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Conserved domains on  [gi|486295938|ref|WP_001574271|]
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MULTISPECIES: YtxH domain-containing protein [Bacilli]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CAF-1_p150 super family cl37818
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
539-687 1.38e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


The actual alignment was detected with superfamily member pfam11600:

Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 45.83  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  539 KEQVKDIPTNARYAVYQGKSKAKENVRDLTSSISQTRADRASGRKEQQEQRRKtiaERRSEMEQVKQKKQPAssvherpa 618
Cdd:pfam11600  20 KDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERR---EKKEKDEKEKAEKLRL-------- 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 486295938  619 tKQEQSHDGQTAKQssiqtSRMESQQAKQERPAVKSDSLSLKAERQNRTtqeRTVQKPATSTTPADRAS 687
Cdd:pfam11600  89 -KEEKRKEKQEALE-----AKLEEKRKKEEEKRLKEEEKRIKAEKAEIT---RFLQKPKTQQAPKTLAG 148
SLC5-6-like_sbd super family cl00456
Solute carrier families 5 and 6-like; solute binding domain; This superfamily includes the ...
311-460 1.83e-03

Solute carrier families 5 and 6-like; solute binding domain; This superfamily includes the solute-binding domain of SLC5 proteins (also called the sodium/glucose cotransporters or solute sodium symporters), SLC6 proteins (also called the sodium- and chloride-dependent neurotransmitter transporters or Na+/Cl--dependent transporters), and nucleobase-cation-symport-1 (NCS1) transporters. SLC5s co-transport Na+ with sugars, amino acids, inorganic ions or vitamins. SLC6s include Na+/Cl--dependent plasma membrane transporters for the monoamine neurotransmitters serotonin, dopamine, and norepinephrine, and the amino acid neurotransmitters GABA and glycine. NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. Members of this superfamily are important in human physiology and disease. They contain a functional core of 10 transmembrane helices (TMs): an inverted structural repeat, TMs1-5 and TMs6-10; TMs numbered to conform to the SLC6 Aquifex aeolicus LeuT.


The actual alignment was detected with superfamily member pfam01490:

Pssm-ID: 444915  Cd Length: 410  Bit Score: 41.14  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  311 TKTINRLGTVFFLF---VFNIGISIFVFLLTGIMI------------FSQVLFIIyaMFLPVSFILSMIPSFDGMSkraI 375
Cdd:pfam01490  76 YRLLGPKGRLLILFailLNLFGVCISYLIFAGDNLpaifdsffdtcpISLVYFII--IFGLIFIPLSFIPNLSALS---I 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  376 IKLFNTILTRAGITLIITTAFSIST---MLYTLSAGYPFFLIAflQIVTFAG-IYFKLSDLMSMFSLQSNdsqsvgsrvM 451
Cdd:pfam01490 151 LSLLAAVSSLYYIVILVLSVAEGIVltaQGVGHLGSKTNIKLA--GTFLAIGiIVFAFEGHAVLLPIQNE---------M 219

                  ....*....
gi 486295938  452 RKPRMLMHA 460
Cdd:pfam01490 220 KNPSKFKAM 228
 
Name Accession Description Interval E-value
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
539-687 1.38e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 45.83  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  539 KEQVKDIPTNARYAVYQGKSKAKENVRDLTSSISQTRADRASGRKEQQEQRRKtiaERRSEMEQVKQKKQPAssvherpa 618
Cdd:pfam11600  20 KDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERR---EKKEKDEKEKAEKLRL-------- 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 486295938  619 tKQEQSHDGQTAKQssiqtSRMESQQAKQERPAVKSDSLSLKAERQNRTtqeRTVQKPATSTTPADRAS 687
Cdd:pfam11600  89 -KEEKRKEKQEALE-----AKLEEKRKKEEEKRLKEEEKRIKAEKAEIT---RFLQKPKTQQAPKTLAG 148
PTZ00121 PTZ00121
MAEBL; Provisional
557-701 3.13e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  557 KSKAKENVRDLTSSISQTRadRASGRKEQQEQRRKTIAERRSEMEQVKQKKQPASSVHERPATKQEQSHDGQTAKQSSIQ 636
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAK--KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486295938  637 TSRMESQQAKQERPAV-KSDSLSLKAERQNRTTQErtVQKPATSTTPADRASQRPVTKERPSTVQR 701
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKkKADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
517-602 9.38e-04

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 39.18  E-value: 9.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938 517 IGQTIGAVA----------DTKDKIVDSAGNLKEQVKDIPTNARYAVYQGKSKAKENVRDLTSSISQTradrASGRKEQQ 586
Cdd:COG4980   12 VGAAVGAAAgllfapksgkETRKKLKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEK----IEELKEEV 87
                         90
                 ....*....|....*.
gi 486295938 587 EQRRKTIAERRSEMEQ 602
Cdd:COG4980   88 EPKIEELKEEAEKLQK 103
Aa_trans pfam01490
Transmembrane amino acid transporter protein; This transmembrane region is found in many amino ...
311-460 1.83e-03

Transmembrane amino acid transporter protein; This transmembrane region is found in many amino acid transporters including UNC-47 and MTR. UNC-47 encodes a vesicular amino butyric acid (GABA) transporter, (VGAT). UNC-47 is predicted to have 10 transmembrane domains. MTR is a N system amino acid transporter system protein involved in methyltryptophan resistance. Other members of this family include proline transporters and amino acid permeases.


Pssm-ID: 279788  Cd Length: 410  Bit Score: 41.14  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  311 TKTINRLGTVFFLF---VFNIGISIFVFLLTGIMI------------FSQVLFIIyaMFLPVSFILSMIPSFDGMSkraI 375
Cdd:pfam01490  76 YRLLGPKGRLLILFailLNLFGVCISYLIFAGDNLpaifdsffdtcpISLVYFII--IFGLIFIPLSFIPNLSALS---I 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  376 IKLFNTILTRAGITLIITTAFSIST---MLYTLSAGYPFFLIAflQIVTFAG-IYFKLSDLMSMFSLQSNdsqsvgsrvM 451
Cdd:pfam01490 151 LSLLAAVSSLYYIVILVLSVAEGIVltaQGVGHLGSKTNIKLA--GTFLAIGiIVFAFEGHAVLLPIQNE---------M 219

                  ....*....
gi 486295938  452 RKPRMLMHA 460
Cdd:pfam01490 220 KNPSKFKAM 228
 
Name Accession Description Interval E-value
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
539-687 1.38e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 45.83  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  539 KEQVKDIPTNARYAVYQGKSKAKENVRDLTSSISQTRADRASGRKEQQEQRRKtiaERRSEMEQVKQKKQPAssvherpa 618
Cdd:pfam11600  20 KDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERR---EKKEKDEKEKAEKLRL-------- 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 486295938  619 tKQEQSHDGQTAKQssiqtSRMESQQAKQERPAVKSDSLSLKAERQNRTtqeRTVQKPATSTTPADRAS 687
Cdd:pfam11600  89 -KEEKRKEKQEALE-----AKLEEKRKKEEEKRLKEEEKRIKAEKAEIT---RFLQKPKTQQAPKTLAG 148
PTZ00121 PTZ00121
MAEBL; Provisional
557-701 3.13e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  557 KSKAKENVRDLTSSISQTRadRASGRKEQQEQRRKTIAERRSEMEQVKQKKQPASSVHERPATKQEQSHDGQTAKQSSIQ 636
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAK--KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486295938  637 TSRMESQQAKQERPAV-KSDSLSLKAERQNRTTQErtVQKPATSTTPADRASQRPVTKERPSTVQR 701
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKkKADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
517-602 9.38e-04

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 39.18  E-value: 9.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938 517 IGQTIGAVA----------DTKDKIVDSAGNLKEQVKDIPTNARYAVYQGKSKAKENVRDLTSSISQTradrASGRKEQQ 586
Cdd:COG4980   12 VGAAVGAAAgllfapksgkETRKKLKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEK----IEELKEEV 87
                         90
                 ....*....|....*.
gi 486295938 587 EQRRKTIAERRSEMEQ 602
Cdd:COG4980   88 EPKIEELKEEAEKLQK 103
PRK12757 PRK12757
cell division protein FtsN; Provisional
594-723 1.22e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 41.18  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938 594 AERRSEMEQVK-QKKQPASSVHERPatkqeqsHDGQTAKQSSIQTSRMesQQAKQERPavksdslslkaerQNRTTQERT 672
Cdd:PRK12757  82 DEQRQLLEQMQaDMRQQPTQLSEVP-------YNEQTPQVPRSTVQIQ--QQAQQQQP-------------PATTAQPQP 139
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 486295938 673 VQKPATSTTPADRASQRPVTKERPSTVQRVQSqnlrnrPPIKSATIKKGSK 723
Cdd:PRK12757 140 VTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVE------APKVEAEKEKEQR 184
Aa_trans pfam01490
Transmembrane amino acid transporter protein; This transmembrane region is found in many amino ...
311-460 1.83e-03

Transmembrane amino acid transporter protein; This transmembrane region is found in many amino acid transporters including UNC-47 and MTR. UNC-47 encodes a vesicular amino butyric acid (GABA) transporter, (VGAT). UNC-47 is predicted to have 10 transmembrane domains. MTR is a N system amino acid transporter system protein involved in methyltryptophan resistance. Other members of this family include proline transporters and amino acid permeases.


Pssm-ID: 279788  Cd Length: 410  Bit Score: 41.14  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  311 TKTINRLGTVFFLF---VFNIGISIFVFLLTGIMI------------FSQVLFIIyaMFLPVSFILSMIPSFDGMSkraI 375
Cdd:pfam01490  76 YRLLGPKGRLLILFailLNLFGVCISYLIFAGDNLpaifdsffdtcpISLVYFII--IFGLIFIPLSFIPNLSALS---I 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  376 IKLFNTILTRAGITLIITTAFSIST---MLYTLSAGYPFFLIAflQIVTFAG-IYFKLSDLMSMFSLQSNdsqsvgsrvM 451
Cdd:pfam01490 151 LSLLAAVSSLYYIVILVLSVAEGIVltaQGVGHLGSKTNIKLA--GTFLAIGiIVFAFEGHAVLLPIQNE---------M 219

                  ....*....
gi 486295938  452 RKPRMLMHA 460
Cdd:pfam01490 220 KNPSKFKAM 228
PIG-U pfam06728
GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via ...
321-394 3.07e-03

GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via glycosylphosphatidylinositol (GPI), which is posttranslationally attached to the carboxyl-terminus by GPI transamidase. The mammalian GPI transamidase is a complex of at least four subunits, GPI8, GAA1, PIG-S, and PIG-T. PIG-U is thought to represent a fifth subunit in this complex and may be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.


Pssm-ID: 429085  Cd Length: 375  Bit Score: 40.67  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  321 FFLFVFNIGISIFVFLLTgIMIFSQVLFI------IYAMFLP------VSFILSMIPSFDGMSKRaiikLFNTILTraGI 388
Cdd:pfam06728 269 FFLFVFNLHPFIYILPLT-IRLRKQPLFAltlllgLISIFKPyptlgdLGLYLSLLPLFRHLFPY----MRYSFLI--GL 341

                  ....*.
gi 486295938  389 TLIITT 394
Cdd:pfam06728 342 TLLVAL 347
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
573-707 3.61e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.41  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938  573 QTRADRASGRKEQQEQRRKT--IAERRSEMEQVKQKK--QPASSVHERPATKQEQSHDGQTAKQSSIQTSRMESQQAK-- 646
Cdd:pfam15558  45 QETLERERRLLLQQSQEQWQaeKEQRKARLGREERRRadRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKqc 124
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486295938  647 QERpavksdslSLKA-ERQNRTTQERTVQKPATSTTPADRASQRPVTKERpstvQRVQSQNL 707
Cdd:pfam15558 125 QEQ--------RLKEkEEELQALREQNSLQLQERLEEACHKRQLKEREEQ----KKVQENNL 174
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
573-689 4.44e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.41  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938 573 QTRADRASGRK-EQQEQRRKTIAERRSEMEQVKQKKQPASSVHERPATKQeqshdgqtAKQssiqtSRMESQQAKQERPA 651
Cdd:COG3064    7 EKAAEAAAQERlEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEE--------ARE-----AKAEAEQRAAELAA 73
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 486295938 652 VKSDSLSlKAERQNRTTQERTVQKPATSTTPADRASQR 689
Cdd:COG3064   74 EAAKKLA-EAEKAAAEAEKKAAAEKAKAAKEAEAAAAA 110
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
555-675 4.67e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938 555 QGKSKAKENVRDLTSSISQTRADRASGRKEQQEQRRKtIAERRSEMEQVKQKKQpasSVHERPATKQEQshdgQTAKQSS 634
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE-LEQARSELEQLEEELE---ELNEQLQAAQAE----LAQAQEE 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 486295938 635 IQTSRMESQQAKQERPAVKSDSLSLKAERQNRTTQERTVQK 675
Cdd:COG4372  103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
499-687 6.73e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 6.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938 499 QADHTRPDGQEKSTLGKRIGQTIGAVADTKDKIVDSAGNLKEQVKDIptnaryavyqgkSKAKENVRDLTSSISQTRADR 578
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI------------AALARRIRALEQELAALEAEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486295938 579 ASGRKEQQEQRRKtIAERRSEMEQV-----KQKKQPASSVHERPATKQEQSHDGQTAKQ-SSIQTSRMESQQAKQERPAV 652
Cdd:COG4942   86 AELEKEIAELRAE-LEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAA 164
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 486295938 653 KSDSLSLKAERQNRTTQERTVQKPATSTTPADRAS 687
Cdd:COG4942  165 LRAELEAERAELEALLAELEEERAALEALKAERQK 199
 
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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