NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|545491197|ref|XP_005617625|]
View 

ubiquitin carboxyl-terminal hydrolase CYLD isoform X2 [Canis lupus familiaris]

Protein Classification

CYLD_phos_site and Peptidase_C19N domain-containing protein( domain architecture ID 11279563)

protein containing domains CYLD_phos_site, CAP_GLY, and Peptidase_C19N

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CYLD_phos_site pfam16607
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ...
 304-459 4.33e-112

Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region on a subset of tumour-suppressor and de-ubiquitinating enzyme CYLD proteins in eukaryotes. It lies between the second pair of CAP_GLY domains, pfam01302, on these proteins. This region of CYLD, being unstructured, carries a number of serine residues which, in response to cellular stimuli, become phosphorylated. This transient phosphorylation-state induces ubiquitination of TRAF2, a ubiquitin ligase that catalyzes both self-ubiquitination and the ubiquitination of specific target molecules involved in signal transduction.


:

Pssm-ID: 465194  Cd Length: 157  Bit Score: 341.55  E-value: 4.33e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197  304 PDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAK 383
Cdd:pfam16607   1 PESVSQERRPPKLAFASRGGGDKGSSSHNKPKATGSTSDPGNRNRSEFFYTLNGSSVDSQPQPKSKNTWYIDEVAEDPAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545491197  384 SLTEISPDFGHASPPLQPPSMNSLSTENRFHSLPFSLTKMPNTNGSIGHSPLSLSVQSVMGELNNAPVQESPPLAM 459
Cdd:pfam16607  81 SLTDTSPGFGHSSPPLQPPPTNSLSSENRFHSLPFSLTKMPSSNGSIGHSPLSLSVQSVMGELNTGPVQESPPSAA 156
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 590-945 7.06e-79

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


:

Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 256.68  E-value: 7.06e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 590 GIQGHYN-SCYLDSTLFCLFAfssvldtvllrpkekndvgyysetqellrteivnplriygyvcatkimklrkilekvea 668
Cdd:cd02670    1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 669 asgftsEEKDPEEFLNILFHQILR--VEPLLKIRSAGQKVQD------CYFYQIFMEKNEKVGVPTIQQLLEWSFINSNl 740
Cdd:cd02670   22 ------EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQDddklvnERLLQIPVPDDDDGGGITLEQCLEQYFNNSV- 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 741 kFAEAPSCLIIQMPRFGK----DFKLFKKIFPSLELNITDLLEDTPRQCRICGglamYECRECYDDPDISAGNIKQFCKT 816
Cdd:cd02670   95 -FAKAPSCLIICLKRYGKtegkAQKMFKKILIPDEIDIPDFVADDPRACSKCQ----LECRVCYDDKDFSPTCGKFKLSL 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 817 CNTQVHLHPKRlnhkynpvslpkdlpdwdwrhgcipcqkmelfavlciETSHYVAFVKYGKD----------DSAWLFFD 886
Cdd:cd02670  170 CSAVCHRGTSL-------------------------------------ETGHYVAFVRYGSYsltetdneayNAQWVFFD 212

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545491197 887 SMADRDGGQNGFNIPqvtpcpevgeylkmspedlhsldsrriqgcARRLLCDAYMCMYQ 945
Cdd:cd02670  213 DMADRDGVSNGFNIP------------------------------AARLLEDPYMLFYQ 241
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 469-537 6.06e-21

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 87.26  E-value: 6.06e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545491197   469 VGSLAEVKENPpFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCR 537
Cdd:smart01052   1 VGDRVEVGGGG-RRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 127-203 2.11e-17

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 77.24  E-value: 2.11e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545491197   127 VGCPVKVqlrsGEEKFPGVVRFRGPLLaerTVSGIFFGVELLEEGRGqgFTDGIYQGKQLFQCDEDCGVFVALDKLE 203
Cdd:smart01052   1 VGDRVEV----GGGGRRGTVRYVGPTP---FAPGVWVGVELDEPLRG--KNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 232-286 1.77e-09

