|
Name |
Accession |
Description |
Interval |
E-value |
| TlyC |
COG1253 |
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ... |
23-440 |
2.05e-170 |
|
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];
Pssm-ID: 440865 [Multi-domain] Cd Length: 435 Bit Score: 485.01 E-value: 2.05e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 23 NAFLAGAEMAFVSVNQGKINQLAEEGDRRAVKVVQLLDKSDDFLSTIQVGITFAGFLSSASAANTFVGYILPYLANIP-- 100
Cdd:COG1253 17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGlp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 101 --AAEILATAIVTVILSYISLVFGELFPKQVAIQIPEKYCLFSAGTISFLNKVFTPFVWLLTASTDVLKAIAPIDFTQRE 178
Cdd:COG1253 97 aaLAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 179 ERLTRSEMRKLIESGRNDGIIDMDEFRMMQGVLSLDSKLAKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDD 258
Cdd:COG1253 177 PAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEGD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 259 KDDILGIVHAKDVLREANRvgFENIQMEDIMREPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVI 338
Cdd:COG1253 257 LDDIVGVVHVKDLLRALLE--GEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 339 VGDIEDEYDEMSFKYKKVSDDTYIIDGSMPIDKFNQLFNAHIY-SGDSDTMAGIIIEQLGRFPQdtINESIQVDDYLFTT 417
Cdd:COG1253 335 VGEIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPeEEDYETLGGLVLEQLGRIPE--VGETVEVDGLRFEV 412
|
410 420
....*....|....*....|...
gi 1092610523 418 TDVDDGRIRKIKVHYQPREEDDE 440
Cdd:COG1253 413 LDMDGRRIDKVLVTRLPEEEEEE 435
|
|
| GldE |
TIGR03520 |
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ... |
24-430 |
1.09e-81 |
|
gliding motility-associated protein GldE; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldC is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. GldE was discovered because of its adjacency to GldD in F. johnsonii. Overexpression of GldE partially supresses the effects of a GldB point mutant suggesting that GldB and GldE interact. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Not all Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility and in fact some do not appear to express the gliding phenotype.
Pssm-ID: 274626 [Multi-domain] Cd Length: 407 Bit Score: 257.27 E-value: 1.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 24 AFLAGAEMAFVSVNQGKINQLAEEGDRRAVKVVQLLDKSDDFLSTIQVG---ITFAGFLSSASAANTFVGYIlpylaNIP 100
Cdd:TIGR03520 8 ALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIAnnfINIAIVLLFTSLSDNLFGSF-----NTE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 101 AAEILataIVTVILSYISLVFGELFPKQVAIQIPEKYCLFSAGTISFLNKVFTPFVWLLTASTDVLKAiapiDFTQREER 180
Cdd:TIGR03520 83 LLRFL---IEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHK----KFGKQKSN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 181 LTRSEMRKLIESGRNDGIIDmDEFRMMQGVLSLDSKLAKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDDKD 260
Cdd:TIGR03520 156 ISVDQLSQALELTDEEDTTK-EEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETID 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 261 DILGIVHAKDVLREANRvgfENIQMEDIMREPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVIVG 340
Cdd:TIGR03520 235 NITGVLYIKDLLPHLNK---KNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 341 DIEDEYDEMSFKYKKVSDDTYIIDGSMPIDKF-------NQLFNAhiYSGDSDTMAGIIIEQLGRFPQdtINESIQVDDY 413
Cdd:TIGR03520 312 DISDEFDDEDLIYSKIDDNNYVFEGKTSLKDFykilkleEDMFDE--VKGEAETLAGFLLEISGGFPK--KGEKITFENF 387
|
410
....*....|....*..
