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Conserved domains on  [gi|728041059|gb|AIY63189|]
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PhoR, partial [Bacillus subtilis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
sCache_like super family cl25077
Single Cache-like; This entry represents the N-terminal Cache-like domain of the alkaline ...
1-72 1.79e-19

Single Cache-like; This entry represents the N-terminal Cache-like domain of the alkaline phosphatase synthesis sensor protein PhoR. It covers part of the PAS-like fold that share a central five-stranded beta- sheet of identical topology to other PAS domains.


The actual alignment was detected with superfamily member pfam16736:

Pssm-ID: 407005  Cd Length: 114  Bit Score: 81.28  E-value: 1.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059    1 KDAGGALDVSASVIDTDGKVLYGSNG---RAADSQKVQALVSGHEG-----ILSTTDNKLYYGLSLRSEGEKTGYVLLSA 72
Cdd:pfam16736  35 EEASEKLDARITIIDADGKVLYDTGGeteDAEHEAIIQELLSGEELqevrvITTDEDDLLYYAVPIQKEGEQEGYILLSS 114
NtrY super family cl34858
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
94-248 2.60e-13

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5000:

Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 68.84  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059  94 AFIVIVYFYSSMTsrykRSIESATNVATELSKGNYDARtygGYIRRSD---KLGHAMNSLAIDLMEMTRTQEMQRDRLLT 170
Cdd:COG5000   22 ALWLALLLARRLT----RPLRRLAEATRAVAAGDLSVR---LPVTGDDeigELARAFNRMTDQLKEQREELEERRRYLET 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 728041059 171 VIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAFEHEEVIQLVEDIFmtETKKCKLLRLPIKIERRY 248
Cdd:COG5000   95 ILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREAL--ERGWQEEIELTRDGRRTL 170
 
Name Accession Description Interval E-value
sCache_like pfam16736
Single Cache-like; This entry represents the N-terminal Cache-like domain of the alkaline ...
1-72 1.79e-19

Single Cache-like; This entry represents the N-terminal Cache-like domain of the alkaline phosphatase synthesis sensor protein PhoR. It covers part of the PAS-like fold that share a central five-stranded beta- sheet of identical topology to other PAS domains.


Pssm-ID: 407005  Cd Length: 114  Bit Score: 81.28  E-value: 1.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059    1 KDAGGALDVSASVIDTDGKVLYGSNG---RAADSQKVQALVSGHEG-----ILSTTDNKLYYGLSLRSEGEKTGYVLLSA 72
Cdd:pfam16736  35 EEASEKLDARITIIDADGKVLYDTGGeteDAEHEAIIQELLSGEELqevrvITTDEDDLLYYAVPIQKEGEQEGYILLSS 114
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
94-248 2.60e-13

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 68.84  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059  94 AFIVIVYFYSSMTsrykRSIESATNVATELSKGNYDARtygGYIRRSD---KLGHAMNSLAIDLMEMTRTQEMQRDRLLT 170
Cdd:COG5000   22 ALWLALLLARRLT----RPLRRLAEATRAVAAGDLSVR---LPVTGDDeigELARAFNRMTDQLKEQREELEERRRYLET 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 728041059 171 VIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAFEHEEVIQLVEDIFmtETKKCKLLRLPIKIERRY 248
Cdd:COG5000   95 ILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREAL--ERGWQEEIELTRDGRRTL 170
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
167-265 8.47e-12

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 60.51  E-value: 8.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059  167 RLLTVIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAFEHEE----VIQLVEDIFMTETKKCKLLRLPI 242
Cdd:pfam00989   2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDdaevAELLRQALLQGEESRGFEVSFRV 81
                          90       100
                  ....*....|....*....|....
gi 728041059  243 -KIERRYFEVDGVPIMGPDDEWKG 265
Cdd:pfam00989  82 pDGRPRHVEVRASPVRDAGGEILG 105
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
166-227 4.66e-04

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 37.76  E-value: 4.66e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 728041059   166 DRLLTVIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAFEHEEVIQLVEDI 227
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
 
Name Accession Description Interval E-value
sCache_like pfam16736
Single Cache-like; This entry represents the N-terminal Cache-like domain of the alkaline ...
1-72 1.79e-19

Single Cache-like; This entry represents the N-terminal Cache-like domain of the alkaline phosphatase synthesis sensor protein PhoR. It covers part of the PAS-like fold that share a central five-stranded beta- sheet of identical topology to other PAS domains.


Pssm-ID: 407005  Cd Length: 114  Bit Score: 81.28  E-value: 1.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059    1 KDAGGALDVSASVIDTDGKVLYGSNG---RAADSQKVQALVSGHEG-----ILSTTDNKLYYGLSLRSEGEKTGYVLLSA 72
Cdd:pfam16736  35 EEASEKLDARITIIDADGKVLYDTGGeteDAEHEAIIQELLSGEELqevrvITTDEDDLLYYAVPIQKEGEQEGYILLSS 114
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
94-248 2.60e-13

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 68.84  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059  94 AFIVIVYFYSSMTsrykRSIESATNVATELSKGNYDARtygGYIRRSD---KLGHAMNSLAIDLMEMTRTQEMQRDRLLT 170
Cdd:COG5000   22 ALWLALLLARRLT----RPLRRLAEATRAVAAGDLSVR---LPVTGDDeigELARAFNRMTDQLKEQREELEERRRYLET 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 728041059 171 VIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAFEHEEVIQLVEDIFmtETKKCKLLRLPIKIERRY 248
Cdd:COG5000   95 ILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREAL--ERGWQEEIELTRDGRRTL 170
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
167-265 8.47e-12

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 60.51  E-value: 8.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059  167 RLLTVIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAFEHEE----VIQLVEDIFMTETKKCKLLRLPI 242
Cdd:pfam00989   2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDdaevAELLRQALLQGEESRGFEVSFRV 81
                          90       100
                  ....*....|....*....|....
gi 728041059  243 -KIERRYFEVDGVPIMGPDDEWKG 265
Cdd:pfam00989  82 pDGRPRHVEVRASPVRDAGGEILG 105
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
162-256 6.36e-07

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 49.77  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059 162 EMQRDRLLTVIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAFEHEEVIQLVedifmtETKKCKLLR-L 240
Cdd:COG3829    7 KELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVL------KTGKPVTGViQ 80
                         90
                 ....*....|....*.
gi 728041059 241 PIKIERRYFEVDGVPI 256
Cdd:COG3829   81 KTGGKGKTVIVTAIPI 96
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
6-257 6.75e-05

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 43.95  E-value: 6.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059   6 ALDVSASVIDTDGKVLYGSNGRAADSQKVQALVSGHEGILSTTDNKLYYGLSLRSEGEKTGYVLLSASEKSDGLKGELWG 85
Cdd:COG2770  137 ALALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLL 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059  86 MLTASLCTAFIVIVYFYSSMTsrykRSIESATNVATELSKGNYDARTyggYIRRSD---KLGHAMNSLAIDL-----MEM 157
Cdd:COG2770  217 LALLALLLALLLALLLARRIT----RPLRRLAEAARRIAAGDLDVRI---PVSRKDeigELARAFNRMADSLresieEAE 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059 158 TRTQEMQRDRLLTVIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAFEHEEVIQLVEDIFMTETKKCKL 237
Cdd:COG2770  290 EEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLL 369
                        250       260
                 ....*....|....*....|
gi 728041059 238 LRLPIKIERRYFEVDGVPIM 257
Cdd:COG2770  370 EAELLVLLALEALALEAELA 389
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
156-263 9.04e-05

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 43.30  E-value: 9.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059 156 EMTRTQEMQRdrllTVIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAF-EHEEVIQLVEDIfMTETKK 234
Cdd:COG3852    1 ALRESEELLR----AILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFpEDSPLRELLERA-LAEGQP 75
                         90       100       110
                 ....*....|....*....|....*....|..
gi 728041059 235 CKLLRLPIKI---ERRYFEVDGVPIMGPDDEW 263
Cdd:COG3852   76 VTEREVTLRRkdgEERPVDVSVSPLRDAEGEG 107
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
166-227 4.66e-04

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 37.76  E-value: 4.66e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 728041059   166 DRLLTVIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAFEHEEVIQLVEDI 227
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
PAS COG2202
PAS domain [Signal transduction mechanisms];
164-262 6.32e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 37.31  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728041059 164 QRDRLLTVIENIGSGLIMIDGRGFINLVNRSYAKQFHINPNHMLRRLYHDAF---EHEEVIQLVEDIFMTETKKCKLLRL 240
Cdd:COG2202  135 SEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLhpeDRERLLELLRRLLEGGRESYELELR 214
                         90       100
                 ....*....|....*....|..
gi 728041059 241 PIKIERRYFEVDGVPIMGPDDE 262
Cdd:COG2202  215 LKDGDGRWVWVEASAVPLRDGG 236
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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