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 54.51  E-value: 1.77e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 545491197   232 INSRVslKLGETIESGTVIFCDVLPGKEslGYFVGVDMDNP-IGNWDGRFDGVQLC 286
Cdd:smart01052   1 VGDRV--EVGGGGRRGTVRYVGPTPFAP--GVWVGVELDEPlRGKNDGSVKGVRYF 52
 
Name Accession Description Interval E-value
CYLD_phos_site pfam16607
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ...
 304-459 4.33e-112

Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region on a subset of tumour-suppressor and de-ubiquitinating enzyme CYLD proteins in eukaryotes. It lies between the second pair of CAP_GLY domains, pfam01302, on these proteins. This region of CYLD, being unstructured, carries a number of serine residues which, in response to cellular stimuli, become phosphorylated. This transient phosphorylation-state induces ubiquitination of TRAF2, a ubiquitin ligase that catalyzes both self-ubiquitination and the ubiquitination of specific target molecules involved in signal transduction.


Pssm-ID: 465194  Cd Length: 157  Bit Score: 341.55  E-value: 4.33e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197  304 PDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAK 383
Cdd:pfam16607   1 PESVSQERRPPKLAFASRGGGDKGSSSHNKPKATGSTSDPGNRNRSEFFYTLNGSSVDSQPQPKSKNTWYIDEVAEDPAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545491197  384 SLTEISPDFGHASPPLQPPSMNSLSTENRFHSLPFSLTKMPNTNGSIGHSPLSLSVQSVMGELNNAPVQESPPLAM 459
Cdd:pfam16607  81 SLTDTSPGFGHSSPPLQPPPTNSLSSENRFHSLPFSLTKMPSSNGSIGHSPLSLSVQSVMGELNTGPVQESPPSAA 156
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 590-945 7.06e-79

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 256.68  E-value: 7.06e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 590 GIQGHYN-SCYLDSTLFCLFAfssvldtvllrpkekndvgyysetqellrteivnplriygyvcatkimklrkilekvea 668
Cdd:cd02670    1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 669 asgftsEEKDPEEFLNILFHQILR--VEPLLKIRSAGQKVQD------CYFYQIFMEKNEKVGVPTIQQLLEWSFINSNl 740
Cdd:cd02670   22 ------EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQDddklvnERLLQIPVPDDDDGGGITLEQCLEQYFNNSV- 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 741 kFAEAPSCLIIQMPRFGK----DFKLFKKIFPSLELNITDLLEDTPRQCRICGglamYECRECYDDPDISAGNIKQFCKT 816
Cdd:cd02670   95 -FAKAPSCLIICLKRYGKtegkAQKMFKKILIPDEIDIPDFVADDPRACSKCQ----LECRVCYDDKDFSPTCGKFKLSL 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 817 CNTQVHLHPKRlnhkynpvslpkdlpdwdwrhgcipcqkmelfavlciETSHYVAFVKYGKD----------DSAWLFFD 886
Cdd:cd02670  170 CSAVCHRGTSL-------------------------------------ETGHYVAFVRYGSYsltetdneayNAQWVFFD 212

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545491197 887 SMADRDGGQNGFNIPqvtpcpevgeylkmspedlhsldsrriqgcARRLLCDAYMCMYQ 945
Cdd:cd02670  213 DMADRDGVSNGFNIP------------------------------AARLLEDPYMLFYQ 241
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 469-537 6.06e-21

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 87.26  E-value: 6.06e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545491197   469 VGSLAEVKENPpFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCR 537
Cdd:smart01052   1 VGDRVEVGGGG-RRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 127-203 2.11e-17

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 77.24  E-value: 2.11e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545491197   127 VGCPVKVqlrsGEEKFPGVVRFRGPLLaerTVSGIFFGVELLEEGRGqgFTDGIYQGKQLFQCDEDCGVFVALDKLE 203
Cdd:smart01052   1 VGDRVEV----GGGGRRGTVRYVGPTP---FAPGVWVGVELDEPLRG--KNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 475-536 7.02e-16

