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Conserved domains on  [gi|1720366656|ref|XP_030101975|]
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rho guanine nucleotide exchange factor 15 isoform X13 [Mus musculus]

Protein Classification

PH domain-containing RhoGEF family protein( domain architecture ID 10646143)

PH domain-containing RhoGEF (rho guanine nucleotide exchange factor) family protein similar to RhoGEF and PH (pleckstrin homology) domain regions of RhoGEFs that accelerate the intrinsic exchange activity of Rho GTPases to stimulate formation of Rho-GTP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
430-606 2.19e-34

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


:

Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 129.34  E-value: 2.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656  430 LFEVVTSEASYLRSLRLLTDTFVLS-QALRDTLTPRDHHTLFSNVQRVQSVSERFLGTLLSRVRSSPHITD-LCDVVHAH 507
Cdd:smart00325   2 LKELLQTERNYVRDLKLLVEVFLKPlKKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVErIGDVFLKL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656  508 AvgPFF-VYVDYVRNQQYQEETYSRLMDtNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILSQTEEGS 586
Cdd:smart00325  82 E--EFFkIYSEYCSNHPDALELLKKLKK-NPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDH 158
                          170       180
                   ....*....|....*....|
gi 1720366656  587 SRQENAQKALGAVSKIIERC 606
Cdd:smart00325 159 EDREDLKKALKAIKELANQV 178
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
630-691 4.70e-06

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd01221:

Pssm-ID: 473070  Cd Length: 131  Bit Score: 46.48  E-value: 4.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366656 630 KVKALPLVSWSRRLELQGELTELGCRRGGVLFTSRPRFTPLCLLLFSDLLLITQPKRPSRFL 691
Cdd:cd01221     1 KIKAFPLISSSRWLVKRGELTELVEDGGSLTFRKKFSKTPVYLFLFNDLLLITKKKSEERYL 62
 
Name Accession Description Interval E-value
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
430-606 2.19e-34

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 129.34  E-value: 2.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656  430 LFEVVTSEASYLRSLRLLTDTFVLS-QALRDTLTPRDHHTLFSNVQRVQSVSERFLGTLLSRVRSSPHITD-LCDVVHAH 507
Cdd:smart00325   2 LKELLQTERNYVRDLKLLVEVFLKPlKKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVErIGDVFLKL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656  508 AvgPFF-VYVDYVRNQQYQEETYSRLMDtNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILSQTEEGS 586
Cdd:smart00325  82 E--EFFkIYSEYCSNHPDALELLKKLKK-NPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDH 158
                          170       180
                   ....*....|....*....|
gi 1720366656  587 SRQENAQKALGAVSKIIERC 606
Cdd:smart00325 159 EDREDLKKALKAIKELANQV 178
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
430-606 5.14e-34

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 128.19  E-value: 5.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656 430 LFEVVTSEASYLRSLRLLTDTFVLSQALRDTLTPRDHHTLFSNVQRVQSVSERFLgtLLSRVRSSPHITDLCDVVHAHAV 509
Cdd:pfam00621   2 IKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQRIGDIFLKFAP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656 510 GpFFVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILSQTEEGSSRQ 589
Cdd:pfam00621  80 G-FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPDY 158
                         170
                  ....*....|....*..
gi 1720366656 590 ENAQKALGAVSKIIERC 606
Cdd:pfam00621 159 EDLKKALEAIKEVAKQI 175
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
426-606 1.63e-30

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 118.55  E-value: 1.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656 426 MQESLFEVVTSEASYLRSLRLLTDTFVLSQALRDT-LTPRDHHTLFSNVQRVQSVSERFLGTLLSRVRSSPHITD-LCDV 503
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGPrIGDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656 504 VHAHAvgPFF-VYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSlpKCERLPLPSFLLLPFQRITRLRMLLQNILSQT 582
Cdd:cd00160    81 FLKLA--PFFkIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAES--ECGRLKLESLLLKPVQRLTKYPLLLKELLKHT 156
                         170       180
                  ....*....|....*....|....
gi 1720366656 583 EEGSSRQENAQKALGAVSKIIERC 606
Cdd:cd00160   157 PDGHEDREDLKKALEAIKEVASQV 180
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
415-628 3.30e-12

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 70.31  E-value: 3.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656  415 LLESLSPQERRMQESLFEVVTSEASYLRSLRLLTDTFVlSQALRDTLTPRDH-----HTLFSNVQRVQSVSERFLGTLLS 489
Cdd:COG5422    474 VWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWI-KPLEESNIIPENArrnfiKHVFANINEIYAVNSKLLKALTN 552
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656  490 RVRSSPHITDLCDVVHAHAvgPFF-VYVDYVRNQQYQEETYSRLMDTN---VRFSAELRRLQSlpkCERLPLPSFLLLPF 565
Cdd:COG5422    553 RQCLSPIVNGIADIFLDYV--PKFePFIKYGASQPYAKYEFEREKSVNpnfARFDHEVERLDE---SRKLELDGYLTKPT 627
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366656  566 QRITRLRMLLQNILSQTEEGSSRQENAQKALGAVSKIIERCSAEVGRMKQTEELIRLTQRLRF 628
Cdd:COG5422    628 TRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLFHLNQQLLF 690
PH_ephexin cd01221
Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine ...
630-691 4.70e-06

Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine nucleotide exchange factor) plays a role in the homeostatic modulation of presynaptic neurotransmitter release. Specific functions are still unknown for Ephexin-2 (also called RhoGEF19) and Ephexin-3 (also called Rho guanine nucleotide exchange factor 5/RhoGEF5, Transforming immortalized mammary oncogene/p60 TIM, and NGEF/neuronalGEF). Ephexin-4 (also called RhoGEF16) acts downstream of EphA2 to promote ligand-independent breast cancer cell migration and invasion toward epidermal growth factor through activation of RhoG. This in turn results in the activation of RhoG which recruits ELMO2 and Dock4 to form a complex with EphA2 at the tips of cortactin-rich protrusions in migrating breast cancer cells. Ephexin-5 is the specific GEF for RhoA activation and the regulation of vascular smooth muscle contractility. It interacts with EPHA4 PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. The members of the Ephexin family contains a RhoGEF (DH) followed by a PH domain and an SH3 domain. The ephexin PH domain is believed to act with the DH domain in mediating protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269929  Cd Length: 131  Bit Score: 46.48  E-value: 4.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366656 630 KVKALPLVSWSRRLELQGELTELGCRRGGVLFTSRPRFTPLCLLLFSDLLLITQPKRPSRFL 691
Cdd:cd01221     1 KIKAFPLISSSRWLVKRGELTELVEDGGSLTFRKKFSKTPVYLFLFNDLLLITKKKSEERYL 62
 
Name Accession Description Interval E-value
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
430-606 2.19e-34

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 129.34  E-value: 2.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656  430 LFEVVTSEASYLRSLRLLTDTFVLS-QALRDTLTPRDHHTLFSNVQRVQSVSERFLGTLLSRVRSSPHITD-LCDVVHAH 507
Cdd:smart00325   2 LKELLQTERNYVRDLKLLVEVFLKPlKKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVErIGDVFLKL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656  508 AvgPFF-VYVDYVRNQQYQEETYSRLMDtNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILSQTEEGS 586
Cdd:smart00325  82 E--EFFkIYSEYCSNHPDALELLKKLKK-NPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDH 158
                          170       180
                   ....*....|....*....|
gi 1720366656  587 SRQENAQKALGAVSKIIERC 606
Cdd:smart00325 159 EDREDLKKALKAIKELANQV 178
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
430-606 5.14e-34

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 128.19  E-value: 5.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656 430 LFEVVTSEASYLRSLRLLTDTFVLSQALRDTLTPRDHHTLFSNVQRVQSVSERFLgtLLSRVRSSPHITDLCDVVHAHAV 509
Cdd:pfam00621   2 IKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQRIGDIFLKFAP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656 510 GpFFVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILSQTEEGSSRQ 589
Cdd:pfam00621  80 G-FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPDY 158
                         170
                  ....*....|....*..
gi 1720366656 590 ENAQKALGAVSKIIERC 606
Cdd:pfam00621 159 EDLKKALEAIKEVAKQI 175
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
426-606 1.63e-30

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 118.55  E-value: 1.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656 426 MQESLFEVVTSEASYLRSLRLLTDTFVLSQALRDT-LTPRDHHTLFSNVQRVQSVSERFLGTLLSRVRSSPHITD-LCDV 503
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGPrIGDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656 504 VHAHAvgPFF-VYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSlpKCERLPLPSFLLLPFQRITRLRMLLQNILSQT 582
Cdd:cd00160    81 FLKLA--PFFkIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAES--ECGRLKLESLLLKPVQRLTKYPLLLKELLKHT 156
                         170       180
                  ....*....|....*....|....
gi 1720366656 583 EEGSSRQENAQKALGAVSKIIERC 606
Cdd:cd00160   157 PDGHEDREDLKKALEAIKEVASQV 180
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
415-628 3.30e-12

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 70.31  E-value: 3.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656  415 LLESLSPQERRMQESLFEVVTSEASYLRSLRLLTDTFVlSQALRDTLTPRDH-----HTLFSNVQRVQSVSERFLGTLLS 489
Cdd:COG5422    474 VWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWI-KPLEESNIIPENArrnfiKHVFANINEIYAVNSKLLKALTN 552
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366656  490 RVRSSPHITDLCDVVHAHAvgPFF-VYVDYVRNQQYQEETYSRLMDTN---VRFSAELRRLQSlpkCERLPLPSFLLLPF 565
Cdd:COG5422    553 RQCLSPIVNGIADIFLDYV--PKFePFIKYGASQPYAKYEFEREKSVNpnfARFDHEVERLDE---SRKLELDGYLTKPT 627
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366656  566 QRITRLRMLLQNILSQTEEGSSRQENAQKALGAVSKIIERCSAEVGRMKQTEELIRLTQRLRF 628
Cdd:COG5422    628 TRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLFHLNQQLLF 690
PH_ephexin cd01221
Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine ...
630-691 4.70e-06

Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine nucleotide exchange factor) plays a role in the homeostatic modulation of presynaptic neurotransmitter release. Specific functions are still unknown for Ephexin-2 (also called RhoGEF19) and Ephexin-3 (also called Rho guanine nucleotide exchange factor 5/RhoGEF5, Transforming immortalized mammary oncogene/p60 TIM, and NGEF/neuronalGEF). Ephexin-4 (also called RhoGEF16) acts downstream of EphA2 to promote ligand-independent breast cancer cell migration and invasion toward epidermal growth factor through activation of RhoG. This in turn results in the activation of RhoG which recruits ELMO2 and Dock4 to form a complex with EphA2 at the tips of cortactin-rich protrusions in migrating breast cancer cells. Ephexin-5 is the specific GEF for RhoA activation and the regulation of vascular smooth muscle contractility. It interacts with EPHA4 PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. The members of the Ephexin family contains a RhoGEF (DH) followed by a PH domain and an SH3 domain. The ephexin PH domain is believed to act with the DH domain in mediating protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269929  Cd Length: 131  Bit Score: 46.48  E-value: 4.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366656 630 KVKALPLVSWSRRLELQGELTELGCRRGGVLFTSRPRFTPLCLLLFSDLLLITQPKRPSRFL 691
Cdd:cd01221     1 KIKAFPLISSSRWLVKRGELTELVEDGGSLTFRKKFSKTPVYLFLFNDLLLITKKKSEERYL 62
 
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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