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Conserved domains on  [gi|1958787278|ref|XP_038934167|]
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potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 isoform X1 [Rattus norvegicus]

Protein Classification

cyclic nucleotide-gated ion channel( domain architecture ID 13328258)

cyclic nucleotide-gated ion channel is a nonselective channel that is opened by the direct binding of cyclic nucleotides, cAMP and cGMP

CATH:  2.60.120.10
PubMed:  12087135|17601606
SCOP:  4000272
TCDB:  1.A.1

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
181-289 1.72e-28

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), 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. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 109.34  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 181 LFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEMK---LSDGSYFGEICLLTRGRR 255
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVykLDEDGREQIvgfLGPGDLFGELALLGNGPR 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958787278 256 TASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAF 289
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
51-325 2.27e-05

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278  51 YSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIqsLDSSRR--QYQEKYKQVEQYMSFHK 128
Cdd:PLN03192  251 YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLV--VEGTRRtmEFRNSIEAASNFVGRNR 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 129 LPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYI 208
Cdd:PLN03192  329 LPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDV 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 209 IREGTIGKKMYFIQHGVVSV-LTKGNKEM---KLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVleeypM 284
Cdd:PLN03192  409 IMQNEAPDDVYIVVSGEVEIiDSEGEKERvvgTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEA-----M 483
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958787278 285 MRRAFETVAIdrldrigKKNSILLHKVQHDLSSGVF---NNQEN 325
Cdd:PLN03192  484 QTRQEDNVVI-------LKNFLQHHKELHDLNVGDLlgdNGGEH 520
PRK07003 super family cl35530
DNA polymerase III subunit gamma/tau;
433-526 4.00e-04

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK07003:

Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.30  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 433 PGSPATRVGPALPARRLSR--ASRPLSASQPSLPHGAPAPSPAASARPASSSTPRLGPAPTTRTAAPSPDRRDSASPGAA 510
Cdd:PRK07003  471 PADSGSASAPASDAPPDAAfePAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAA 550
                          90
                  ....*....|....*.
gi 1958787278 511 SGLDPLDSARSRLSSN 526
Cdd:PRK07003  551 AALDVLRNAGMRVSSD 566
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
181-289 1.72e-28

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), 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. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 109.34  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 181 LFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEMK---LSDGSYFGEICLLTRGRR 255
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVykLDEDGREQIvgfLGPGDLFGELALLGNGPR 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958787278 256 TASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAF 289
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
181-290 5.44e-20

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 85.53  E-value: 5.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278  181 LFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEM---KLSDGSYFGEICLLTRGRR 255
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVykVLEDGEEQivgTLGPGDFFGELALLTNSRR 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958787278  256 TASVRADTY--CRLYSLSVDNFNEVLEEYPMMRRAFE 290
Cdd:smart00100  81 AASAAAVALelATLLRIDFRDFLQLLPELPQLLLELL 117
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
182-310 9.48e-19

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 84.65  E-value: 9.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 182 FANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEMKLS---DGSYFGEICLLTRGRRT 256
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDGREQILGflgPGDFFGELSLLGGEPSP 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958787278 257 ASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHK 310
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFL 134
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
199-282 1.82e-18

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 80.35  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 199 FEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTK---GNKEM--KLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVD 273
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTledGREQIlaVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80

                  ....*....
gi 1958787278 274 NFNEVLEEY 282
Cdd:pfam00027  81 DFLELLERD 89
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
208-283 9.27e-09

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 55.76  E-value: 9.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 208 IIREGTIGKKMYFIQHGVVSVLTKGN--KEM---KLSDGSYFGEICLLTRG-RRTASVRADTYCRLYSLSVDNFNEVLEE 281
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegKEMilsYLNQGDFIGELGLFEEGqERSAWVRAKTACEVAEISYKKFRQLIQV 110

                  ..
gi 1958787278 282 YP 283
Cdd:PRK11753  111 NP 112
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
51-325 2.27e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278  51 YSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIqsLDSSRR--QYQEKYKQVEQYMSFHK 128
Cdd:PLN03192  251 YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLV--VEGTRRtmEFRNSIEAASNFVGRNR 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 129 LPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYI 208
Cdd:PLN03192  329 LPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDV 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 209 IREGTIGKKMYFIQHGVVSV-LTKGNKEM---KLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVleeypM 284
Cdd:PLN03192  409 IMQNEAPDDVYIVVSGEVEIiDSEGEKERvvgTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEA-----M 483
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958787278 285 MRRAFETVAIdrldrigKKNSILLHKVQHDLSSGVF---NNQEN 325
Cdd:PLN03192  484 QTRQEDNVVI-------LKNFLQHHKELHDLNVGDLlgdNGGEH 520
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
433-526 4.00e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.30  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 433 PGSPATRVGPALPARRLSR--ASRPLSASQPSLPHGAPAPSPAASARPASSSTPRLGPAPTTRTAAPSPDRRDSASPGAA 510
Cdd:PRK07003  471 PADSGSASAPASDAPPDAAfePAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAA 550
                          90
                  ....*....|....*.
gi 1958787278 511 SGLDPLDSARSRLSSN 526
Cdd:PRK07003  551 AALDVLRNAGMRVSSD 566
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
181-289 1.72e-28

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), 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. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 109.34  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 181 LFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEMK---LSDGSYFGEICLLTRGRR 255
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVykLDEDGREQIvgfLGPGDLFGELALLGNGPR 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958787278 256 TASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAF 289
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
181-290 5.44e-20

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 85.53  E-value: 5.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278  181 LFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEM---KLSDGSYFGEICLLTRGRR 255
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVykVLEDGEEQivgTLGPGDFFGELALLTNSRR 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958787278  256 TASVRADTY--CRLYSLSVDNFNEVLEEYPMMRRAFE 290
Cdd:smart00100  81 AASAAAVALelATLLRIDFRDFLQLLPELPQLLLELL 117
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
182-310 9.48e-19

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 84.65  E-value: 9.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 182 FANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEMKLS---DGSYFGEICLLTRGRRT 256
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDGREQILGflgPGDFFGELSLLGGEPSP 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958787278 257 ASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHK 310
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFL 134
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
199-282 1.82e-18

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 80.35  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 199 FEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTK---GNKEM--KLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVD 273
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTledGREQIlaVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80

                  ....*....
gi 1958787278 274 NFNEVLEEY 282
Cdd:pfam00027  81 DFLELLERD 89
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
208-283 9.27e-09

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 55.76  E-value: 9.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 208 IIREGTIGKKMYFIQHGVVSVLTKGN--KEM---KLSDGSYFGEICLLTRG-RRTASVRADTYCRLYSLSVDNFNEVLEE 281
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegKEMilsYLNQGDFIGELGLFEEGqERSAWVRAKTACEVAEISYKKFRQLIQV 110

                  ..
gi 1958787278 282 YP 283
Cdd:PRK11753  111 NP 112
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
51-325 2.27e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278  51 YSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIqsLDSSRR--QYQEKYKQVEQYMSFHK 128
Cdd:PLN03192  251 YISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLV--VEGTRRtmEFRNSIEAASNFVGRNR 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 129 LPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYI 208
Cdd:PLN03192  329 LPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDV 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 209 IREGTIGKKMYFIQHGVVSV-LTKGNKEM---KLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVleeypM 284
Cdd:PLN03192  409 IMQNEAPDDVYIVVSGEVEIiDSEGEKERvvgTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEA-----M 483
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958787278 285 MRRAFETVAIdrldrigKKNSILLHKVQHDLSSGVF---NNQEN 325
Cdd:PLN03192  484 QTRQEDNVVI-------LKNFLQHHKELHDLNVGDLlgdNGGEH 520
PLN02868 PLN02868
acyl-CoA thioesterase family protein
164-245 3.52e-04

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 43.17  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 164 REEIVNFncrklVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTK----GNKEMKLS 239
Cdd:PLN02868    3 TESVVEF-----LGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPaeeeSRPEFLLK 77

                  ....*.
gi 1958787278 240 DGSYFG 245
Cdd:PLN02868   78 RYDYFG 83
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
433-526 4.00e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.30  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787278 433 PGSPATRVGPALPARRLSR--ASRPLSASQPSLPHGAPAPSPAASARPASSSTPRLGPAPTTRTAAPSPDRRDSASPGAA 510
Cdd:PRK07003  471 PADSGSASAPASDAPPDAAfePAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAA 550
                          90
                  ....*....|....*.
gi 1958787278 511 SGLDPLDSARSRLSSN 526
Cdd:PRK07003  551 AALDVLRNAGMRVSSD 566
 
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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