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 72.82  E-value: 7.02e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545491197  475 VKENPPFYGVIRWIGQPPGLNEVLAGLELeDECAGCTDGTFRGTRYFTCALKKALFVKLKSC 536
Cdd:pfam01302   5 VEVPGGRRGTVRYVGPVPFAPGVWVGVEL-DEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 127-202 3.07e-12

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 62.42  E-value: 3.07e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545491197  127 VGCPVKVqlrsgEEKFPGVVRFRGPLlaeRTVSGIFFGVELlEEGRGQgfTDGIYQGKQLFQCDEDCGVFVALDKL 202
Cdd:pfam01302   1 VGDRVEV-----PGGRRGTVRYVGPV---PFAPGVWVGVEL-DEPVGK--NDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 232-286 1.77e-09

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 54.51  E-value: 1.77e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 545491197   232 INSRVslKLGETIESGTVIFCDVLPGKEslGYFVGVDMDNP-IGNWDGRFDGVQLC 286
Cdd:smart01052   1 VGDRV--EVGGGGRRGTVRYVGPTPFAP--GVWVGVELDEPlRGKNDGSVKGVRYF 52
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 232-284 3.63e-06

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 45.09  E-value: 3.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 545491197  232 INSRVSLKLGETiesGTVIFCDVLPGKEslGYFVGVDMDNPIGNWDGRFDGVQ 284
Cdd:pfam01302   1 VGDRVEVPGGRR---GTVRYVGPVPFAP--GVWVGVELDEPVGKNDGSVKGVR 48
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
596-886 1.00e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 45.51  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197  596 NSCYLDSTLFCLFAFSSVLDtVLLRPKEKNDVGYYSETQELLR--TEIVNPLRIYGYVCATKIMKLRKILEKVEAA-SGF 672
Cdd:pfam00443   8 NTCYMNSVLQSLFSIPPFRD-YLLRISPLSEDSRYNKDINLLCalRDLFKALQKNSKSSSVSPKMFKKSLGKLNPDfSGY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197  673 TSEekDPEEFLNILFHQILRVEPLLKIRSagqkvQDCYFYQIF--MEKNekvgvpTIQQLlewsfINSNLKFAEAPSC-L 749
Cdd:pfam00443  87 KQQ--DAQEFLLFLLDGLHEDLNGNHSTE-----NESLITDLFrgQLKS------RLKCL-----SCGEVSETFEPFSdL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197  750 IIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPrqcricgglaMYECRECYDDpdisAGNIKQFC-KTCNTQVHLHPKR- 827
Cdd:pfam00443 149 SLPIPGDSAELKTASLQICFLQFSKLEELDDEE----------KYYCDKCGCK----QDAIKQLKiSRLPPVLIIHLKRf 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545491197  828 -----LNHKYN-PVSLPKDLP-DWDWRHGCIPC----QKMELFAVLC----IETSHYVAFVKYGKDDSaWLFFD 886
Cdd:pfam00443 215 synrsTWEKLNtEVEFPLELDlSRYLAEELKPKtnnlQDYRLVAVVVhsgsLSSGHYIAYIKAYENNR-WYKFD 287
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 482-583 5.60e-04

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 43.91  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 482 YGVIRWIGQPPGLNEVLAGLELeDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFG 561
Cdd:COG5244   16 FGTVRFIGKTKFKDGIWIGLEL-DDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGNAAYEKIKGGLVCESKGMDK 94

                         90       100
                 ....*....|....*....|..
gi 545491197 562 gyLSEVVEENTPPKMEKEGLEI 583
Cdd:COG5244   95 --DGEIKQENHEDRIHFEESKI 114
 
Name Accession Description Interval E-value
CYLD_phos_site pfam16607
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ...
 304-459 4.33e-112

Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region on a subset of tumour-suppressor and de-ubiquitinating enzyme CYLD proteins in eukaryotes. It lies between the second pair of CAP_GLY domains, pfam01302, on these proteins. This region of CYLD, being unstructured, carries a number of serine residues which, in response to cellular stimuli, become phosphorylated. This transient phosphorylation-state induces ubiquitination of TRAF2, a ubiquitin ligase that catalyzes both self-ubiquitination and the ubiquitination of specific target molecules involved in signal transduction.


Pssm-ID: 465194  Cd Length: 157  Bit Score: 341.55  E-value: 4.33e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197  304 PDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAK 383
Cdd:pfam16607   1 PESVSQERRPPKLAFASRGGGDKGSSSHNKPKATGSTSDPGNRNRSEFFYTLNGSSVDSQPQPKSKNTWYIDEVAEDPAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545491197  384 SLTEISPDFGHASPPLQPPSMNSLSTENRFHSLPFSLTKMPNTNGSIGHSPLSLSVQSVMGELNNAPVQESPPLAM 459
Cdd:pfam16607  81 SLTDTSPGFGHSSPPLQPPPTNSLSSENRFHSLPFSLTKMPSSNGSIGHSPLSLSVQSVMGELNTGPVQESPPSAA 156
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 590-945 7.06e-79

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 256.68  E-value: 7.06e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 590 GIQGHYN-SCYLDSTLFCLFAfssvldtvllrpkekndvgyysetqellrteivnplriygyvcatkimklrkilekvea 668
Cdd:cd02670    1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 669 asgftsEEKDPEEFLNILFHQILR--VEPLLKIRSAGQKVQD------CYFYQIFMEKNEKVGVPTIQQLLEWSFINSNl 740
Cdd:cd02670   22 ------EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQDddklvnERLLQIPVPDDDDGGGITLEQCLEQYFNNSV- 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 741 kFAEAPSCLIIQMPRFGK----DFKLFKKIFPSLELNITDLLEDTPRQCRICGglamYECRECYDDPDISAGNIKQFCKT 816
Cdd:cd02670   95 -FAKAPSCLIICLKRYGKtegkAQKMFKKILIPDEIDIPDFVADDPRACSKCQ----LECRVCYDDKDFSPTCGKFKLSL 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 817 CNTQVHLHPKRlnhkynpvslpkdlpdwdwrhgcipcqkmelfavlciETSHYVAFVKYGKD----------DSAWLFFD 886
Cdd:cd02670  170 CSAVCHRGTSL-------------------------------------ETGHYVAFVRYGSYsltetdneayNAQWVFFD 212

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545491197 887 SMADRDGGQNGFNIPqvtpcpevgeylkmspedlhsldsrriqgcARRLLCDAYMCMYQ 945
Cdd:cd02670  213 DMADRDGVSNGFNIP------------------------------AARLLEDPYMLFYQ 241
Bbox1_CYLD cd19816
B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins; ...
 782-838 4.48e-25

B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins; CYLD, also termed ubiquitin carboxyl-terminal hydrolase CYLD, or deubiquitinating enzyme CYLD, or ubiquitin thioesterase CYLD, or ubiquitin-specific-processing protease CYLD, is a microtubule-associated deubiquitinase that specifically cleaves Lys-63-linked polyubiquitin chains. It plays a pivotal role in a wide range of cellular activities, including innate immunity, cell division, and ciliogenesis. CYLD antagonizes NF-kappaB and JNK signaling by disassembly of Lys63-linked ubiquitin chains synthesized in response to cytokine stimulation. Structural characterization reveals a small zinc-binding B-box inserted within the ubiquitin specific protease (USP) domain of CYLD. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs) and is responsible for its intermolecular interaction and cytoplasmic localization. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380874  Cd Length: 56  Bit Score: 98.70  E-value: 4.48e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 545491197 782 PRQCRICGGLAMYECRECYDDPDISaGNIKQFCKTCNTQVHLHPKRLNHKYNPVSLP 838
Cdd:cd19816    1 PRECIICGGLAEYECRDCYLDPGIG-GKIKAFCKKCNKQTHLHPKRQNHKPRPLSVP 56
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 469-537 6.06e-21

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 87.26  E-value: 6.06e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545491197   469 VGSLAEVKENPpFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCR 537
Cdd:smart01052   1 VGDRVEVGGGG-RRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 127-203 2.11e-17

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 77.24  E-value: 2.11e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545491197   127 VGCPVKVqlrsGEEKFPGVVRFRGPLLaerTVSGIFFGVELLEEGRGqgFTDGIYQGKQLFQCDEDCGVFVALDKLE 203
Cdd:smart01052   1 VGDRVEV----GGGGRRGTVRYVGPTP---FAPGVWVGVELDEPLRG--KNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 475-536 7.02e-16

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 72.82  E-value: 7.02e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545491197  475 VKENPPFYGVIRWIGQPPGLNEVLAGLELeDECAGCTDGTFRGTRYFTCALKKALFVKLKSC 536
Cdd:pfam01302   5 VEVPGGRRGTVRYVGPVPFAPGVWVGVEL-DEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 127-202 3.07e-12

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 62.42  E-value: 3.07e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545491197  127 VGCPVKVqlrsgEEKFPGVVRFRGPLlaeRTVSGIFFGVELlEEGRGQgfTDGIYQGKQLFQCDEDCGVFVALDKL 202
Cdd:pfam01302   1 VGDRVEV-----PGGRRGTVRYVGPV---PFAPGVWVGVEL-DEPVGK--NDGSVKGVRYFECPPKHGVFVRPSKV 65
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 590-945 3.89e-11

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 64.43  E-value: 3.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 590 GIQGHYNSCYLDSTLFCLFAfssvldtvllrpkEKNDVgyysetQELLRTEivnplriygyvcatkimkLRKILEKVEAA 669
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS-------------EQQDA------HEFLLFL------------------LDKLHEELKKS 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 670 SGFTSEEKDPEEFLNILFHQILRVEplLKIRSAGQ---KVQDCYFYQIFMEKNEKvGVPTIQQLLEWSFINSNL------ 740
Cdd:cd02257   44 SKRTSDSSSLKSLIHDLFGGKLEST--IVCLECGHesvSTEPELFLSLPLPVKGL-PQVSLEDCLEKFFKEEILegdncy 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 741 --------------KFAEAPSCLIIQMPRFGKDF-----KLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYecrecyd 801
Cdd:cd02257  121 kcekkkkqeatkrlKIKKLPPVLIIHLKRFSFNEdgtkeKLNTKVSFPLELDLSPYLSEGEKDSDSDNGSYKY------- 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 802 dpdisagnikqfcktcntqvhlhpkrlnhkynpvslpkdlpdwdwrhgcipcqkmELFAVLC-----IETSHYVAFVKYG 876
Cdd:cd02257  194 -------------------------------------------------------ELVAVVVhsgtsADSGHYVAYVKDP 218

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545491197 877 KDDSaWLFFDSMadrdggqngfnipQVTPCPEvgeylkmspEDLHSLdsrriqgcaRRLLCDAYMCMYQ 945
Cdd:cd02257  219 SDGK-WYKFNDD-------------KVTEVSE---------EEVLEF---------GSLSSSAYILFYE 255
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 232-286 1.77e-09

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 54.51  E-value: 1.77e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 545491197   232 INSRVslKLGETIESGTVIFCDVLPGKEslGYFVGVDMDNP-IGNWDGRFDGVQLC 286
Cdd:smart01052   1 VGDRV--EVGGGGRRGTVRYVGPTPFAP--GVWVGVELDEPlRGKNDGSVKGVRYF 52
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 232-284 3.63e-06