gi 1092610523 414 LFTTTDVDDGRIRKIKV 430
Cdd:TIGR03520 388 EFTIEAMDKKRIKQVKV 404
|
|
| PRK11573 |
PRK11573 |
hypothetical protein; Provisional |
24-430 |
4.48e-53 |
|
hypothetical protein; Provisional
Pssm-ID: 236933 [Multi-domain] Cd Length: 413 Bit Score: 183.03 E-value: 4.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 24 AFLAGAEMAFVSVNQGKINQLAEEGDRRAVKVVQLLDKSDDFLSTIQVGITFAGFLSSASAanTFVGYILPYLANIpaae 103
Cdd:PRK11573 6 AYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALG--TIVGMRLYGDAGV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 104 ilatAIVTVILSYISLVFGELFPKQVAIQIPEKYCLFSAGTISFLNKVFTPFVWLLTASTDVLKAIAPI-DFTQREERLT 182
Cdd:PRK11573 80 ----AIATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIkTDIVVSGALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 183 RSEMRKLIESGRNDgiIDMDEFRMMQGVLSLDSKLAKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDDKDDI 262
Cdd:PRK11573 156 KEELRTIVHESRSQ--ISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 263 LGIVHakdvLREANRVGFENIQM--EDIMR---EPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEV 337
Cdd:PRK11573 234 ISMLR----VREAYRLMTEKKEFtkENMLRaadEIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 338 IVGDIEDEYD-EMSFKYKKVSDDTYIIDGSMPIDKFNQLFNAHIYSGDSDTMAGIIIEQLGRFPQdtINESIQVDDYLFT 416
Cdd:PRK11573 310 IVGDFTTSMSpTLAEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPV--AGTRVRIGEYDID 387
|
410
....*....|....
gi 1092610523 417 TTDVDDGRIRKIKV 430
Cdd:PRK11573 388 ILDVQDNMIKQVKV 401
|
|
| CBS_pair_CorC_HlyC_assoc |
cd04590 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ... |
218-336 |
4.86e-50 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341366 [Multi-domain] Cd Length: 119 Bit Score: 165.36 E-value: 4.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 218 AKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDDKDDILGIVHAKDVLREANRvGFENIQMEDIMREPYFAPE 297
Cdd:cd04590 2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLE-GREKLDLRALLRPPLFVPE 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1092610523 298 TVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIE 336
Cdd:cd04590 81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
|
|
| CNNM |
pfam01595 |
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ... |
23-203 |
2.86e-46 |
|
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal transporter proteins such as cyclin M 1/2 (CNNM). CNNMs are integral membrane proteins that are conserved from bacteria to humans. CNNM family members influence metal ion homeostasis through mechanisms that may not involve direct membrane transport of the ions. Structurally, CNNMs are complex proteins that contain an extracellular N-terminal domain preceding a transmembrane domain, a 'Bateman module', which consists of two cystathionine- beta-synthase (CBS) domains pfam00571, and a C-terminal cNMP (cyclic nucleotide monophosphate) binding domain. This entry describes the CNNM transmembrane domain which contains four hydrophobic regions and forms a dimer through hydrophobic contacts between TM2 and TM3, in which each chain is composed of three transmembrane helices (TM1-3), a pair of short helices exposed on the intracellular side, and a juxtamembrane (JM) helix that forms a belt-like structure. The homodimer adopts an inward-facing conformation with a negatively charged cavity containing a conserved pi-helical turn in TM3 that coordinates a Mg2 ion.
Pssm-ID: 460260 Cd Length: 183 Bit Score: 158.15 E-value: 2.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 23 NAFLAGAEMAFVSVNQGKINQLAEEGDRRAVKVVQLLDKSDDFLSTIQVGITFAGFLSSASAANTFVGYILPylanipaA 102
Cdd:pfam01595 10 SAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAP-------L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 103 EILATAIVTVILSYISLVFGELFPKQVAIQIPEKYCLFSAGTISFLNKVFTPFVWLLTASTDVLKAIAPIDFTQREERLT 182
Cdd:pfam01595 83 GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESEPAVT 162
|
170 180
....*....|....*....|.
gi 1092610523 183 RSEMRKLIESGRNDGIIDMDE 203
Cdd:pfam01595 163 EEELRSLVEESAEEGVIEEEE 183
|
|
| CorC_HlyC |
smart01091 |
Transporter associated domain; This small domain is found in a family of proteins with the ... |
354-431 |
8.13e-20 |
|
Transporter associated domain; This small domain is found in a family of proteins with the DUF21 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates.
Pssm-ID: 215020 [Multi-domain] Cd Length: 78 Bit Score: 83.26 E-value: 8.13e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092610523 354 KKVSDDTYIIDGSMPIDKFNQLFNAHIYSGDSDTMAGIIIEQLGRFPQdtINESIQVDDYLFTTTDVDDGRIRKIKVH 431
Cdd:smart01091 1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPE--VGDSVEIGGLRFEVLEVDGRRIDKVRVT 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TlyC |
COG1253 |
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ... |
23-440 |
2.05e-170 |
|
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];
Pssm-ID: 440865 [Multi-domain] Cd Length: 435 Bit Score: 485.01 E-value: 2.05e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 23 NAFLAGAEMAFVSVNQGKINQLAEEGDRRAVKVVQLLDKSDDFLSTIQVGITFAGFLSSASAANTFVGYILPYLANIP-- 100
Cdd:COG1253 17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGlp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 101 --AAEILATAIVTVILSYISLVFGELFPKQVAIQIPEKYCLFSAGTISFLNKVFTPFVWLLTASTDVLKAIAPIDFTQRE 178
Cdd:COG1253 97 aaLAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 179 ERLTRSEMRKLIESGRNDGIIDMDEFRMMQGVLSLDSKLAKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDD 258
Cdd:COG1253 177 PAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEGD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 259 KDDILGIVHAKDVLREANRvgFENIQMEDIMREPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVI 338
Cdd:COG1253 257 LDDIVGVVHVKDLLRALLE--GEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 339 VGDIEDEYDEMSFKYKKVSDDTYIIDGSMPIDKFNQLFNAHIY-SGDSDTMAGIIIEQLGRFPQdtINESIQVDDYLFTT 417
Cdd:COG1253 335 VGEIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPeEEDYETLGGLVLEQLGRIPE--VGETVEVDGLRFEV 412
|
410 420
....*....|....*....|...
gi 1092610523 418 TDVDDGRIRKIKVHYQPREEDDE 440
Cdd:COG1253 413 LDMDGRRIDKVLVTRLPEEEEEE 435
|
|
| CorB |
COG4536 |
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ... |
24-431 |
9.44e-119 |
|
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion transport and metabolism];
Pssm-ID: 443602 [Multi-domain] Cd Length: 420 Bit Score: 352.84 E-value: 9.44e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 24 AFLAGAEMAFVSVNQGKINQLAEEGDRRAVKVVQLLDKSDDFLSTIQVGITFAGFLSSASAANTFVGYILPylanipAAE 103
Cdd:COG4536 21 AFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVIAIRLFGD------AGV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 104 ILATAIVTVILsyisLVFGELFPKQVAIQIPEKYCLFSAGTISFLNKVFTPFVWLLTASTDVLKAIAPIDF-TQREERLT 182
Cdd:COG4536 95 AIATLVLTLLI----LIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKPdADASDLLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 183 RSEMRKLIESGRNDGIIDMDEFRMMQGVLSLDSKLAKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDDKDDI 262
Cdd:COG4536 171 EEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRGDIDNI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 263 LGIVHAKDVLREANRVGFENIQMEDIMREPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVIVGDI 342
Cdd:COG4536 251 VGVLHVRDLLRALRKGDLSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILEEIVGEI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 343 EDEYDEMSFKYKKVSDDTYIIDGSMPIDKFNQLFNAHIYSGDSDTMAGIIIEQLGRFPQdtINESIQVDDYLFTTTDVDD 422
Cdd:COG4536 331 TDEHDPDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPE--AGQSFTIHGYRFEILQVQD 408
|
....*....
gi 1092610523 423 GRIRKIKVH 431
Cdd:COG4536 409 NRIKTVRIR 417
|
|
| GldE |
TIGR03520 |
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ... |
24-430 |
1.09e-81 |
|
gliding motility-associated protein GldE; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldC is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. GldE was discovered because of its adjacency to GldD in F. johnsonii. Overexpression of GldE partially supresses the effects of a GldB point mutant suggesting that GldB and GldE interact. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Not all Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility and in fact some do not appear to express the gliding phenotype.
Pssm-ID: 274626 [Multi-domain] Cd Length: 407 Bit Score: 257.27 E-value: 1.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 24 AFLAGAEMAFVSVNQGKINQLAEEGDRRAVKVVQLLDKSDDFLSTIQVG---ITFAGFLSSASAANTFVGYIlpylaNIP 100
Cdd:TIGR03520 8 ALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIAnnfINIAIVLLFTSLSDNLFGSF-----NTE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 101 AAEILataIVTVILSYISLVFGELFPKQVAIQIPEKYCLFSAGTISFLNKVFTPFVWLLTASTDVLKAiapiDFTQREER 180
Cdd:TIGR03520 83 LLRFL---IEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHK----KFGKQKSN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 181 LTRSEMRKLIESGRNDGIIDmDEFRMMQGVLSLDSKLAKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDDKD 260
Cdd:TIGR03520 156 ISVDQLSQALELTDEEDTTK-EEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETID 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 261 DILGIVHAKDVLREANRvgfENIQMEDIMREPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVIVG 340
Cdd:TIGR03520 235 NITGVLYIKDLLPHLNK---KNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 341 DIEDEYDEMSFKYKKVSDDTYIIDGSMPIDKF-------NQLFNAhiYSGDSDTMAGIIIEQLGRFPQdtINESIQVDDY 413
Cdd:TIGR03520 312 DISDEFDDEDLIYSKIDDNNYVFEGKTSLKDFykilkleEDMFDE--VKGEAETLAGFLLEISGGFPK--KGEKITFENF 387
|
410
....*....|....*..
gi 1092610523 414 LFTTTDVDDGRIRKIKV 430
Cdd:TIGR03520 388 EFTIEAMDKKRIKQVKV 404
|
|
| CorC |
COG4535 |
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ... |
182-440 |
1.54e-76 |
|
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion transport and metabolism];
Pssm-ID: 443601 [Multi-domain] Cd Length: 288 Bit Score: 240.01 E-value: 1.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 182 TRSEMRKLIESGRNDGIIDMDEFRMMQGVLSLDSKLAKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDDKDD 261
Cdd:COG4535 29 DREELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 262 ILGIVHAKDVLREAnRVGFENIQMEDIMREPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVIVGD 341
Cdd:COG4535 109 VIGILLAKDLLRYL-AQDAEEFDLRDLLRPAVFVPESKRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQIVGE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 342 IEDEYDEMSFKY--KKVSDDTYIIDGSMPIDKFNQLFNAHIYSGDSDTMAGIIIEQLGRFPQdtINESIQVDDYLFTTTD 419
Cdd:COG4535 188 IEDEHDEDEDEDniRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTIGGLVAQEFGHLPK--RGESIEIDGLRFKVLR 265
|
250 260
....*....|....*....|.
gi 1092610523 420 VDDGRIRKIKVHYQPREEDDE 440
Cdd:COG4535 266 ADSRRIHLLRVTRLPPAAEPD 286
|
|
| PRK11573 |
PRK11573 |
hypothetical protein; Provisional |
24-430 |
4.48e-53 |
|
hypothetical protein; Provisional
Pssm-ID: 236933 [Multi-domain] Cd Length: 413 Bit Score: 183.03 E-value: 4.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 24 AFLAGAEMAFVSVNQGKINQLAEEGDRRAVKVVQLLDKSDDFLSTIQVGITFAGFLSSASAanTFVGYILPYLANIpaae 103
Cdd:PRK11573 6 AYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALG--TIVGMRLYGDAGV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 104 ilatAIVTVILSYISLVFGELFPKQVAIQIPEKYCLFSAGTISFLNKVFTPFVWLLTASTDVLKAIAPI-DFTQREERLT 182
Cdd:PRK11573 80 ----AIATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIkTDIVVSGALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 183 RSEMRKLIESGRNDgiIDMDEFRMMQGVLSLDSKLAKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDDKDDI 262
Cdd:PRK11573 156 KEELRTIVHESRSQ--ISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 263 LGIVHakdvLREANRVGFENIQM--EDIMR---EPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEV 337
Cdd:PRK11573 234 ISMLR----VREAYRLMTEKKEFtkENMLRaadEIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 338 IVGDIEDEYD-EMSFKYKKVSDDTYIIDGSMPIDKFNQLFNAHIYSGDSDTMAGIIIEQLGRFPQdtINESIQVDDYLFT 416
Cdd:PRK11573 310 IVGDFTTSMSpTLAEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPV--AGTRVRIGEYDID 387
|
410
....*....|....
gi 1092610523 417 TTDVDDGRIRKIKV 430
Cdd:PRK11573 388 ILDVQDNMIKQVKV 401
|
|
| CBS_pair_CorC_HlyC_assoc |
cd04590 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ... |
218-336 |
4.86e-50 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341366 [Multi-domain] Cd Length: 119 Bit Score: 165.36 E-value: 4.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 218 AKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDDKDDILGIVHAKDVLREANRvGFENIQMEDIMREPYFAPE 297
Cdd:cd04590 2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLE-GREKLDLRALLRPPLFVPE 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1092610523 298 TVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIE 336
Cdd:cd04590 81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
|
|
| PRK15094 |
PRK15094 |
magnesium/cobalt transporter CorC; |
183-431 |
3.59e-48 |
|
magnesium/cobalt transporter CorC;
Pssm-ID: 185050 [Multi-domain] Cd Length: 292 Bit Score: 166.52 E-value: 3.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 183 RSEMRKLIESGRNDGIIDMDEFRMMQGVLSLDSKLAKGVMVPRTDTFMLDIEDDREENLQLILQSQYSRIPVYRDDKDDI 262
Cdd:PRK15094 34 RDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 263 LGIVHAKDVLrEANRVGFENIQMEDIMREPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVIVGDI 342
Cdd:PRK15094 114 EGILMAKDLL-PFMRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 343 EDEYD-EMSFKYKKVSDDTYIIDGSMPIDKFNQLFNAHIYSGDSDTMAGIIIEQLGRFPQDtiNESIQVDDYLFTTTDVD 421
Cdd:PRK15094 193 EDEYDeEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGHLPAR--GETIDIDGYQFKVAMAD 270
|
250
....*....|
gi 1092610523 422 DGRIrkIKVH 431
Cdd:PRK15094 271 SRRI--IQVH 278
|
|
| CNNM |
pfam01595 |
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ... |
23-203 |
2.86e-46 |
|
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal transporter proteins such as cyclin M 1/2 (CNNM). CNNMs are integral membrane proteins that are conserved from bacteria to humans. CNNM family members influence metal ion homeostasis through mechanisms that may not involve direct membrane transport of the ions. Structurally, CNNMs are complex proteins that contain an extracellular N-terminal domain preceding a transmembrane domain, a 'Bateman module', which consists of two cystathionine- beta-synthase (CBS) domains pfam00571, and a C-terminal cNMP (cyclic nucleotide monophosphate) binding domain. This entry describes the CNNM transmembrane domain which contains four hydrophobic regions and forms a dimer through hydrophobic contacts between TM2 and TM3, in which each chain is composed of three transmembrane helices (TM1-3), a pair of short helices exposed on the intracellular side, and a juxtamembrane (JM) helix that forms a belt-like structure. The homodimer adopts an inward-facing conformation with a negatively charged cavity containing a conserved pi-helical turn in TM3 that coordinates a Mg2 ion.
Pssm-ID: 460260 Cd Length: 183 Bit Score: 158.15 E-value: 2.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 23 NAFLAGAEMAFVSVNQGKINQLAEEGDRRAVKVVQLLDKSDDFLSTIQVGITFAGFLSSASAANTFVGYILPylanipaA 102
Cdd:pfam01595 10 SAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAP-------L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 103 EILATAIVTVILSYISLVFGELFPKQVAIQIPEKYCLFSAGTISFLNKVFTPFVWLLTASTDVLKAIAPIDFTQREERLT 182
Cdd:pfam01595 83 GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESEPAVT 162
|
170 180
....*....|....*....|.
gi 1092610523 183 RSEMRKLIESGRNDGIIDMDE 203
Cdd:pfam01595 163 EEELRSLVEESAEEGVIEEEE 183
|
|
| CorC_HlyC |
smart01091 |
Transporter associated domain; This small domain is found in a family of proteins with the ... |
354-431 |
8.13e-20 |
|
Transporter associated domain; This small domain is found in a family of proteins with the DUF21 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates.
Pssm-ID: 215020 [Multi-domain] Cd Length: 78 Bit Score: 83.26 E-value: 8.13e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092610523 354 KKVSDDTYIIDGSMPIDKFNQLFNAHIYSGDSDTMAGIIIEQLGRFPQdtINESIQVDDYLFTTTDVDDGRIRKIKVH 431
Cdd:smart01091 1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPE--VGDSVEIGGLRFEVLEVDGRRIDKVRVT 76
|
|
| CorC_HlyC |
pfam03471 |
Transporter associated domain; This small domain is found in a family of proteins with the ... |
354-434 |
8.95e-17 |
|
Transporter associated domain; This small domain is found in a family of proteins with the pfam01595 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates.
Pssm-ID: 460935 [Multi-domain] Cd Length: 81 Bit Score: 74.89 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 354 KKVSDDTYIIDGSMPIDKFNQLFNAHIYSGDSDTMAGIIIEQLGRFPQDTINESIQVDDYLFTTTDVDDGRIRKIKVHYQ 433
Cdd:pfam03471 1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDKVEVELGGLRFTVLEMDGRRIKKVRITKL 80
|
.
gi 1092610523 434 P 434
Cdd:pfam03471 81 E 81
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
241-345 |
6.60e-09 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 54.10 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 241 LQLILQSQYSRIPVYrDDKDDILGIVHAKDVLREANRVGFENIQM-------EDIM-REPYFAPETVFIDDLLLEFKRNH 312
Cdd:COG3448 25 LELMREHGIRGLPVV-DEDGRLVGIVTERDLLRALLPDRLDELEErlldlpvEDVMtRPVVTVTPDTPLEEAAELMLEHG 103
|
90 100 110
....*....|....*....|....*....|...
gi 1092610523 313 LHMAILKDEYGGVVGLVTLEDLIEVIVGDIEDE 345
Cdd:COG3448 104 IHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
225-335 |
1.37e-08 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 52.63 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 225 RTDTFMLDIEDDREENLQLILQSQYSRIPVyRDDKDDILGIVHAKDVLRE-ANRVGFENIQMEDIM-REPYFAPETVFID 302
Cdd:cd02205 1 TRDVVTVDPDTTVREALELMAENGIGALPV-VDDDGKLVGIVTERDILRAlVEGGLALDTPVAEVMtPDVITVSPDTDLE 79
|
90 100 110
....*....|....*....|....*....|...
gi 1092610523 303 DLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLI 335
Cdd:cd02205 80 EALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
205-338 |
7.00e-08 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 52.58 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 205 RMMQGVLSLDSKLAKGVMVPRTDTfmLDIEDDREENLQLILQSQYSRIPVYRDDKddILGIVHAKDVLRE-ANRVGFENI 283
Cdd:COG2524 75 VAEKELGLVLKMKVKDIMTKDVIT--VSPDTTLEEALELMLEKGISGLPVVDDGK--LVGIITERDLLKAlAEGRDLLDA 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092610523 284 QMEDIM-REPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVI 338
Cdd:COG2524 151 PVSDIMtRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
217-343 |
4.61e-07 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 48.71 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 217 LAKGVMvpRTDTFMLDIEDDREENLQLILQSQYSRIPVYrDDKDDILGIVHAKDVLRE--ANRVGFENIQMEDIM-REPY 293
Cdd:COG0517 2 KVKDIM--TTDVVTVSPDATVREALELMSEKRIGGLPVV-DEDGKLVGIVTDRDLRRAlaAEGKDLLDTPVSEVMtRPPV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1092610523 294 FAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVIVGDIE 343
Cdd:COG0517 79 TVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
241-338 |
1.77e-06 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 46.75 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 241 LQLILQSQYSRIPVyRDDKDDILGIVHAKDVLRE--ANRVGFENIQMEDIM-REPYFAPETVFIDDLLLEFKRNHL-HMA 316
Cdd:COG2905 22 ARLMTEKGVGSLVV-VDDDGRLVGIITDRDLRRRvlAEGLDPLDTPVSEVMtRPPITVSPDDSLAEALELMEEHRIrHLP 100
|
90 100
....*....|....*....|..
gi 1092610523 317 ILKDeyGGVVGLVTLEDLIEVI 338
Cdd:COG2905 101 VVDD--GKLVGIVSITDLLRAL 120
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
213-336 |
1.04e-05 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 44.90 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092610523 213 LDSKLAKGVMVpRTDTFMLDIEDDREENLQLILQSQYSRIPVYrDDKDDILGIVHAKDVLREAnrvgfENIQMEDIMREP 292
Cdd:COG4109 13 KEILLVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVV-DENGRLVGIVTSKDILGKD-----DDTPIEDVMTKN 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1092610523 293 yfaPETVFIDDLLlefkRNHLHMAILK--------DEYGGVVGLVTLEDLIE 336
Cdd:COG4109 86 ---PITVTPDTSL----ASAAHKMIWEgiellpvvDDDGRLLGIISRQDVLK 130
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
223-274 |
2.05e-04 |
|
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.
Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 39.12 E-value: 2.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1092610523 223 VPRTDTFMLDIEDDREENLQLILQSQYSRIPVYrDDKDDILGIVHAKDVLRE 274
Cdd:pfam00571 4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVV-DEDGKLVGIVTLKDLLRA 54
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
286-340 |
1.15e-03 |
|
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: 36.81 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092610523 286 EDIM-REPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVIVG 340
Cdd:pfam00571 2 KDIMtKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
286-358 |
2.32e-03 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 38.31 E-value: 2.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092610523 286 EDIM-REPYFAPETVFIDDLLLEFKRNHLHMAILKDEYGGVVGLVTLEDLIEVIVGDIEDEYDEmSFKYKKVSD 358
Cdd:COG3448 5 RDIMtRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEE-RLLDLPVED 77
|
|
| |
