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Conserved domains on  [gi|32565518|ref|NP_495439|]
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RING-type E3 ubiquitin transferase [Caenorhabditis elegans]

Protein Classification

zinc finger family protein( domain architecture ID 706824)

zinc finger family protein may be involved in transcriptional regulation; similar to Schizosaccharomyces pombe E3 ubiquitin-protein ligase hel2, which that plays a key role in the ribosome quality control (RQC), and Homo sapiens histone H4 transcription factor

Gene Ontology:  GO:0008270
PubMed:  11179890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5236 super family cl28715
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
47-356 3.48e-35

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


The actual alignment was detected with superfamily member COG5236:

Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 140.93  E-value: 3.48e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565518  47 NPARQNQSSRQPTKVDMKKYERMISAAHTNFSDipcgQKSIDCDICCKKNDVFGIGSCRHPVCAECVIRMRILGNSKTCP 126
Cdd:COG5236  26 KPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTD----EENMNCQICAGSTTYSARYPCGHQICHACAVRLRALYMQKGCP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565518 127 VCRSDIDILSFctTDDDLANVplSFKKTAHPDEDRYDIRFSNKIAGTKYEKYLAHVCKICKTDdgerLEFPSFMSLRQHM 206
Cdd:COG5236 102 LCRTETEAVVF--TASSPADI--TDRRQWKGREEKVGIFYEGEDVRDEMEDLLSFKCPKSKCH----RRCGSLKELKKHY 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565518 207 ASRHEQSYCHICTDNLNLFSRERKTYTRDQLQRHMRSGDfDDKSFKGHPQCLFCEQKFLDEENRYRHLRKDHFFCQFCES 286
Cdd:COG5236 174 KAQHGFVLCSECIGNKKDFWNEIRLFRSSTLRDHKNGGL-EEEGFKGHPLCIFCKIYFYDDDELRRHCRLRHEACHICDM 252

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32565518 287 DGTMTNVFFGKHDGLKKHYKEHHYICETEECREMG-IAFANKFELDLHRANEHAERRNLIELGFGQRPSDP 356
Cdd:COG5236 253 VGPIRYQYFKSYEDLEAHFRNAHYCCTFQTCRVGKcYVFPYHTELLEHLTRFHKVNARLSEIPRPGRCSIP 323
 
Name Accession Description Interval E-value
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
47-356 3.48e-35

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 140.93  E-value: 3.48e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565518  47 NPARQNQSSRQPTKVDMKKYERMISAAHTNFSDipcgQKSIDCDICCKKNDVFGIGSCRHPVCAECVIRMRILGNSKTCP 126
Cdd:COG5236  26 KPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTD----EENMNCQICAGSTTYSARYPCGHQICHACAVRLRALYMQKGCP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565518 127 VCRSDIDILSFctTDDDLANVplSFKKTAHPDEDRYDIRFSNKIAGTKYEKYLAHVCKICKTDdgerLEFPSFMSLRQHM 206
Cdd:COG5236 102 LCRTETEAVVF--TASSPADI--TDRRQWKGREEKVGIFYEGEDVRDEMEDLLSFKCPKSKCH----RRCGSLKELKKHY 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565518 207 ASRHEQSYCHICTDNLNLFSRERKTYTRDQLQRHMRSGDfDDKSFKGHPQCLFCEQKFLDEENRYRHLRKDHFFCQFCES 286
Cdd:COG5236 174 KAQHGFVLCSECIGNKKDFWNEIRLFRSSTLRDHKNGGL-EEEGFKGHPLCIFCKIYFYDDDELRRHCRLRHEACHICDM 252

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32565518 287 DGTMTNVFFGKHDGLKKHYKEHHYICETEECREMG-IAFANKFELDLHRANEHAERRNLIELGFGQRPSDP 356
Cdd:COG5236 253 VGPIRYQYFKSYEDLEAHFRNAHYCCTFQTCRVGKcYVFPYHTELLEHLTRFHKVNARLSEIPRPGRCSIP 323
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
 88-137 1.60e-20

RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ZNF598 associates with eukaryotic initiation factor 4E (eIF4E) homologous protein from mammals (m4EHP) by binding to Grb10-interacting GYF protein 2 (GIGYF2). The m4EHP-GIGYF2 complex functions as a translational repressor and is essential for normal embryonic development of mammalian. ZNF598 harbors a C3HC4-type RING-HC finger at its N-terminus.


Pssm-ID: 438277 [Multi-domain]  Cd Length: 51  Bit Score: 85.36  E-value: 1.60e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 32565518  88 DCDICCKKNDVFGIGSCRHPVCAECVIRMRILGNSKTCPVCRSDIDILSF 137
Cdd:cd16615   2 TCVICCEEIEYFAVGPCNHPVCYKCSLRMRVLYKDKYCPICRTELDKVIF 51
zf-RING_5 pfam14634
zinc-RING finger domain;
89-130 4.43e-05

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 41.64  E-value: 4.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 32565518    89 CDICCK---KNDVFGIGSCRHPVCAECVIRmriLGNSKTCPVCRS 130
Cdd:pfam14634   2 CNKCFKelsKTRPFYLTSCGHIFCEECLTR---LLQERQCPICKK 43
PHA02929 PHA02929
N1R/p28-like protein; Provisional
 85-129 2.33e-03

N1R/p28-like protein; Provisional


Pssm-ID: 222944 [Multi-domain]  Cd Length: 238  Bit Score: 40.53  E-value: 2.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 32565518   85 KSIDCDICCK-------KNDVFGIGS-CRHPVCAECVIRMRilGNSKTCPVCR 129
Cdd:PHA02929 173 KDKECAICMEkvydkeiKNMYFGILSnCNHVFCIECIDIWK--KEKNTCPVCR 223
 
Name Accession Description Interval E-value
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
47-356 3.48e-35

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 140.93  E-value: 3.48e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565518  47 NPARQNQSSRQPTKVDMKKYERMISAAHTNFSDipcgQKSIDCDICCKKNDVFGIGSCRHPVCAECVIRMRILGNSKTCP 126
Cdd:COG5236  26 KPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTD----EENMNCQICAGSTTYSARYPCGHQICHACAVRLRALYMQKGCP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565518 127 VCRSDIDILSFctTDDDLANVplSFKKTAHPDEDRYDIRFSNKIAGTKYEKYLAHVCKICKTDdgerLEFPSFMSLRQHM 206
Cdd:COG5236 102 LCRTETEAVVF--TASSPADI--TDRRQWKGREEKVGIFYEGEDVRDEMEDLLSFKCPKSKCH----RRCGSLKELKKHY 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565518 207 ASRHEQSYCHICTDNLNLFSRERKTYTRDQLQRHMRSGDfDDKSFKGHPQCLFCEQKFLDEENRYRHLRKDHFFCQFCES 286
Cdd:COG5236 174 KAQHGFVLCSECIGNKKDFWNEIRLFRSSTLRDHKNGGL-EEEGFKGHPLCIFCKIYFYDDDELRRHCRLRHEACHICDM 252

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32565518 287 DGTMTNVFFGKHDGLKKHYKEHHYICETEECREMG-IAFANKFELDLHRANEHAERRNLIELGFGQRPSDP 356
Cdd:COG5236 253 VGPIRYQYFKSYEDLEAHFRNAHYCCTFQTCRVGKcYVFPYHTELLEHLTRFHKVNARLSEIPRPGRCSIP 323
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
 88-137 1.60e-20

RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ZNF598 associates with eukaryotic initiation factor 4E (eIF4E) homologous protein from mammals (m4EHP) by binding to Grb10-interacting GYF protein 2 (GIGYF2). The m4EHP-GIGYF2 complex functions as a translational repressor and is essential for normal embryonic development of mammalian. ZNF598 harbors a C3HC4-type RING-HC finger at its N-terminus.


Pssm-ID: 438277 [Multi-domain]  Cd Length: 51  Bit Score: 85.36  E-value: 1.60e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 32565518  88 DCDICCKKNDVFGIGSCRHPVCAECVIRMRILGNSKTCPVCRSDIDILSF 137
Cdd:cd16615   2 TCVICCEEIEYFAVGPCNHPVCYKCSLRMRVLYKDKYCPICRTELDKVIF 51
zf-RING_5 pfam14634
zinc-RING finger domain;
89-130 4.43e-05

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 41.64  E-value: 4.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 32565518    89 CDICCK---KNDVFGIGSCRHPVCAECVIRmriLGNSKTCPVCRS 130
Cdd:pfam14634   2 CNKCFKelsKTRPFYLTSCGHIFCEECLTR---LLQERQCPICKK 43
RING-HC_CeBARD1-like cd23143
RING finger, HC subclass, found in Caenorhabditis elegans BRCA1-associated RING domain protein ...
 87-133 1.85e-04

RING finger, HC subclass, found in Caenorhabditis elegans BRCA1-associated RING domain protein 1 (CeBARD1) and similar proteins; CeBARD1, also called Ce-BRD-1, Cebrd-1, or RING-type E3 ubiquitin transferase BARD1, is a constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity. It plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by ionizing radiation. It protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability. CeBARD1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438505 [Multi-domain]  Cd Length: 47  Bit Score: 39.84  E-value: 1.85e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 32565518  87 IDCDICCKKN-DVFGIGSCRHPVCAECVirMRILGNSKTCPVCRSDID 133
Cdd:cd23143   2 IECVICSEPQiDTFLLSSCGHIYCWECF--TEFIEKRHMCPSCRFPLD 47
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
89-133 6.81e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 38.51  E-value: 6.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 32565518    89 CDICCKKNDVFGIGSCRH-PVCAECVIRMRilGNSKTCPVCRSDID 133
Cdd:pfam13920   5 CVICLDRPRNVVLLPCGHlCLCEECAERLL--RKKKKCPICRQPIE 48
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 89-128 9.27e-04

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 37.85  E-value: 9.27e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 32565518  89 CDICCKKNDVFGIGSCRHPVCAECVIRMrILGNSKTCPVC 128
Cdd:cd16449   3 CPICLERLKDPVLLPCGHVFCRECIRRL-LESGSIKCPIC 41
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 89-129 1.25e-03

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438112 [Multi-domain]  Cd Length: 43  Bit Score: 37.38  E-value: 1.25e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 32565518  89 CDICCKK---NDVFGIGSCRHPVCAECvIRMRILGNSKTCPVCR 129
Cdd:cd16448   1 CVICLEEfeeGDVVRLLPCGHVFHLAC-ILRWLESGNNTCPLCR 43
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
 89-132 1.34e-03

RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) and similar proteins; RSPRY1 is a hypothetical RING and SPRY domain-containing protein of unknown physiological function. Mutations in its corresponding gene RSPRY1 may associate with a distinct skeletal dysplasia syndrome. RSPRY1 contains a B30.2/SPRY domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438228 [Multi-domain]  Cd Length: 43  Bit Score: 37.34  E-value: 1.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 32565518  89 CDICCKKNDVFGIGSCRHP-VCAECVIRMrilgnsKTCPVCRSDI 132
Cdd:cd16566   5 CTLCFDKVADTELRPCGHSgFCMECALQL------ETCPLCRQPI 43
zf-RING_2 pfam13639
Ring finger domain;
87-129 1.34e-03

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 37.39  E-value: 1.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 32565518    87 IDCDICCkknDVFGIGS------CRHPVCAECVirMRILGNSKTCPVCR 129
Cdd:pfam13639   1 DECPICL---EEFEEGDkvvvlpCGHHFHRECL--DKWLRSSNTCPLCR 44
PHA02929 PHA02929
N1R/p28-like protein; Provisional
 85-129 2.33e-03

N1R/p28-like protein; Provisional


Pssm-ID: 222944 [Multi-domain]  Cd Length: 238  Bit Score: 40.53  E-value: 2.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 32565518   85 KSIDCDICCK-------KNDVFGIGS-CRHPVCAECVIRMRilGNSKTCPVCR 129
Cdd:PHA02929 173 KDKECAICMEkvydkeiKNMYFGILSnCNHVFCIECIDIWK--KEKNTCPVCR 223
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
 88-134 2.68e-03

RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; RNF222 is an uncharacterized C3HC4-type RING-HC finger-containing protein. It may function as an E3 ubiquitin-protein ligase.


Pssm-ID: 438226 [Multi-domain]  Cd Length: 50  Bit Score: 36.61  E-value: 2.68e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 32565518  88 DCDICCKKNDVFG-IGSCRHPVCAECVIRMrILGNSKTCPVCRSDIDI 134
Cdd:cd16564   2 ECPVCYEDFDDAPrILSCGHSFCEDCLVKQ-LVSMTISCPICRRVTFI 48
RING-HC_MKRN cd16521
RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily ...
 87-129 4.77e-03

RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily includes ribonucleoproteins that are characterized by a variety of zinc-finger motifs, including typical arrays of one to four C3H1-type zinc fingers and a C3HC4-type RING-HC finger. Another motif rich in Cys and His residues (CH), with so far unknown function, is also generally present in MKRN proteins. MKRN proteins may have E3 ubiquitin ligase activity.


Pssm-ID: 438184 [Multi-domain]  Cd Length: 53  Bit Score: 36.10  E-value: 4.77e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 32565518  87 IDCDIC----CKKNDVFGIGS-CRHPVCAECvIRM------RILGNSKTCPVCR 129
Cdd:cd16521   1 IECGICmevvLEKERRFGILSnCNHVFCLEC-IREwrsskdFENSIVRSCPICR 53
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
 89-132 9.00e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; Cbl-c, also known as RING finger protein 57 (RNF57), SH3-binding protein Cbl-3, SH3-binding protein Cbl-c, or signal transduction protein Cbl-c, is an E3 ubiquitin-protein ligase expressed exclusively in epithelial cells. It contains a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a C3HC4-type RING-HC finger, and a short proline-rich region, but lacks the ubiquitin-associated (UBA) leucine zipper motif that are present in Cbl and Cbl-b. Cbl-c acts as a regulator of epidermal growth factor receptor (EGFR)-mediated signal transduction. It also suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation. Moreover, Cbl-c ubiquitinates and downregulates RETMEN2A and implicates Enigma (PDLIM7) as a positive regulator of RETMEN2A by blocking Cbl-mediated ubiquitination and degradation. The ubiquitin ligase activity of Cbl-c is increased via the interaction of its RING-HC finger domain with a LIM domain of the paxillin homolog, hydrogen peroxide induced construct 5 (Hic-5).


Pssm-ID: 438370 [Multi-domain]  Cd Length: 65  Bit Score: 35.83  E-value: 9.00e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 32565518  89 CDICCKKNDVFGIGSCRHPVCAECVIRMRiLGNSKTCPVCRSDI 132
Cdd:cd16710  16 CKICAERDKDVRIEPCGHLLCSCCLAAWQ-HSDSQTCPFCRCEI 58
 
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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