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 45.09  E-value: 3.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 545491197  232 INSRVSLKLGETiesGTVIFCDVLPGKEslGYFVGVDMDNPIGNWDGRFDGVQ 284
Cdd:pfam01302   1 VGDRVEVPGGRR---GTVRYVGPVPFAP--GVWVGVELDEPVGKNDGSVKGVR 48
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
596-886 1.00e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 45.51  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197  596 NSCYLDSTLFCLFAFSSVLDtVLLRPKEKNDVGYYSETQELLR--TEIVNPLRIYGYVCATKIMKLRKILEKVEAA-SGF 672
Cdd:pfam00443   8 NTCYMNSVLQSLFSIPPFRD-YLLRISPLSEDSRYNKDINLLCalRDLFKALQKNSKSSSVSPKMFKKSLGKLNPDfSGY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197  673 TSEekDPEEFLNILFHQILRVEPLLKIRSagqkvQDCYFYQIF--MEKNekvgvpTIQQLlewsfINSNLKFAEAPSC-L 749
Cdd:pfam00443  87 KQQ--DAQEFLLFLLDGLHEDLNGNHSTE-----NESLITDLFrgQLKS------RLKCL-----SCGEVSETFEPFSdL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197  750 IIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPrqcricgglaMYECRECYDDpdisAGNIKQFC-KTCNTQVHLHPKR- 827
Cdd:pfam00443 149 SLPIPGDSAELKTASLQICFLQFSKLEELDDEE----------KYYCDKCGCK----QDAIKQLKiSRLPPVLIIHLKRf 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545491197  828 -----LNHKYN-PVSLPKDLP-DWDWRHGCIPC----QKMELFAVLC----IETSHYVAFVKYGKDDSaWLFFD 886
Cdd:pfam00443 215 synrsTWEKLNtEVEFPLELDlSRYLAEELKPKtnnlQDYRLVAVVVhsgsLSSGHYIAYIKAYENNR-WYKFD 287
Bbox1_HOIP cd19815
B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, ...
 784-835 2.61e-04

B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, also termed RING finger protein 31 (RNF31), or zinc in-between-RING-finger ubiquitin-associated domain protein, together with HOIL-1 and SHARPIN, forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis. It also interacts with the atypical mammalian orphan receptor DAX-1, trigger DAX-1 ubiquitination and stabilization, and participate in repressing steroidogenic gene expression. HOIP contains a B-box motif that shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380873  Cd Length: 43  Bit Score: 39.24  E-value: 2.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 545491197 784 QCRICGGL-AMYECRECYDdpdisagnikQFCKTCNTQVHLHPKRLNHKYNPV 835
Cdd:cd19815    1 LCDLCGEAaASVFCASCED----------KLCLSCDDLYHKHPARRSHHRQPI 43
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 482-583 5.60e-04

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 43.91  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545491197 482 YGVIRWIGQPPGLNEVLAGLELeDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFG 561
Cdd:COG5244   16 FGTVRFIGKTKFKDGIWIGLEL-DDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGNAAYEKIKGGLVCESKGMDK 94

                         90       100
                 ....*....|....*....|..
gi 545491197 562 gyLSEVVEENTPPKMEKEGLEI 583
Cdd:COG5244   95 --DGEIKQENHEDRIHFEESKI 114
Bbox1_DUF2009 cd20208
B-box-type 1 zinc finger found in DUF2009 domain-containing proteins and similar proteins; ...
 784-835 7.77e-03

B-box-type 1 zinc finger found in DUF2009 domain-containing proteins and similar proteins; This group is composed of uncharacterized proteins containing a zinc finger B-box domain and a DUF2009 domain, and similar zinc finger B-box domain-containing proteins. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380909 [Multi-domain]  Cd Length: 43  Bit Score: 35.04  E-value: 7.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 545491197 784 QCRICG-GLAMYECRECYDDpdisagnikqFCKTCNTQVHLHPKRLNHKYNPV 835
Cdd:cd20208    1 MCIECEdQPAEVRCEECGDE----------FCEVCFQSQHRKGKRRLHSFRPV 43
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH