKAEEAKKEAEEDKKKAeEAKKDEEEKKKIAHLKKEEEKK 1769


                   ..
gi 1840277627  856 AD 857
Cdd:PTZ00121  1770 AE 1771
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 419-535 7.91e-09

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: 54.34  E-value: 7.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALRHRsqyfegVMKCNR 498
Cdd:cd04623     2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRD------VVTCTP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1840277627 499 HETLETIVDRIVKaevHR---LVVVDENaRIVGIVSLSDI 535
Cdd:cd04623    76 DDTVEECMALMTE---RRirhLPVVEDG-KLVGIVSIGDV 111
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 419-469 1.19e-08

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: 51.83  E-value: 1.19e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAE 469
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 752-893 1.24e-08

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 58.85  E-value: 1.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  752 KTDGMKPEAENETEEMKPEAETEAEGVKPE-AETEAEgvkPEAETEAEG-VKPEAETEAEG---VKPEAETEAEGVKPEG 826
Cdd:TIGR00927  632 KGDVAEAEHTGERTGEEGERPTEAEGENGEeSGGEAE---QEGETETKGeNESEGEIPAERkgeQEGEGEIEAKEADHKG 708

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1840277627  827 ETEAEKPEAE--TEAEGLNSEAETEAEVEFKADVMMAEAEAELVAEAEAKVDVVPVMDEVGTEAVVEAD 893
Cdd:TIGR00927  709 ETEAEEVEHEgeTEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKED 777
PTZ00121 PTZ00121
MAEBL; Provisional
 541-857 1.58e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 1.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  541 LTPAGINRKSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEAD----VEEGTPEE-- 614
Cdd:PTZ00121  1072 LKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkAEEARKAEda 1151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  615 -------TAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKD 687
Cdd:PTZ00121  1152 krveiarKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  688 EAEAEgmKDEAEAEGMKSE-TEAEVMKFEAETEAEGMKSETEVETD-GMKPEAEAEAEEMKSETEVKtdgmKPEAENETE 765
Cdd:PTZ00121  1232 AEEAK--KDAEEAKKAEEErNNEEIRKFEEARMAHFARRQAAIKAEeARKADELKKAEEKKKADEAK----KAEEKKKAD 1305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  766 EMKPEAET--EAEGVKPEAEteaegvkpEAETEAEGVKPEAEtEAEGVKPEAETEAEGVKPEGETEAEKPEAE----TEA 839
Cdd:PTZ00121  1306 EAKKKAEEakKADEAKKKAE--------EAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAekkkEEA 1376

                          330
                   ....*....|....*...
gi 1840277627  840 EGLNSEAETEAEVEFKAD 857
Cdd:PTZ00121  1377 KKKADAAKKKAEEKKKAD 1394
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 715-888 1.62e-08

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 58.47  E-value: 1.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  715 EAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKtdgmkpeAENETEemkpeAETEAEGvkpEAETEAEGvkpeaE 794
Cdd:TIGR00927  639 EHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETK-------GENESE-----GEIPAER---KGEQEGEG-----E 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  795 TEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEaekpeaeTEAEGLNSEAETEAEVEFKADVMMAEAEAELVAEAEAK 874
Cdd:TIGR00927  699 IEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIE-------TGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETE 771

                          170
                   ....*....|....
gi 1840277627  875 VDVVPVMDEVGTEA 888
Cdd:TIGR00927  772 AEGKEDEDEGEIQA 785
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 346-465 1.67e-08

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: 53.21  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 346 LVNITPDASIFDAVYSLIKNKIHRLPVIDpVSGNALYILTHKRILKFLqL---FVCEMPKPA--FMKqnleeltigtyHD 420
Cdd:cd04629     5 PVTLTPDTSILEAVELLLEHKISGAPVVD-EQGRLVGFLSEQDCLKAL-LeasYHCEPGGTVadYMS-----------TE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1840277627 421 IAFIHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVIN 465
Cdd:cd04629    72 VLTVSPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQISRRDVLR 115
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 344-464 1.81e-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: 53.97  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDP-------VSG----NALYILTHKRILKFLQLFVCEMPKPAFMKQNLEE 412
Cdd:cd04586     3 TDVVTVTPDTSVREAARLLLEHRISGLPVVDDdgklvgiVSEgdllRREEPGTEPRRVWWLDALLESPERLAEEYVKAHG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1840277627 413 LTIG---TyHDIAFIHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVI 464
Cdd:cd04586    83 RTVGdvmT-RPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLL 135
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 493-540 1.86e-08

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: 51.45  E-value: 1.86e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1840277627 493 VMKCNRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQALV 540
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
PTZ00121 PTZ00121
MAEBL; Provisional
 589-845 2.12e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 2.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  589 EEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTEAEVMKDEAEA---EGMKDEAEAEGMKDEAEAEGMKDEAEAE 665
Cdd:PTZ00121  1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  666 GMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEAEVMKfEAETEAEGMKSETEVETDGMKPEAEAEAEEM 745
Cdd:PTZ00121  1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE-EDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  746 KSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETE---AEGVKPEAE--TEAEGVKPEAETEAEGVKPEAETE-A 819
Cdd:PTZ00121  1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDkkkAEEAKKDEEekKKIAHLKKEEEKKAEEIRKEKEAViE 1782

                          250       260
                   ....*....|....*....|....*.
gi 1840277627  820 EGVKPEGETEAEKPEAETEAEGLNSE 845
Cdd:PTZ00121  1783 EELDEEDEKRRMEVDKKIKDIFDNFA 1808
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 347-465 2.54e-08

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: 53.39  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 347 VNITPDASIFDAVYSLIKNKIHRLPVidpVSGNALY-ILTHKRILKFLQlfvcemPKPAFmkqnlEELTIGTYH------ 419
Cdd:cd04631    11 ITATPGTPIEDVAKIMVRNGFRRLPV---VSDGKLVgIVTSTDIMRYLG------SGEAF-----EKLKTGNIHevlnvp 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1840277627 420 -------DIAFIHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVIN 465
Cdd:cd04631    77 issimkrDIITTTPDTDLGEAAELMLEKNIGALPVVDD-GKLVGIITERDILR 128
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 420-535 2.84e-08

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: 52.63  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 420 DIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKtYNNLDITVTQalrhrsqyfeGVMKCNRH 499
Cdd:cd04605     9 DVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALK-KDSLEEIMTR----------NVITARPD 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1840277627 500 ETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDI 535
Cdd:cd04605    78 EPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
PTZ00121 PTZ00121
MAEBL; Provisional
 558-855 4.66e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 4.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  558 EAQTSPEALVEAEPEANTEvvvvEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEG----MKSEAVTEAEVMKD 633
Cdd:PTZ00121  1442 EAKKADEAKKKAEEAKKAE----EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeakKAAEAKKKADEAKK 1517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  634 EAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEAEVMK 713
Cdd:PTZ00121  1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  714 FEAETEAEGMKSETEVETDGMKpeaeAEAEEMKSETEVKTDGMKPEAENETEEMKPE----AETEAEGVKPEAETEAEGV 789
Cdd:PTZ00121  1598 MKLYEEEKKMKAEEAKKAEEAK----IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEelkkAEEENKIKAAEEAKKAEED 1673

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840277627  790 KPEAEtEAEGVKPEAETEAEGVKPEAET--EAEGVKPEGETEAEKPEAETEAEGLNS----EAETEAEVEFK 855
Cdd:PTZ00121  1674 KKKAE-EAKKAEEDEKKAAEALKKEAEEakKAEELKKKEAEEKKKAEELKKAEEENKikaeEAKKEAEEDKK 1744
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 345-394 1.37e-07

