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Conserved domains on  [gi|156071470|ref|NP_001185|]
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potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 [Homo sapiens]

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
Gene Ontology:  GO:0016020|GO:0030551|GO:0005216|GO:0006811|GO:0022832
PubMed:  12087135|17601606
SCOP:  4000272
TCDB:  1.A.1

Graphical summary

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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 ...
 544-652 5.57e-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: 108.95  E-value: 5.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 544 LFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEMK---LSDGSYFGEICLLTRGRR 618
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVykLDEDGREQIvgfLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 156071470 619 TASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAF 652
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 150-688 4.83e-24

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 108.80  E-value: 4.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 150 GPAGEPRGSQASFMQRQFGALLQP--GVNKFSLRMFGSQKavereqervksagaWIIHPYsDFRF-YWDFTMLLFMVGNL 226
Cdd:PLN03192  12 GKGTGEEDDSGSLSLRNLSKVILPplGVPSYNQNHIGSDG--------------WIISPM-DSRYrWWETLMVVLVAYSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 227 IIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYI-F 305
Cdd:PLN03192  77 WVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALaY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 306 LIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIhqWeeifhmtydlasavMRICNLISMMLLLCHWDGCLQ 385
Cdd:PLN03192 157 LITGTVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYF--W--------------IRCARLLSVTLFLVHCAGCLY 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 386 FLVPMLQDFPRNCWVS--INGMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHAT 463
Cdd:PLN03192 221 YLIADRYPHQGKTWIGavIPNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMT 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 464 ALIqsLDSSRR--QYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIvnfnCRKL--- 538
Cdd:PLN03192 301 NLV--VEGTRRtmEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSI----CQHLflp 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 539 -VASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV-LTKGNKEM---KLSDGSYFGEICLL 613
Cdd:PLN03192 375 vVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIiDSEGEKERvvgTLGCGDIFGEVGAL 454

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156071470 614 TRGRRTASVRADTYCRLYSLSVDNFNEVleeypMMRRAFETVAIdrldrigKKNSILLHKVQHDLNSGVF---NNQEN 688
Cdd:PLN03192 455 CCRPQSFTFRTKTLSQLLRLKTSTLIEA-----MQTRQEDNVVI-------LKNFLQHHKELHDLNVGDLlgdNGGEH 520
PBP1 super family cl34930
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 57-185 9.02e-05

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


The actual alignment was detected with superfamily member COG5180:

Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 46.21  E-value: 9.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  57 RAEALPPEAADEGGPRGRL----RSRDSSCGRPGTPGAASTAKGSPNGECGRGEPQCSPAGPEGPARGPKVSFSCRGAAS 132
Cdd:COG5180  337 RPAGVPEAASDAGQPPSAYppaeEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALD 416

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156071470 133 GPAPGPGPAEEAGSEEAGPAGEPRGSQASF-MQRQFGALLQPGVNKF-SLRMFGS 185
Cdd:COG5180  417 GGGRETASLGGAAGGAGQGPKADFVPGDAEsVSGPAGLADQAGAAAStAMADFVA 471
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 544-652 5.57e-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: 108.95  E-value: 5.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 544 LFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEMK---LSDGSYFGEICLLTRGRR 618
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVykLDEDGREQIvgfLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 156071470 619 TASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAF 652
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 150-688 4.83e-24

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 108.80  E-value: 4.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 150 GPAGEPRGSQASFMQRQFGALLQP--GVNKFSLRMFGSQKavereqervksagaWIIHPYsDFRF-YWDFTMLLFMVGNL 226
Cdd:PLN03192  12 GKGTGEEDDSGSLSLRNLSKVILPplGVPSYNQNHIGSDG--------------WIISPM-DSRYrWWETLMVVLVAYSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 227 IIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYI-F 305
Cdd:PLN03192  77 WVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALaY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 306 LIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIhqWeeifhmtydlasavMRICNLISMMLLLCHWDGCLQ 385
Cdd:PLN03192 157 LITGTVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYF--W--------------IRCARLLSVTLFLVHCAGCLY 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 386 FLVPMLQDFPRNCWVS--INGMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHAT 463
Cdd:PLN03192 221 YLIADRYPHQGKTWIGavIPNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMT 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 464 ALIqsLDSSRR--QYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIvnfnCRKL--- 538
Cdd:PLN03192 301 NLV--VEGTRRtmEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSI----CQHLflp 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 539 -VASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV-LTKGNKEM---KLSDGSYFGEICLL 613
Cdd:PLN03192 375 vVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIiDSEGEKERvvgTLGCGDIFGEVGAL 454

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156071470 614 TRGRRTASVRADTYCRLYSLSVDNFNEVleeypMMRRAFETVAIdrldrigKKNSILLHKVQHDLNSGVF---NNQEN 688
Cdd:PLN03192 455 CCRPQSFTFRTKTLSQLLRLKTSTLIEA-----MQTRQEDNVVI-------LKNFLQHHKELHDLNVGDLlgdNGGEH 520
Ion_trans_N pfam08412
Ion transport protein N-terminal; This metazoan domain is found to the N-terminus of pfam00520 ...
 167-209 1.69e-20

Ion transport protein N-terminal; This metazoan domain is found to the N-terminus of pfam00520 in voltage- and cyclic nucleotide-gated K/Na ion channels.


Pssm-ID: 400630  Cd Length: 43  Bit Score: 85.05  E-value: 1.69e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 156071470  167 FGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSD 209
Cdd:pfam08412   1 LKSLLQPSDNKLSMKLFGSKKAVEKEKERQKEAGVWIIHPCSN 43
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 544-653 1.02e-19

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: 1.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470   544 LFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEM---KLSDGSYFGEICLLTRGRR 618
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVykVLEDGEEQivgTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 156071470   619 TASVRADTY--CRLYSLSVDNFNEVLEEYPMMRRAFE 653
Cdd:smart00100  81 AASAAAVALelATLLRIDFRDFLQLLPELPQLLLELL 117
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 545-673 4.20e-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: 86.58  E-value: 4.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 545 FANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEMKLS---DGSYFGEICLLTRGRRT 619
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDGREQILGflgPGDFFGELSLLGGEPSP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156071470 620 ASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHK 673
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFL 134
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 562-645 3.23e-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: 3.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  562 FEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTK---GNKEM--KLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVD 636
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTledGREQIlaVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*....
gi 156071470  637 NFNEVLEEY 645
Cdd:pfam00027  81 DFLELLERD 89
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
571-646 1.38e-08

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 56.14  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 571 IIREGTIGKKMYFIQHGVVSVLTKGN--KEM---KLSDGSYFGEICLLTRG-RRTASVRADTYCRLYSLSVDNFNEVLEE 644
Cdd:PRK11753  31 LIHAGEKAETLYYIVKGSVAVLIKDEegKEMilsYLNQGDFIGELGLFEEGqERSAWVRAKTACEVAEISYKKFRQLIQV 110


                 ..
gi 156071470 645 YP 646
Cdd:PRK11753 111 NP 112
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 57-185 9.02e-05

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 46.21  E-value: 9.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  57 RAEALPPEAADEGGPRGRL----RSRDSSCGRPGTPGAASTAKGSPNGECGRGEPQCSPAGPEGPARGPKVSFSCRGAAS 132
Cdd:COG5180  337 RPAGVPEAASDAGQPPSAYppaeEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALD 416

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156071470 133 GPAPGPGPAEEAGSEEAGPAGEPRGSQASF-MQRQFGALLQPGVNKF-SLRMFGS 185
Cdd:COG5180  417 GGGRETASLGGAAGGAGQGPKADFVPGDAEsVSGPAGLADQAGAAAStAMADFVA 471
PHA03378 PHA03378
EBNA-3B; Provisional
 62-200 3.31e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.67  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  62 PPEaadegGPRGRLRSRDSSCGRPGTPGAASTAKGSPNGECGRGE-PQCSPAGPEGPARGPKVSFSCRGAASGPAPGPGP 140
Cdd:PHA03378 706 PPA-----APPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARpPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPP 780

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156071470 141 aeeagseEAGPAG--EPRGSQASFMQRQFGallqPGVNKFSLRMFGSQKAVEREQERVKSAG 200
Cdd:PHA03378 781 -------QAPPAPqqRPRGAPTPQPPPQAG----PTSMQLMPRAAPGQQGPTKQILRQLLTG 831
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 62-155 3.02e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 41.04  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  62 PPEAADEGGPRGR-----------LRSRDSSCGRPGTPGAASTAKGSPNGEcgRGEP----QCSPAGPEGPA-----RGP 121
Cdd:NF038329 187 PAGEKGPQGPRGEtgpageqgpagPAGPDGEAGPAGEDGPAGPAGDGQQGP--DGDPgptgEDGPQGPDGPAgkdgpRGD 264

                         90       100       110
                 ....*....|....*....|....*....|....
gi 156071470 122 KvsfscrgaasGPAPGPGPAEEAGseEAGPAGEP 155
Cdd:NF038329 265 R----------GEAGPDGPDGKDG--ERGPVGPA 286
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 544-652 5.57e-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: 108.95  E-value: 5.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 544 LFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEMK---LSDGSYFGEICLLTRGRR 618
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVykLDEDGREQIvgfLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 156071470 619 TASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAF 652
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 150-688 4.83e-24

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 108.80  E-value: 4.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 150 GPAGEPRGSQASFMQRQFGALLQP--GVNKFSLRMFGSQKavereqervksagaWIIHPYsDFRF-YWDFTMLLFMVGNL 226
Cdd:PLN03192  12 GKGTGEEDDSGSLSLRNLSKVILPplGVPSYNQNHIGSDG--------------WIISPM-DSRYrWWETLMVVLVAYSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 227 IIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYI-F 305
Cdd:PLN03192  77 WVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALaY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 306 LIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIhqWeeifhmtydlasavMRICNLISMMLLLCHWDGCLQ 385
Cdd:PLN03192 157 LITGTVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYF--W--------------IRCARLLSVTLFLVHCAGCLY 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 386 FLVPMLQDFPRNCWVS--INGMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHAT 463
Cdd:PLN03192 221 YLIADRYPHQGKTWIGavIPNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMT 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 464 ALIqsLDSSRR--QYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIvnfnCRKL--- 538
Cdd:PLN03192 301 NLV--VEGTRRtmEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSI----CQHLflp 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 539 -VASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV-LTKGNKEM---KLSDGSYFGEICLL 613
Cdd:PLN03192 375 vVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIiDSEGEKERvvgTLGCGDIFGEVGAL 454

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156071470 614 TRGRRTASVRADTYCRLYSLSVDNFNEVleeypMMRRAFETVAIdrldrigKKNSILLHKVQHDLNSGVF---NNQEN 688
Cdd:PLN03192 455 CCRPQSFTFRTKTLSQLLRLKTSTLIEA-----MQTRQEDNVVI-------LKNFLQHHKELHDLNVGDLlgdNGGEH 520
Ion_trans_N pfam08412
Ion transport protein N-terminal; This metazoan domain is found to the N-terminus of pfam00520 ...
 167-209 1.69e-20

Ion transport protein N-terminal; This metazoan domain is found to the N-terminus of pfam00520 in voltage- and cyclic nucleotide-gated K/Na ion channels.


Pssm-ID: 400630  Cd Length: 43  Bit Score: 85.05  E-value: 1.69e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 156071470  167 FGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSD 209
Cdd:pfam08412   1 LKSLLQPSDNKLSMKLFGSKKAVEKEKERQKEAGVWIIHPCSN 43
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 211-474 2.44e-20

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 91.17  E-value: 2.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  211 RFYWDFTMLLFMVGNLIIIPVGITF-FKDETTAPWIVFNVVSDTFFLMDLVLNFRTgiviednteiildpEKIKKKYLRT 289
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFqPEEPLTTVLEILDYVFTGIFTLEMLLKIIA--------------AGFKKRYFRS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  290 -WFVVDFVSSIPVDYIFLIVEKGIDSEVyktaRALRIVRFtkilsllrllrlSRLIRYIHQWEEIFHMTYdlasAVMRIC 368
Cdd:pfam00520  67 pWNILDFVVVLPSLISLVLSSVGSLSGL----RVLRLLRL------------LRLLRLIRRLEGLRTLVN----SLIRSL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  369 NLISMMLLLCHWDGCLQFLVPMlQDFPRNCWVSINGMVNHSWSELYSFALFKAMSHMLCIGYG-------RQAPESMTDI 441
Cdd:pfam00520 127 KSLGNLLLLLLLFLFIFAIIGY-QLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGWGdimydtiDGKGEFWAYI 205

                         250       260       270
                  ....*....|....*....|....*....|...
gi 156071470  442 WLTMLSMIVGATCYAMFIGHATALIQSLDSSRR 474
Cdd:pfam00520 206 YFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 544-653 1.02e-19

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: 1.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470   544 LFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEM---KLSDGSYFGEICLLTRGRR 618
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVykVLEDGEEQivgTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 156071470   619 TASVRADTY--CRLYSLSVDNFNEVLEEYPMMRRAFE 653
Cdd:smart00100  81 AASAAAVALelATLLRIDFRDFLQLLPELPQLLLELL 117
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 545-673 4.20e-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: 86.58  E-value: 4.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 545 FANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSV--LTKGNKEMKLS---DGSYFGEICLLTRGRRT 619
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDGREQILGflgPGDFFGELSLLGGEPSP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156071470 620 ASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHK 673
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFL 134
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 562-645 3.23e-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: 3.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  562 FEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTK---GNKEM--KLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVD 636
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTledGREQIlaVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*....
gi 156071470  637 NFNEVLEEY 645
Cdd:pfam00027  81 DFLELLERD 89
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
571-646 1.38e-08

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 56.14  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 571 IIREGTIGKKMYFIQHGVVSVLTKGN--KEM---KLSDGSYFGEICLLTRG-RRTASVRADTYCRLYSLSVDNFNEVLEE 644
Cdd:PRK11753  31 LIHAGEKAETLYYIVKGSVAVLIKDEegKEMilsYLNQGDFIGELGLFEEGqERSAWVRAKTACEVAEISYKKFRQLIQV 110


                 ..
gi 156071470 645 YP 646
Cdd:PRK11753 111 NP 112
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 57-185 9.02e-05

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 46.21  E-value: 9.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  57 RAEALPPEAADEGGPRGRL----RSRDSSCGRPGTPGAASTAKGSPNGECGRGEPQCSPAGPEGPARGPKVSFSCRGAAS 132
Cdd:COG5180  337 RPAGVPEAASDAGQPPSAYppaeEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALD 416

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156071470 133 GPAPGPGPAEEAGSEEAGPAGEPRGSQASF-MQRQFGALLQPGVNKF-SLRMFGS 185
Cdd:COG5180  417 GGGRETASLGGAAGGAGQGPKADFVPGDAEsVSGPAGLADQAGAAAStAMADFVA 471
PHA03378 PHA03378
EBNA-3B; Provisional
 62-200 3.31e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.67  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  62 PPEaadegGPRGRLRSRDSSCGRPGTPGAASTAKGSPNGECGRGE-PQCSPAGPEGPARGPKVSFSCRGAASGPAPGPGP 140
Cdd:PHA03378 706 PPA-----APPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARpPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPP 780

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156071470 141 aeeagseEAGPAG--EPRGSQASFMQRQFGallqPGVNKFSLRMFGSQKAVEREQERVKSAG 200
Cdd:PHA03378 781 -------QAPPAPqqRPRGAPTPQPPPQAG----PTSMQLMPRAAPGQQGPTKQILRQLLTG 831
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 527-608 5.72e-04

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 43.17  E-value: 5.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470 527 REEIVNFncrklVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTK----GNKEMKLS 602
Cdd:PLN02868   3 TESVVEF-----LGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPaeeeSRPEFLLK 77


                 ....*.
gi 156071470 603 DGSYFG 608
Cdd:PLN02868  78 RYDYFG 83
PHA03378 PHA03378
EBNA-3B; Provisional
 59-173 1.84e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.98  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  59 EALPPEAADEGGPRGRLRSRDSSCGRPGTPGAASTAKGSPNGECGRGEPQCSPAGPEGPARGPKvsfscrgaaSGPAPGP 138
Cdd:PHA03378 728 AAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPR---------GAPTPQP 798

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 156071470 139 GP---------AEEAGSEEAGPA--------------GEPRGSQASFMQRQFGALLQP 173
Cdd:PHA03378 799 PPqagptsmqlMPRAAPGQQGPTkqilrqlltggvkrGRPSLKKPAALERQAAAGPTP 856
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 58-161 2.67e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470   58 AEALPPEAADEGGPRGRLRSRDSSCGRPGTPGAASTAKGSPNGECGRGEPQCSPAGPEGPARGPKVSfSCRGAASGPAPG 137
Cdd:PHA03307  280 SRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPS-PSRSPSPSRPPP 358

                          90       100       110
                  ....*....|....*....|....*....|...
gi 156071470  138 P---------GPAEEAGSEEAGPAGEPRGSQAS 161
Cdd:PHA03307  359 PadpssprkrPRPSRAPSSPAASAGRPTRRRAR 391
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 62-155 3.02e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 41.04  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  62 PPEAADEGGPRGR-----------LRSRDSSCGRPGTPGAASTAKGSPNGEcgRGEP----QCSPAGPEGPA-----RGP 121
Cdd:NF038329 187 PAGEKGPQGPRGEtgpageqgpagPAGPDGEAGPAGEDGPAGPAGDGQQGP--DGDPgptgEDGPQGPDGPAgkdgpRGD 264

                         90       100       110
                 ....*....|....*....|....*....|....
gi 156071470 122 KvsfscrgaasGPAPGPGPAEEAGseEAGPAGEP 155
Cdd:NF038329 265 R----------GEAGPDGPDGKDG--ERGPVGPA 286
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 61-166 4.22e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  61 LPPEAADEGGPRGRL-----RSRDSSCGRPGTPGAASTAKGSPngecgrgEPQCSPAGPEGPARGPKVSFSCRGAASGPA 135
Cdd:PRK07764 364 LPSASDDERGLLARLerlerRLGVAGGAGAPAAAAPSAAAAAP-------AAAPAPAAAAPAAAAAPAPAAAPQPAPAPA 436

                         90       100       110
                 ....*....|....*....|....*....|.
gi 156071470 136 PGPGPAEEAGSEEAGPAGEPRGSQASFMQRQ 166
Cdd:PRK07764 437 PAPAPPSPAGNAPAGGAPSPPPAAAPSAQPA 467
PHA03169 PHA03169
hypothetical protein; Provisional
 64-158 6.38e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.95  E-value: 6.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  64 EAADEGGPRGRlrsrdsscGRPGTPGAASTAKGSPNGECGRGEPQC-SPAGPEGPARgpkvsfscRGAASGPAPGPGPAE 142
Cdd:PHA03169  85 EERGQGGPSGS--------GSESVGSPTPSPSGSAEELASGLSPENtSGSSPESPAS--------HSPPPSPPSHPGPHE 148

                         90
                 ....*....|....*.
gi 156071470 143 EAGSEEAGPAGEPRGS 158
Cdd:PHA03169 149 PAPPESHNPSPNQQPS 164
PHA03381 PHA03381
tegument protein VP22; Provisional
 65-209 7.35e-03

tegument protein VP22; Provisional


Pssm-ID: 177618 [Multi-domain]  Cd Length: 290  Bit Score: 39.22  E-value: 7.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156071470  65 AADEGGPRGRLRSRDSSCGrPGTPGAAStAKGSPNGECGRGEPQCSPAGPEGPARGPKVSFSCRG----AASGPAPGPGP 140
Cdd:PHA03381  78 SSEDERPADPRPSRRPHAQ-PEASGPGP-ARGARGPAGSRGRGRRAESPSPRDPPNPKGASAPRGrksaCADSAALLDAP 155

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156071470 141 AEEAGSEEAGPAGEPRGSQASFMQRQFGALLQPGVNKFSLRMFGSqkAVER---EQERVKSAGAW-IIHPYSD 209
Cdd:PHA03381 156 APAAPKRQKTPAGLARKLHFSTAPTSPTAPWTPRVAGFNKRTFCA--AVGRvaaTHARMAAAQLWdLSHPRND 226
 
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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