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: 48.66  E-value: 1.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1840277627  345 PLVNITPDASIFDAVYSLIKNKIHRLPVIDPVsGNALYILTHKRILKFLQ 394
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIKALA 49
PHA03169 PHA03169
hypothetical protein; Provisional
 612-848 1.76e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 54.59  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 612 PEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEgmkDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEA 691
Cdd:PHA03169   48 PPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGE---KEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 692 EGMKDEAEAEGMKSETEAEvmkfeaeteaEGMKSETEVETDGmkpeaeaeaeemKSETEVKTDGMKPEAENETEEmkpea 771
Cdd:PHA03169  125 GSSPESPASHSPPPSPPSH----------PGPHEPAPPESHN------------PSPNQQPSSFLQPSHEDSPEE----- 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1840277627 772 eteAEGVKPEAETEAEGvKPEAETEAEGVKPEAETEAEGvKPEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAET 848
Cdd:PHA03169  178 ---PEPPTSEPEPDSPG-PPQSETPTSSPPPQSPPDEPG-EPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPG 249
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 344-464 1.85e-07

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: 51.02  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDP---VSGnalyILTHKRILKFLQLfvcemPKPAFMKQNLEELTIGTY-- 418
Cdd:cd04600     3 RDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRarrLVG----IVTLADLLKHADL-----DPPRGLRGRLRRTLGLRRdr 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1840277627 419 ---------HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVI 464
Cdd:cd04600    74 petvgdimtRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLI 128
PHA03169 PHA03169
hypothetical protein; Provisional
 634-853 3.89e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 53.44  E-value: 3.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 634 EAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEaEAEGMKDEAEAEGMKSETEAEvmK 713
Cdd:PHA03169   32 QAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEE-RGQGGPSGSGSESVGSPTPSP--S 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 714 FEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGmKPEAENETEEMKPEAETEAEGvkPEAETEAEGVKPEA 793
Cdd:PHA03169  109 GSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPA-PPESHNPSPNQQPSSFLQPSH--EDSPEEPEPPTSEP 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 794 ETEAEGvKPEAETEAEGVKPEAETEAEGvKPEGETEAEKPEAETEAEGLNSEAETEAEVE 853
Cdd:PHA03169  186 EPDSPG-PPQSETPTSSPPPQSPPDEPG-EPQSPTPQQAPSPNTQQAVEHEDEPTEPERE 243
growth_prot_Scy NF041483
polarized growth protein Scy;
613-850 1.01e-06

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 52.91  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  613 EETAAEGMKS--EAVTEAEVMKDEA------EAEGMKDEAEAEGMKDEAEAEGM-----------KDEAE---------- 663
Cdd:NF041483   170 DESRAEAEQAlaAARAEAERLAEEArqrlgsEAESARAEAEAILRRARKDAERLlnaastqaqeaTDHAEqlrsstaaes 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  664 -------------AEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSE----TEAEVMKF--EAETEAEGMK 724
Cdd:NF041483   250 dqarrqaaelsraAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQrtrtAKEEIARLvgEATKEAEALK 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  725 SETE-------VETDGMKPEAEAEAEEMKSEtevKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEA 797
Cdd:NF041483   330 AEAEqaladarAEAEKLVAEAAEKARTVAAE---DTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEA 406

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1840277627  798 EGVKPEAETEAEGVKPEA------------ETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEA 850
Cdd:NF041483   407 DRLRGEAADQAEQLKGAAkddtkeyraktvELQEEARRLRGEAEQLRAEAVAEGERIRGEARREA 471
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 419-539 1.21e-06

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: 47.92  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFD-VINLAAEktynNLDITVTQAlrhrsqyfEGVMK-- 495
Cdd:cd17775     3 REVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDiVVEVVAK----GLDPKDVTV--------GDIMSad 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1840277627 496 ---CNRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQAL 539
Cdd:cd17775    71 litAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 547-721 1.31e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 51.73  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 547 NRKSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEgmksEAVT 626
Cdd:PRK09510   65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEE----AAAK 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 627 EAEVMKDEAEAEGMKDEAEAEGMKDEA---EAEGMKDEAEAEGMKDEAEVEGMKDEAEAegmKDEAEAEGMKDEAEAEGM 703
Cdd:PRK09510  141 AAAAAKAKAEAEAKRAAAAAKKAAAEAkkkAEAEAAKKAAAEAKKKAEAEAAAKAAAEA---KKKAEAEAKKKAAAEAKK 217

                         170
                  ....*....|....*...
gi 1840277627 704 KSETEAEVMKFEAETEAE 721
Cdd:PRK09510  218 KAAAEAKAAAAKAAAEAK 235
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 424-536 1.38e-06

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: 47.90  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSkFDVINLAAEKTYNNLDITVTQalrhrsqyfegVMKCNRHETLE 503
Cdd:cd04583     7 ITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVD-IEDINRNYRKAKKVGEIMERD-----------VFTVKEDSLLR 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1840277627 504 TIVDRIVKAEVHRLVVVDENARIVGIV---SLSDIL 536
Cdd:cd04583    75 DTVDRILKRGLKYVPVVDEQGRLVGLVtraSLVDIV 110
PTZ00121 PTZ00121
MAEBL; Provisional
 558-847 1.43e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  558 EAQTSPEALVEAEPEANTEVVVVEAfpdteTEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEA------------- 624
Cdd:PTZ00121  1326 EAKKKADAAKKKAEEAKKAAEAAKA-----EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAeekkkadeakkka 1400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  625 ---VTEAEVMKDEAEAEGMKDEA--------EAEGMKDEAE----AEGMKDEAE----AEGMKDEAE----VEGMKDEAE 681
Cdd:PTZ00121  1401 eedKKKADELKKAAAAKKKADEAkkkaeekkKADEAKKKAEeakkADEAKKKAEeakkAEEAKKKAEeakkADEAKKKAE 1480

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  682 AEGMKDEAEAEGMKDEAEAEGMKSETEA-----EVMKFEAETEAEGMKSETEVET--DGMKPEAEAEAEEMKSETEVKT- 753
Cdd:PTZ00121  1481 EAKKADEAKKKAEEAKKKADEAKKAAEAkkkadEAKKAEEAKKADEAKKAEEAKKadEAKKAEEKKKADELKKAEELKKa 1560

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  754 -DGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEG-VKPEAETEAEGVKPEGETEAE 831
Cdd:PTZ00121  1561 eEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKK 1640

                          330
                   ....*....|....*..
gi 1840277627  832 KPEAET-EAEGLNSEAE 847
Cdd:PTZ00121  1641 KEAEEKkKAEELKKAEE 1657
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 426-535 1.70e-06

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: 47.60  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 426 PDTPIIKALNIFVDRRVSALpVVDESGKVVDIYSKFDVinLAaektynnLDITVTQALRhrsQYFEGVM----KC-NRHE 500
Cdd:cd09833    12 PDTPLADAAARMAERRCSSI-LIVENGEIVGIWTERDA--LK-------LDFSDPDAFR---RPISEVMsspvLTiPQDT 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1840277627 501 TLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDI 535
Cdd:cd09833    79 TLGEAAVRFRQEGVRHLLVVDDDGRPVGIVSQTDV 113
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 344-465 2.01e-06

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: 47.52  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFL-QLFVCEMPKPAFMKQNLEEltigtyhdia 422
Cdd:cd09836     3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDD-DGKPVGIVTERDIVRAVaEGIDLDTPVEEIMTKNLVT---------- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1840277627 423 fIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVIN 465
Cdd:cd09836    72 -VSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAR 113
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 336-464 3.66e-06

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: 47.34  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 336 ELYLQETfKPLVNITPDASIFDAVYSLIKNKIHRLPVIDpvsGNALY-ILTHKRILKFLQLFVCEMPKPAFMKQN----L 410
Cdd:cd17777     3 ELMIIAS-PPVLSISPSAPILSAFEKMNRRGIRRLVVVD---ENKLEgILSARDLVSYLGGGCLFKIVESRHQGDlysaL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1840277627 411 EELTIGTYH--DIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVI 464
Cdd:cd17777    79 NREVVETIMtpNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLV 134
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
558-700 3.82e-06

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 50.26  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 558 EAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGI-----VEADVEEGTPEETAAEGMKSEAVTEAEVMK 632
Cdd:COG2268   229 EQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEAnaereVQRQLEIAEREREIELQEKEAEREEAELEA 308

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840277627 633 DE---AEAEGMKDEAEAEGmkdEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEA 700
Cdd:COG2268   309 DVrkpAEAEKQAAEAEAEA---EAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKP 376
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 551-851 4.18e-06

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 50.78  E-value: 4.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  551 SQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTEAEV 630
Cdd:COG5271    363 DAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDD 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  631 MKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDeAEAEGMKDEAEAEGMKSETEAE 710
Cdd:COG5271    443 IATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEED-AEAEADSDELTAEETSADDGAD 521

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  711 VMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVK 790
Cdd:COG5271    522 TDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASE 601

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840277627  791 PEAETEAEGVKPEAETEAEGVKPEAETEAEGVKpegETEAEKPEAETEAEGLNSEAETEAE 851
Cdd:COG5271    602 DEAAEEEEADDDEADADADGAADEEETEEEAAE---DEAAEPETDASEAADEDADAETEAE 659
growth_prot_Scy NF041483
polarized growth protein Scy;
627-850 4.23e-06

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 50.98  E-value: 4.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  627 EAEVMKDEAEAEGMK--DEAEAEGMKDEAEAEGMKD----EAEAEGMKDEAEvegMKDEAEAEGMKDEAEAEGMKDEAEA 700
Cdd:NF041483   144 ESHVNENVAWAEQLRarTESQARRLLDESRAEAEQAlaaaRAEAERLAEEAR---QRLGSEAESARAEAEAILRRARKDA 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  701 EGMKseTEAEVMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEvktdgmkpeaenETEEMKPEAETEAEGVKP 780
Cdd:NF041483   221 ERLL--NAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ------------EAEEALREARAEAEKVVA 286

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  781 EAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEkpEAETEAEGLNSEAETEA 850
Cdd:NF041483   287 EAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALA--DARAEAEKLVAEAAEKA 354
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
269-393 4.89e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 46.78  E-value: 4.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 269 DTTLqvKKAFFALVANGVRAAPLWETKKQsFVGMLTITDFINILHRYYKSPMVqiYELEEHKIE---TwrelylqetfKP 345
Cdd:COG3448    18 DTTL--REALELMREHGIRGLPVVDEDGR-LVGIVTERDLLRALLPDRLDELE--ERLLDLPVEdvmT----------RP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1840277627 346 LVNITPDASIFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFL 393
Cdd:COG3448    83 VVTVTPDTPLEEAAELMLEHGIHRLPVVDD-DGRLVGIVTRTDLLRAL 129
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 447-851 5.40e-06

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 50.40  E-value: 5.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  447 VVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALRHRSQYFEGVMKCNRHETLETIVDRIVKAEVHRLVVVDENARI 526
Cdd:COG5271    221 LAAEEGASAVVEEEDASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAAD 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  527 VGIVSLSDILQALVLTPAGINRKSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEAD 606
Cdd:COG5271    301 PESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGAD 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  607 VEEGTPEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEA--EGMKDEAEVEGMKDEAEAEG 684
Cdd:COG5271    381 TDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSaeDDIATDEEADSLADEEEEAE 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  685 MKDEAEAEGMKDEAEAEGMKSETEAEVMKFEAETEAEGmKSETEVETDGMKPEAEAEAEEMK---SETEVKTDGMKPEAE 761
Cdd:COG5271    461 AELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEE-DAEAEADSDELTAEETSADDGADtdaAADPEDSDEDALEDE 539

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  762 NETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGV--KPEGETEAEKPEAETEA 839
Cdd:COG5271    540 TEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASedEAAEEEEADDDEADADA 619

                          410
                   ....*....|..
gi 1840277627  840 EGLNSEAETEAE 851
Cdd:COG5271    620 DGAADEEETEEE 631
PTZ00121 PTZ00121
MAEBL; Provisional
 548-853 5.69e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 5.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  548 RKSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVE----GIVEADVEEGTPEETAAEGMK-- 621
Cdd:PTZ00121  1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdknmALRKAEEAKKAEEARIEEVMKly 1601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  622 -SEAVTEAEVMKDEAE----AEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEA-EGMKDEAEAEGMK 695
Cdd:PTZ00121  1602 eEEKKMKAEEAKKAEEakikAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkKAEEDKKKAEEAK 1681

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  696 DEAE-----AEGMKSETE-----AEVMKFEAET--EAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDgmkPEAENE 763
Cdd:PTZ00121  1682 KAEEdekkaAEALKKEAEeakkaEELKKKEAEEkkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD---EEEKKK 1758

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  764 TEEMKPEAETEAEGVKPEAETEaegVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKP-----EGETEAEKPEAETE 838
Cdd:PTZ00121  1759 IAHLKKEEEKKAEEIRKEKEAV---IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEgnlviNDSKEMEDSAIKEV 1835

                          330
                   ....*....|....*
gi 1840277627  839 AEGLNSEAETEAEVE 853
Cdd:PTZ00121  1836 ADSKNMQLEEADAFE 1850
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 423-536 6.22e-06

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: 45.99  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 423 FIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVIN-LAAEKTynNLDITVTQALRHRsqyFEgvmKCNRHET 501
Cdd:cd04608    14 TVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSsLLAGRA--QPSDPVSKAMYKQ---FK---QVDLDTP 85

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1840277627 502 LETiVDRIVKaEVHRLVVVDENARIVGIVSLSDIL 536
Cdd:cd04608    86 LGA-LSRILE-RDHFALVVDGQGKVLGIVTRIDLL 118
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 344-466 6.92e-06

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: 341408 [Multi-domain]  Cd Length: 112  Bit Score: 45.64  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDPVSGNALYILTHKRILKFLQLFVCEMPKPAFMKQnleeltigtyhDIAF 423
Cdd:cd17772     2 SPVISVEPDTTIAEAAELMTRYNINALPVVDGGTGRLVGIITRQVAEKAIYHGLGDLPVSEYMTT-----------EFAT 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVINL 466
Cdd:cd17772    71 VTPDAPLSEIQEIIVEQRQRLVPVVED-GRLVGVITRTDLLNL 112
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 344-459 7.14e-06

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: 45.69  E-value: 7.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFLqlfvcempkpAFMKQNLEEltIGTyHDIAF 423
Cdd:cd04605     8 KDVATIREDISIEEAAKIMIDKNVTHLPVVSE-DGKLIGIVTSWDISKAV----------ALKKDSLEE--IMT-RNVIT 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYS 459
Cdd:cd04605    74 ARPDEPIELAARKMEKHNISALPVVDDDRRVIGIIT 109
PHA03169 PHA03169
hypothetical protein; Provisional
 548-764 9.45e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.20  E-value: 9.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 548 RKSSQPQPPPEAQTSPEALVEAEPEANTEvvvvEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTE 627
Cdd:PHA03169   41 ARAAKPAPPAPTTSGPQVRAVAEQGHRQT----ESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELAS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 628 AEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSET 707
Cdd:PHA03169  117 GLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSE 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1840277627 708 EAEvmkfEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENET 764
Cdd:PHA03169  197 TPT----SSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPG 249
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 418-536 1.13e-05

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: 45.03  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 418 YHDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINlaaektynnldiTVTQALRHrsqyfEGVMKCN 497
Cdd:cd04597     4 YDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDIAR------------TVDYIMTK-----DNLIVFK 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1840277627 498 RHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDIL 536
Cdd:cd04597    67 EDDYLDEVKEIMLNTNFRNYPVVDENNKFLGTISRKHLI 105
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 424-538 1.76e-05

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: 44.41  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVinlaaEKtynnlditvtqALRHRSQY--FEGVMKCN---- 497
Cdd:cd04595     7 VSPDTTIEEARKIMLRYGHTGLPVVED-GKLVGIISRRDV-----DK-----------AKHHGLGHapVKGYMSTNviti 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1840277627 498 -RHETLETIVDRIVKAEVHRLVVVDENaRIVGIVSLSDILQA 538
Cdd:cd04595    70 dPDTSLEEAQELMVEHDIGRLPVVEEG-KLVGIVTRSDVLRY 110
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 344-393 2.15e-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: 2.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFL 393
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRAL 55
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 549-721 2.31e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.88  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 549 KSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEH-VAEPATTVEGIVEADVEEGTPEETAAEGMKSEA-VT 626
Cdd:PRK09510   75 KRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKkQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAeAK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 627 EAEVMKDEAEAEGMKDEAEAEGMKDEAEAegmKDEAEAEGMKDEAEVEGMKDEAEAEGmKDEAEAEGmKDEAEAEGMKSE 706
Cdd:PRK09510  155 RAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEAKK-KAAAEAKK-KAAAEAKAAAAK 229

                         170
                  ....*....|....*
gi 1840277627 707 TEAEVmKFEAETEAE 721
Cdd:PRK09510  230 AAAEA-KAAAEKAAA 243
rne PRK10811
ribonuclease E; Reviewed
 552-702 2.73e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 48.11  E-value: 2.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  552 QPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAegmkSEAVTEAEVM 631
Cdd:PRK10811   865 QVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQV----ITESDVAVAQ 940

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840277627  632 KDEAEAEGMKDEAEAEgmKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEG 702
Cdd:PRK10811   941 EVAEHAEPVVEPQDET--ADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEA 1009
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 265-313 2.97e-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: 42.11  E-value: 2.97e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1840277627  265 LVVFDTTLQVKKAFFALVANGVRAAPLWeTKKQSFVGMLTITDFINILH 313
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVV-DEEGRLVGIVTRRDIIKALA 49
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 420-539 3.37e-05

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: 44.53  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 420 DIAFIHPDTPIIKALNIFVDRRVSALPVVDE-SGKVVDIYSKFDVI---------NLAAEKTYNNLDITVTQALRHRSQy 489
Cdd:cd17779     9 DVITIPPTTTIIGAIKTMTEKGFRRLPVADAgTKRLEGIVTSMDIVdflgggskyNLVEKKHNGNLLAAINEPVREIMT- 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1840277627 490 fEGVMKCNRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQAL 539
Cdd:cd17779    88 -RDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 420-539 3.45e-05

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: 44.24  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 420 DIAFIHPDTPIIKALNIFVDRRVSALPVVDeSGKVVDIYSKFDVI-NLAAEKTYNnlDITVTQALRHRSQYFEGVMKCNR 498
Cdd:cd17778     9 PVVTIYPDDTLKEAMELMVTRGFRRLPVVS-GGKLVGIVTAMDIVkYFGSHEAKK--RLTTGDIDEAYSTPVEEIMSKEV 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1840277627 499 H-----ETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQAL 539
Cdd:cd17778    86 VtiepdADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIAL 131
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 424-535 3.46e-05

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: 44.48  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDV-----INLAAEKTYNNLDITVTQALRHRSQY----FEGVM 494
Cdd:cd04640    10 IDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDIlgekpLKIVQERGIPREELLVADVMTPRDKLealdYEDVA 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1840277627 495 KCNRHETLETIVDrivKAEVHRLVV---VDENARIVGIVSLSDI 535
Cdd:cd04640    90 HARVGDVVETLKA---SGRQHALVVdrdEDGRQEVRGIFSASQI 130
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 424-538 5.21e-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: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVinlaAEKTYNNlditVTQALRHRSQYfegVMkcnRHETLE 503
Cdd:cd04594     7 VSAYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDI----ENKSPGK----VGKYVVRGSPY---VT---PTSSLE 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1840277627 504 TIVDRIVKAEVhRLVVVDENARIVGIVSLSDILQA 538
Cdd:cd04594    73 EAWEIMMRNKS-RWVAVVEKGKFLGIITLDDLLEA 106
rne PRK10811
ribonuclease E; Reviewed
 506-675 6.55e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 46.96  E-value: 6.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  506 VDRIVKAEVHRLVVVDENARIVGIVSlsdilqalVLTPAGINRKSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPD 585
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQVQPVVAE--------VPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPE 918

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  586 TETEEHVAEPATTVEGIVEADVEEG-TPEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEA 664
Cdd:PRK10811   919 VIAAPVTEQPQVITESDVAVAQEVAeHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVE 998

                          170
                   ....*....|.
gi 1840277627  665 EGMKDEAEVEG 675
Cdd:PRK10811   999 PEVAPAQVPEA 1009
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 344-464 6.78e-05

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: 43.47  E-value: 6.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 344 KPLVNITPDASIFDAVYSLIKNKIHRLPVIDpvSGNALYILTHKRILKFLQLFVCEMPKP-----AFMKQNLEELTigtY 418
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVS--GGKLVGIVTAMDIVKYFGSHEAKKRLTtgdidEAYSTPVEEIM---S 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVI 464
Cdd:cd17778    83 KEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 16-215 6.78e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 6.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627   16 PRKNRMLRLNMPDLSSFAMPFLEGDASHVNKDNIPKGDGSCQSASPTKGFFSR-GPFSRPSSPKSA----PARTRNSPSS 90
Cdd:PHA03307   207 PRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRpAPITLPTRIWEAsgwnGPSSRPGPAS 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627   91 PKTifPYPSSHQDSPPKSPRRLSFSGIFRSSSRESKDSTSNSTSPVSIKLFSRARKAS-----------GVSSPPLTPPT 159
Cdd:PHA03307   287 SSS--SPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSpgpspsrspspSRPPPPADPSS 364

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1840277627  160 QVAKQPPAFLLEAYRIEPERPETRMRSYS-SPPDTGQHL--RLPCAKPATTPSAPIATS 215
Cdd:PHA03307   365 PRKRPRPSRAPSSPAASAGRPTRRRARAAvAGRARRRDAtgRFPAGRPRPSPLDAGAAS 423
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
613-735 7.12e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.40  E-value: 7.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 613 EETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKdeaEVEGMKDEAEAEGMKDEAEAE 692
Cdd:COG2268   222 EAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAER---EVQRQLEIAEREREIELQEKE 298

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1840277627 693 GMKDEAEAE---GMKSETEAEVMKFEAETEAEGMKSETEVETDGMK 735
Cdd:COG2268   299 AEREEAELEadvRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKR 344
rne PRK10811
ribonuclease E; Reviewed
 550-684 8.03e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 46.57  E-value: 8.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  550 SSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAfPDTETEEHVAE--PATTVEGIVE-----ADVEEGTPEETAAEgmKS 622
Cdd:PRK10811   871 AEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAE-PQPEEVVVVETthPEVIAAPVTEqpqviTESDVAVAQEVAEH--AE 947

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840277627  623 EAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEG 684
Cdd:PRK10811   948 PVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEA 1009
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 493-540 8.36e-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: 42.62  E-value: 8.36e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1840277627 493 VMKCNRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQALV 540
Cdd:cd02205     4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALV 51
rne PRK10811
ribonuclease E; Reviewed
 551-720 8.59e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 46.57  E-value: 8.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  551 SQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTEteehVAEPATTVEGIVEADVEEGTPEETAAegmksEAVTEAEV 630
Cdd:PRK10811   844 RYPVVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVE----PVVSAPVVEAVAEVVEEPVVVAEPQP-----EEVVVVET 914

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  631 MKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAE-----AEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKS 705
Cdd:PRK10811   915 THPEVIAAPVTEQPQVITESDVAVAQEVAEHAEpvvepQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETV 994

                          170
                   ....*....|....*
gi 1840277627  706 ETEAEVMKFEAETEA 720
Cdd:PRK10811   995 TAVEPEVAPAQVPEA 1009
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 613-810 9.20e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.95  E-value: 9.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 613 EETAAEGMKSEAVTEAEVMKDEAE---AEGMKDEAEaEGMKDEAEAEGMKDEA---EAEGMKDEAEVEGMKDEAEAEgmk 686
Cdd:PRK09510   86 QQQAEELQQKQAAEQERLKQLEKErlaAQEQKKQAE-EAAKQAALKQKQAEEAaakAAAAAKAKAEAEAKRAAAAAK--- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 687 dEAEAEGMKDEAEAEGMKSETEAevmKFEAETEAegmksetevetdgmkpeaeaeaeEMKSETEVKTDGMKPEAENETEE 766
Cdd:PRK09510  162 -KAAAEAKKKAEAEAAKKAAAEA---KKKAEAEA-----------------------AAKAAAEAKKKAEAEAKKKAAAE 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1840277627 767 MKPEAETEAEGVKPEAETEAegvKPEAETEAEGVKPEAETEAEG 810
Cdd:PRK09510  215 AKKKAAAEAKAAAAKAAAEA---KAAAEKAAAAKAAEKAAAAKA 255
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 568-858 1.26e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 45.78  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  568 EAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAE 647
Cdd:COG5271    424 ASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAE 503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  648 GMKDEAEAEG----MKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGmkdEAEAEGMKSETEAEVMKFEAETEAEGM 723
Cdd:COG5271    504 ADSDELTAEEtsadDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDA---DETDEPEATAEEDEPDEAEAETEDATE 580

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  724 KSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENET--------EEMKPEAETEAEGVKPEAETEAEGVKPEAET 795
Cdd:COG5271    581 NADADETEESADESEEAEASEDEAAEEEEADDDEADADADGaadeeeteEEAAEDEAAEPETDASEAADEDADAETEAEA 660

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1840277627  796 EAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAEVEFKADV 858
Cdd:COG5271    661 SADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEEADTEADG 723
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 432-538 1.28e-04

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: 41.95  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 432 KALNIFVDRRVSALPVV-DESGKVVDIYSKFDVINlaaektynNLDITVTQALRHRSqyfegVMKCNRHETLETIVDRIV 510
Cdd:cd04638    16 DVLEILKKKAISGVPVVkKETGKLVGIVTRKDLLR--------NPDEEQIALLMSRD-----PITISPDDTLSEAAELML 82

                          90       100
                  ....*....|....*....|....*...
gi 1840277627 511 KAEVHRLVVVDENaRIVGIVSLSDILQA 538
Cdd:cd04638    83 EHNIRRVPVVDDD-KLVGIVTVADLVRA 109
Med26_M pfam15694
Mediator complex subunit 26 middle domain; Med26_M is the middle domain of subunit 26 of ...
 72-243 1.29e-04

Mediator complex subunit 26 middle domain; Med26_M is the middle domain of subunit 26 of Mediator. Med19 and Med26 act synergistically to mediate the interaction between REST (a Kruppel-type zinc finger transcription factor that binds to a 21-bp RE1 silencing element present in over 900 human genes) and Mediator.


Pssm-ID: 464807 [Multi-domain]  Cd Length: 255  Bit Score: 44.48  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  72 SRPSSPksAPARTRNSPSSPKTIFPYPSSHQDS-----PPKSPRRLSFS------GIF--RSSSRESKDSTSnstSPVSI 138
Cdd:pfam15694  51 PHTSSP--GLGKPPSTSSLLKAAVLQQQARLDEtggppQPKSPRCSSFSprnsrhETFarRSSTYAPKGSVP---SPSPR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 139 KLFSRARKASGVSSP-PLTPPTQVAK--QPPAFLLEAYRIEPERPETrmRSYSSPPDTGQHLRLPCAKP-ATTPSAPIAT 214
Cdd:pfam15694 126 SQVLDAQVPSPLPLSqPSTPPVQAKRleKPPQSSPESSQHWLEQSDS--ESHQRHQDGSATLLSQSVSPgCKTPLHPGEN 203

                         170       180
                  ....*....|....*....|....*....
gi 1840277627 215 SRSRTVhglTEGMLEKLDLEDEAVEESES 243
Cdd:pfam15694 204 SLPHLG---FSPDSSKADSDGAASSGSDS 229
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-465 1.66e-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: 41.71  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 345 PLVNITPDASIFDAVYSLIKNKIHRLPVIDpvSGNALYILTHKRILKFLQLFVCEMPKPAFMKQNleeltigtyhdIAFI 424
Cdd:cd04595     3 PVKTVSPDTTIEEARKIMLRYGHTGLPVVE--DGKLVGIISRRDVDKAKHHGLGHAPVKGYMSTN-----------VITI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1840277627 425 HPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVIN 465
Cdd:cd04595    70 DPDTSLEEAQELMVEHDIGRLPVVEE-GKLVGIVTRSDVLR 109
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 604-717 3.73e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 604 EADVEEGTPEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAegmKDEAEAEGMKDEAEVEGMKDEAEAE 683
Cdd:PRK09510  148 KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA---KKKAEAEAKKKAAAEAKKKAAAEAK 224

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1840277627 684 GMKDEAEAEGMKDEAEAEGMKSETEAEVMKFEAE 717
Cdd:PRK09510  225 AAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 416-538 4.44e-04

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: 43.92  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 416 GTYHDIAFIHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVinlaaeKTYNNLDITVTQalrhrsqyfegVMK 495
Cdd:pfam00478  85 GMITDPVTLSPDATVADALALMERYGISGVPVVDD-GKLVGIVTNRDL------RFETDLSQPVSE-----------VMT 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1840277627 496 CNR------HETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQA 538
Cdd:pfam00478 147 KENlvtapeGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDIEKA 195
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
249-394 5.33e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 41.05  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 249 FMKSHKCYDIVpTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWETKKQsFVGMLTITDFINilhryyKSPMVQIYELEE 328
Cdd:COG4109    12 FKEILLVEDIM-TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGR-LVGIVTSKDILG------KDDDTPIEDVMT 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1840277627 329 HKIETwrelylqetfkplvnITPDASIFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFLQ 394
Cdd:COG4109    84 KNPIT---------------VTPDTSLASAAHKMIWEGIELLPVVDD-DGRLLGIISRQDVLKALQ 133
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 612-703 5.54e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 612 PEETAAEGMKSEAVTEAEVMKDEAEAEGmKDEAEAEgmkDEAEAEGMKDEAEAEGMKDEAEVEgMKDEAEAEgMKDEAEA 691
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEA-KAKAEAE---AKAKAEEAKAKAEAAKAKAAAEAA-AKAEAEAA-AAAAAEA 225

                          90
                  ....*....|..
gi 1840277627 692 EGMKDEAEAEGM 703
Cdd:TIGR02794 226 ERKADEAELGDI 237
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 423-457 5.73e-04

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: 40.65  E-value: 5.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1840277627 423 FIHPDTPIIKALNIFVDRRVSALPVVDESGKVVDI 457
Cdd:cd17781    72 CVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGV 106
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 549-680 5.94e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.43  E-value: 5.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 549 KSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTEA 628
Cdd:PRK13108  313 SAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDAE 392

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1840277627 629 EVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAeaeGMKDEAEVEGMKDEA 680
Cdd:PRK13108  393 AASAAPEEPAALASEAHDETEPEVPEKAAPIPDP---AKPDELAVAGPGDDP 441
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
499-545 6.58e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 40.67  E-value: 6.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1840277627 499 HETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQALVLTPAG 545
Cdd:COG4109    33 DDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDTPIE 79
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 555-853 6.66e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 43.46  E-value: 6.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  555 PPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTEAEVMKDE 634
Cdd:COG5271    528 PEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEE 607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  635 AEAEGMKDEAEAEGMKDEAEAEG--MKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEAEVM 712
Cdd:COG5271    608 EEADDDEADADADGAADEEETEEeaAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAA 687

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  713 KFEAETEaegmkSETEVETDGMKPEAEAEAEEMKSETEvktDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPE 792
Cdd:COG5271    688 AAEASDD-----EEETEEADEDAETASEEADAEEADTE---ADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAE 759

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840277627  793 AETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAEVE 853
Cdd:COG5271    760 EAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEE 820
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 411-539 8.93e-04

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: 40.40  E-value: 8.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 411 EELTIGTYHDIAFIHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVINLAAEKTYNNLditvtqaLRHRSQYf 490
Cdd:cd17777     2 KELMIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDE-NKLEGILSARDLVSYLGGGCLFKI-------VESRHQG- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1840277627 491 eGVMKCNRHETLETIVDR-------------IVKAEVHR----LVVVDENARIVGIVSLSDILQAL 539
Cdd:cd17777    73 -DLYSALNREVVETIMTPnpvyvyedsdlieALTIMVTRgigsLPVVDRDGRPVGIVTERDLVLYL 137
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 534-720 9.03e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.53  E-value: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 534 DILQALVLTPAGIN------RKSSQPQPPPEAQTSPEALVEAEPEAntevvvveafpdtetEEHVAEPATTVEGIVEADV 607
Cdd:TIGR02794  36 EIIQAVLVDPGAVAqqanriQQQKKPAAKKEQERQKKLEQQAEEAE---------------KQRAAEQARQKELEQRAAA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 608 EEGTPEETAAEGMKSEAVTEAEVMKDEAEAE-GMKDEAEAEGMKDE-----AEAEGMKDEAEAEgmKDEAEVEGMKDEAE 681
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEaKAKAEAEAERKAKEeaakqAEEEAKAKAAAEA--KKKAEEAKKKAEAE 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1840277627 682 AEGMKD---EAEAEGMKDEAEAEGMKSETEAEvMKFEAETEA 720
Cdd:TIGR02794 179 AKAKAEaeaKAKAEEAKAKAEAAKAKAAAEAA-AKAEAEAAA 219
PTZ00491 PTZ00491
major vault protein; Provisional
 627-733 1.03e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 42.70  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 627 EAEVMKDEAEAEGMKD---EAEAEGMKDE------AEAEGmkdEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEG--MK 695
Cdd:PTZ00491  684 ERQKMHDKAKAEEQRTkllELQAESAAVEssgqsrAEALA---EAEARLIEAEAEVEQAELRAKALRIEAEAELEKlrKR 760

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1840277627 696 DEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVETDG 733
Cdd:PTZ00491  761 QELELEYEQAQNELEIAKAKELADIEATKFERIVEALG 798
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 426-539 1.07e-03

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: 39.71  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 426 PDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDV-INLAAEKTynNLDITVTQAL-------RHRSQYFEGVMKCN 497
Cdd:cd17784     9 PNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLgHNLILDKY--ELGTTVEEVMvkdvatvHPDETLLEAIKKMD 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1840277627 498 RHETLETIVDrivkaevhRLVVVDeNARIVGIVSLSDILQAL 539
Cdd:cd17784    87 SNAPDEEIIN--------QLPVVD-DGKLVGIISDGDIIRAI 119
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
 759-840 1.08e-03

Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 39.51  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 759 EAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEgvkPEAETEAEGVKPEGETEAEKPEAETE 838
Cdd:COG2811    12 EAEEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEEAQERLEEAR---EEAEAEAEEIIEEGEKEAEALKKKAE 88


                  ..
gi 1840277627 839 AE 840
Cdd:COG2811    89 DK 90
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 627-701 1.12e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.54  E-value: 1.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1840277627 627 EAEVMKDEAEAEGMKDEAEAegMKDEAEAEGMKDEAEAEGMKDEAEVEGmkdEAEAEGMKDEAEAEG--MKDEAEAE 701
Cdd:COG0711    33 QEKIADGLAEAERAKEEAEA--ALAEYEEKLAEARAEAAEIIAEARKEA---EAIAEEAKAEAEAEAerIIAQAEAE 104
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 424-455 1.18e-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: 39.67  E-value: 1.18e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDESGKVV 455
Cdd:cd04604    83 ISPDALAAEALELMEEHKITVLPVVDEDGKPV 114
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 760-812 1.25e-03

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 41.75  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1840277627 760 AENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVK 812
Cdd:COG0330   179 AEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFR 231
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 783-850 1.31e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 40.75  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1840277627 783 ETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKpEAETEAEGLNSEAETEA 850
Cdd:PRK02292    4 ETVVEDIRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAER-EIEQLREQELSSAKLEA 70
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 515-565 1.55e-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: 39.47  E-value: 1.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1840277627 515 HR---LVVVDENARIVGIVSLSDILQALVLTPAGINRKSSQPQPPPEAQTSPEA 565
Cdd:cd04600    24 HRikaLPVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLGLRRDRPETV 77
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 424-536 1.69e-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: 38.86  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 424 IHPDTPIIKALNIFVDRRVSALPVVDEsGKVVDIYSKFDVINLAAektyNNLditVTQALRhrsqyfEGVMKCNRHETLE 503
Cdd:cd04599     8 ISPLDSVARAAALMERQRIGGLPVVEN-GKLVGIITSRDVRRAHP----NRL---VADAMS------RNVVTISPEASLW 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1840277627 504 TIVDRIVKAEVHRLVVVDENaRIVGIVSLSDIL 536
Cdd:cd04599    74 EAKELMEEHGIERLVVVEEG-RLVGIITKSTLY 105
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 496-541 1.84e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.04  E-value: 1.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1840277627 496 CNRHETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQALVL 541
Cdd:COG2905    12 VSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLA 57
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 768-849 2.13e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 41.50  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 768 KPEAETEAEGVKPEAEtEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPE---GETEAEKPEAETEAEGLNS 844
Cdd:PRK13108  362 AVEETSEADIEREQPG-DLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEkaaPIPDPAKPDELAVAGPGDD 440


                  ....*
gi 1840277627 845 EAETE 849
Cdd:PRK13108  441 PAEPD 445
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 550-858 2.17e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 41.92  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  550 SSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFP-DTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTEA 628
Cdd:COG5271    594 SEEAEASEDEAAEEEEADDDEADADADGAADEEETeEEAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDES 673

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  629 EVMKDEAEAEGmkDEAEAEGMKDEAEA-EGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSET 707
Cdd:COG5271    674 ETSSEDAEEDA--DAAAAEASDDEEETeEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADA 751

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  708 EAEVMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAE--TEAEGVKPEAETE 785
Cdd:COG5271    752 EEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEadEEEDLDGEDEETA 831

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1840277627  786 AEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAEVEFKADV 858
Cdd:COG5271    832 DEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAA 904
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 349-465 2.18e-03

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: 38.48  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 349 ITPDASIFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFLQLFVcempkpafMKQNLeeltigtyhdIAFIHPDT 428
Cdd:cd04597    10 LSPETSIKDAWNLMDENNLKTLPVTDD-NGKLIGLLSISDIARTVDYIM--------TKDNL----------IVFKEDDY 70

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1840277627 429 -PIIKalNIFVDRRVSALPVVDESGKVVDIYSKFDVIN 465
Cdd:cd04597    71 lDEVK--EIMLNTNFRNYPVVDENNKFLGTISRKHLIN 106
PTZ00491 PTZ00491
major vault protein; Provisional
 679-841 2.29e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 41.93  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 679 EAEA--EGMKDEAEAEG------MKDEAEAEgmksETEAEVMKFEAETEAegmkseteVETDGMKpeaeaeaeemksete 750
Cdd:PTZ00491  665 EAAArhQAELLEQEARGrlerqkMHDKAKAE----EQRTKLLELQAESAA--------VESSGQS--------------- 717

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 751 vktdgmKPEAENETEEMKPEAETEAEgvkpEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEA 830
Cdd:PTZ00491  718 ------RAEALAEAEARLIEAEAEVE----QAELRAKALRIEAEAELEKLRKRQELELEYEQAQNELEIAKAKELADIEA 787

                         170
                  ....*....|.
gi 1840277627 831 EKPEAETEAEG 841
Cdd:PTZ00491  788 TKFERIVEALG 798
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 653-832 2.57e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 41.12  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 653 AEAEGMKDEAEAEGMKDEAEVEGMKDEA-EAEGMKDEAEAEGMKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEvET 731
Cdd:PRK13108  291 VVDEALEREPAELAAAAVASAASAVGPVgPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETS-EA 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 732 DGMKPEAEAeaeemksetevkTDGMKPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPE-AETEAEGVKPEaETEAEG 810
Cdd:PRK13108  370 DIEREQPGD------------LAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEkAAPIPDPAKPD-ELAVAG 436

                         170       180
                  ....*....|....*....|..
gi 1840277627 811 VKPEAeTEAEGVKPEGETEAEK 832
Cdd:PRK13108  437 PGDDP-AEPDGIRRQDDFSSRR 457
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 ...
 426-536 2.62e-03

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: 38.45  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 426 PDTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYnNLDITVTQ-------ALRHRSQYFEGVMKCNR 498
Cdd:cd17771    11 PDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQI-DLDAPISEvmtpdpvRLPPSASAFEAALLMAE 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1840277627 499 HetletivdrivkaEVHRLVVVDeNARIVGIVSLSDIL 536
Cdd:cd17771    90 H-------------GFRHVCVVD-NGRLVGVVSERDLF 113
PTZ00491 PTZ00491
major vault protein; Provisional
 634-730 2.80e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 41.54  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 634 EAEA--EGMKDEAEAEG------MKDEAEAEGMKD---EAEAEGMKDEAE---VEGMKDEAEAEGMKDEAEAEGMKDEAE 699
Cdd:PTZ00491  665 EAAArhQAELLEQEARGrlerqkMHDKAKAEEQRTkllELQAESAAVESSgqsRAEALAEAEARLIEAEAEVEQAELRAK 744

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1840277627 700 AEGMKSETEAEVMKFEAETEAEGMKSETEVE 730
Cdd:PTZ00491  745 ALRIEAEAELEKLRKRQELELEYEQAQNELE 775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 72-213 2.87e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627   72 SRPSSPKSAPARTRNSPSSPKTIFPYPSSHQDSPPKSPR-----RLSFSGIFRSSSRESKDSTSNSTSPVSIKlfSRARK 146
Cdd:PHA03247  2805 ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgppppSLPLGGSVAPGGDVRRRPPSRSPAAKPAA--PARPP 2882

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  147 ASGVSSPPLTPPTQVAKQPPaflleayrIEPER---PETRMRSYSSPPDTGQHLRLPCAKPATTPSAPIA 213
Cdd:PHA03247  2883 VRRLARPAVSRSTESFALPP--------DQPERppqPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 572-853 3.37e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 41.15  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  572 EANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEetaaegmKSEAVTEAEVMKDEAEAEG--MKDEAEAEGM 649
Cdd:COG5271    570 EAEAETEDATENADADETEESADESEEAEASEDEAAEEEEAD-------DDEADADADGAADEEETEEeaAEDEAAEPET 642

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  650 KDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGmKSETEAEVMKFEAETEAEGMKSETEV 729
Cdd:COG5271    643 DASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDE-EETEEADEDAETASEEADAEEADTEA 721

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  730 ETDGmKPEAEAEAEEMKSETEVKTDGMKPEAENETEEMKPEAETEAEGVKPEAETE-AEGVKPEAETEAEGVKPEAETEA 808
Cdd:COG5271    722 DGTA-EEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEkADAEEAATDEEAEAAAEEKEKVA 800

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1840277627  809 EGVKPEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAEVE 853
Cdd:COG5271    801 DEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAED 845
PTZ00121 PTZ00121
MAEBL; Provisional
 600-857 3.43e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  600 EGIVEADVEEGTPEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEA-EGMKDEAEAEGMKDEA--EAEGMKDEAEVEGM 676
Cdd:PTZ00121  1057 EGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAkKTETGKAEEARKAEEAkkKAEDARKAEEARKA 1136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  677 KDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEA----EVMKFEAETEAEGMKSETEVET--DGMKPEAEAEAEEMKSETE 750
Cdd:PTZ00121  1137 EDARKAEEARKAEDAKRVEIARKAEDARKAEEArkaeDAKKAEAARKAEEVRKAEELRKaeDARKAEAARKAEEERKAEE 1216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  751 VK--TDGMKPEAENETEEMKPEAEtEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPegET 828
Cdd:PTZ00121  1217 ARkaEDAKKAEAVKKAEEAKKDAE-EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK--AD 1293

                          250       260
                   ....*....|....*....|....*....
gi 1840277627  829 EAEKPEAETEAEglnsEAETEAEVEFKAD 857
Cdd:PTZ00121  1294 EAKKAEEKKKAD----EAKKKAEEAKKAD 1318
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 500-539 3.77e-03

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: 38.67  E-value: 3.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1840277627 500 ETLETIVDRIVKAEVHRLVVVDENARIVGIVSLSDILQAL 539
Cdd:cd17774    86 DSLWTAHQLMQQRRIRRLVVVGEQGELLGIVTQTSLLQAL 125
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 347-455 3.92e-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: 40.83  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 347 VNITPDASIFDAVYSLIKNKIHRLPVIDpvSGNALYILThKRILKFLQlfvcempkpaFMKQNLEEltIGTYHDIAFIHP 426
Cdd:pfam00478  91 VTLSPDATVADALALMERYGISGVPVVD--DGKLVGIVT-NRDLRFET----------DLSQPVSE--VMTKENLVTAPE 155

                          90       100
                  ....*....|....*....|....*....
gi 1840277627 427 DTPIIKALNIFVDRRVSALPVVDESGKVV 455
Cdd:pfam00478 156 GTTLEEAKEILHKHKIEKLPVVDDNGRLV 184
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 551-858 4.17e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 41.15  E-value: 4.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  551 SQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTEAEV 630
Cdd:COG5271    628 TEEEAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAET 707

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  631 M---KDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEGMKDEAEAEGMKSET 707
Cdd:COG5271    708 AseeADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDE 787

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  708 EAEVMKFEAETEAEGMKSETEVETDGMKPEAEAEAEEMKSETEVKTDGMKPEAENETEEmKPEAETEAEGVKPEAETEAE 787
Cdd:COG5271    788 EAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDD-EEDDDAAAAKDVDADLDLDA 866

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840277627  788 GVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKPEAETEAEGLNSEAETEAEVEFKADV 858
Cdd:COG5271    867 DLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEE 937
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 760-857 4.31e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 40.73  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 760 AENETEEMKPEAETEAEGVKPEAEtEAEGVKPEAETEA---EGVKPEAETEAEGV------------KPEAETEAEGVKP 824
Cdd:PRK13108  296 LEREPAELAAAAVASAASAVGPVG-PGEPNQPDDVAEAvkaEVAEVTDEVAAESVvqvadrdgestpAVEETSEADIERE 374

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1840277627 825 E-GETEAEKPEAETEAEGLNSEAETEAEVEFKAD 857
Cdd:PRK13108  375 QpGDLAGQAPAAHQVDAEAASAAPEEPAALASEA 408
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
419-486 4.85e-03

Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 40.44  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDESGKVV------DIYskfDVINLAAEKTYNN---------LDITVTQAL 483
Cdd:COG2239   201 TDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVgiitvdDVV---DVIEEEATEDILKlagvsededLFASVLKLA 277


                  ...
gi 1840277627 484 RHR 486
Cdd:COG2239   278 RKR 280
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 772-820 5.05e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 39.21  E-value: 5.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1840277627 772 ETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAE 820
Cdd:PRK02292    4 ETVVEDIRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAE 52
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 589-736 5.34e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 40.35  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 589 EEHVAEP-ATTVEGIVEADVEEGTPEETAAEGMKSEAVTE-AEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEG 666
Cdd:PRK13108  292 VDEALERePAELAAAAVASAASAVGPVGPGEPNQPDDVAEaVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADI 371

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840277627 667 MKDEA-EVEGMKDEAEAEGMKDEAEAEGmKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVETDGMKP 736
Cdd:PRK13108  372 EREQPgDLAGQAPAAHQVDAEAASAAPE-EPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDP 441
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
 759-831 5.37e-03

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 36.75  E-value: 5.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1840277627 759 EAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEgvkPEAETEAEGVKPEGETEAE 831
Cdd:TIGR02926   6 KAEEDAEELIEEAEEERKQRIAEAREEARELLEEAEEEASKLGEEIIKEAE---EEIEKEAEKIREEGEKEIE 75
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 419-536 5.46e-03

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: 37.48  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 419 HDIAFIHPDTPIIKALNIFVDRRVSALPVVDES-GKVVDI-YSKfDVINLAAEktyNNLDITVTQALRhRSQYFEGVMKC 496
Cdd:cd04590    10 TDVVALDADATLEELLELILESGYSRFPVYEGDlDNIIGVlHVK-DLLAALLE---GREKLDLRALLR-PPLFVPETTPL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1840277627 497 nrHETLEtivdRIVKAEVHRLVVVDENARIVGIVSLSDIL 536
Cdd:cd04590    85 --DDLLE----EFRKERSHMAIVVDEYGGTAGIVTLEDIL 118
PHA03247 PHA03247
large tegument protein UL36; Provisional
 57-214 5.54e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 5.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627   57 QSASPTKGFFSRGPFSRPSSPKSAPartrnspssPKTIFPYPsshqdsPPKSPR-RLSFSGIFRSSSRESKDSTSNSTSP 135
Cdd:PHA03247  2594 QSARPRAPVDDRGDPRGPAPPSPLP---------PDTHAPDP------PPPSPSpAANEPDPHPPPTVPPPERPRDDPAP 2658

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  136 VSIKLFSRAR---KASGVSSPPLTPPTQVAKQPPAFLLEAYRIEPERPETRmrsySSPPDTGQHLRLPCAKPATTPSAPI 212
Cdd:PHA03247  2659 GRVSRPRRARrlgRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPE----PAPHALVSATPLPPGPAAARQASPA 2734


                   ..
gi 1840277627  213 AT 214
Cdd:PHA03247  2735 LP 2736
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 662-857 5.59e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.83  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 662 AEAEGMKDEAEVEGMKDEAEAEGMKDEAEAEgmkdEAEAEGMKSETEAEVMKFEAETEAEgMKSETEVETDGMKPeaeae 741
Cdd:TIGR02794  57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAE----QARQKELEQRAAAEKAAKQAEQAAK-QAEEKQKQAEEAKA----- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 742 aeemKSETEVKTdgmKPEAENE---TEEMKPEAETEAEG-VKPEAETEAEGVKPEAETEAegvKPEAETEAEGVKPEAET 817
Cdd:TIGR02794 127 ----KQAAEAKA---KAEAEAErkaKEEAAKQAEEEAKAkAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKA 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1840277627 818 EAEGVKPEGETEAEKpEAETEAeglnsEAETEAEVEFKAD 857
Cdd:TIGR02794 197 KAEAAKAKAAAEAAA-KAEAEA-----AAAAAAEAERKAD 230
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 40-220 5.65e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627   40 DASHVNKDNIPKGDGSCQSASPTKGFFSRGPFSRPSSPKSAPA-----RTRNSPSSPKTIFPYPSSHQDSPPKSPRRLSF 114
Cdd:PHA03307   133 DLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPlsspeETARAPSSPPAEPPPSTPPAAASPRPPRRSSP 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  115 SGIFRSSS-----RESKDSTSNSTSpVSIKLFSRARKASGVSSPPLTPPTQVAKQPPafllEAYRIEPERPETrmRSYSS 189
Cdd:PHA03307   213 ISASASSPapapgRSAADDAGASSS-DSSSSESSGCGWGPENECPLPRPAPITLPTR----IWEASGWNGPSS--RPGPA 285

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1840277627  190 PPDTGQHLRLPCAKPAtTPSAPIATSRSRTV 220
Cdd:PHA03307   286 SSSSSPRERSPSPSPS-SPGSGPAPSSPRAS 315
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 427-538 6.15e-03

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: 37.56  E-value: 6.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 427 DTPIIKALNIFVDRRVSALPVVDESGKVVDIYSKFDVINLAAEKTYnnLDITVTQALRHRSqyfegVMKCNRHETLETIV 506
Cdd:cd04613    11 GMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEEEL--WDLVVVKDLATTD-----VITVTPDDDLYTAL 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1840277627 507 DRIVKAEVHRLVVVDEN--ARIVGIVSLSDILQA 538
Cdd:cd04613    84 LKFTSTNLDQLPVVDDDdpGKVLGMLSRRDVIAA 117
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
 781-851 6.47e-03

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 36.75  E-value: 6.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840277627 781 EAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKpEAETEAEGLNSEAETEAE 851
Cdd:TIGR02926   6 KAEEDAEELIEEAEEERKQRIAEAREEARELLEEAEEEASKLGEEIIKEAEE-EIEKEAEKIREEGEKEIE 75
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 641-840 7.02e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.00  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 641 KDEAEAEGMKDEAE--AEGMKDEAE---AEGMKDEAEVEgmkdEAEAEGMKDEAEAEGMKDEAEaegmKSETEAEVMKFE 715
Cdd:NF033838  304 KKVAEAEKKVEEAKkkAKDQKEEDRrnyPTNTYKTLELE----IAESDVKVKEAELELVKEEAK----EPRNEEKIKQAK 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 716 AETEAEgmKSE-TEVEtdgmkpeaeaeaeemksetEVKTDGMKP--EAENETEEMKPEAETEAEGVKPEAETEAEGVKPE 792
Cdd:NF033838  376 AKVESK--KAEaTRLE-------------------KIKTDRKKAeeEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPK 434

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1840277627 793 AETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKPEAETEAE 840
Cdd:NF033838  435 PEKPAEQPKAEKPADQQAEEDYARRSEEEYNRLTQQQPPKTEKPAQPS 482
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 518-858 7.95e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 40.00  E-value: 7.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  518 VVVDENARIVGIVSLSDILQALVLTPAGINRKSSQPQPPPEAQTSPEALVEAEPEANTEVVVVEAFPDTETEEHVAEPAT 597
Cdd:COG5271    221 LAAEEGASAVVEEEDASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAAD 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  598 TVEGIVEADVEEGTPEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKD-EAEAEGMKDEAEVEGM 676
Cdd:COG5271    301 PESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDaEDEAAGEAADESEGAD 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  677 KDEAEAEGMKDEAEAEGMKDEAEAEGMKSETEAEVMKFEAETEAEGMKSETEVeTDGMKPEAEAEAEEMKSETEVKTDGM 756
Cdd:COG5271    381 TDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDES-TDVTSAEDDIATDEEADSLADEEEEA 459

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627  757 KPEAENETEEMKPEAETEAEGVKPEAETEAEGVKPEAET--EAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKPE 834
Cdd:COG5271    460 EAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEdaEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDE 539

                          330       340
                   ....*....|....*....|....
gi 1840277627  835 AETEAEGLNSEAETEAEVEFKADV 858
Cdd:COG5271    540 TEGEENAPGSDQDADETDEPEATA 563
rpsP PRK14521
30S ribosomal protein S16; Provisional
 759-840 8.91e-03

30S ribosomal protein S16; Provisional


Pssm-ID: 237744 [Multi-domain]  Cd Length: 186  Bit Score: 38.22  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 759 EAENETEEMKPEAETEAEGVK---PEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEAETEAEGVKPEGETEAEKPEA 835
Cdd:PRK14521   98 QAEAKFEAWKEEKEGKVNAKKdklSKAKKAAKKAALEAEKKVNEARAEAVAEKKAAEAAAVAAEEAAAAEEEEAEEAPAE 177


                  ....*
gi 1840277627 836 ETEAE 840
Cdd:PRK14521  178 EAPAE 182
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 588-849 9.84e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.06  E-value: 9.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 588 TEEHVAEPATTVEGIVEADVEEGTPEETAAEGMKSEAVTEAEVMKDEAEAEGMKDEAEAEGMKDEAEAEGMKDEAEAEGM 667
Cdd:TIGR02794  24 YHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 668 KDEAEvegmKDEAEAEGMKDEAEAEGMKDEAEAEgMKSETEAEV-MKFEAETEAEgmksetevetdgmkpeaeaeaeemk 746
Cdd:TIGR02794 104 AKQAE----QAAKQAEEKQKQAEEAKAKQAAEAK-AKAEAEAERkAKEEAAKQAE------------------------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840277627 747 setEVKTDGMKPEAENETEEMKPEAETEAegvKPEAETEAEGVKPEAETEAEGVKPEAETEAegvKPEAETEAEGVKpeg 826
Cdd:TIGR02794 154 ---EEAKAKAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKAKAEAAKAKAAAEA---AAKAEAEAAAAA--- 221

                         250       260
                  ....*....|....*....|....*.
gi 1840277627 827 ETEAEKPEAETEAE---GLNSEAETE 849
Cdd:TIGR02794 222 AAEAERKADEAELGdifGLASGSNAE 247
CBS_pair_bac_arch cd17785
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 497-541 9.96e-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: 341421 [Multi-domain]  Cd Length: 136  Bit Score: 37.25  E-value: 9.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1840277627 497 NRHETLETIVDRIVKAEVHRLV-VVDENARIVGIVSLSDILQALVL 541
Cdd:cd17785    16 HENTSIRDVIDKMIEDPKTRSVyVVDDDEKLLGIITLMELLKYIGY 61
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH