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Conserved domains on  [gi|30681590|ref|NP_850020|]
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uncharacterized protein AT2G22010 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 137-265 1.01e-81

SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1).


:

Pssm-ID: 293940  Cd Length: 128  Bit Score: 263.03  E-value: 1.01e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  137 SARANACIWKGKWMYEVALETSGIQQLGWATLACPFTDQKGVGDADDSYAFDGRRVSKWNKEAEPYGQSWVAGDVIGCCI 216
Cdd:cd12882    1 SIRANACVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 30681590  217 DLNCDEIYFYRNGVSLGAAFTGIRKlGPGFGYYPAISLSQGERCELNFG 265
Cdd:cd12882   81 DLDKGTISFYRNGRSLGVAFDNVRR-GPGLAYFPAVSLSFGERLELNFG 128
RKP_N pfam19322
E3 ubiquitin-protein ligase RKP N-terminus; This domain represents the N-terminal region of ...
 1-137 8.78e-78

E3 ubiquitin-protein ligase RKP N-terminus; This domain represents the N-terminal region of the E3 ubiquitin-protein ligase RKP from plants. It was demonstrated that RKP is a functional ubiquitin E3 ligase and is able to interact with cell-cycle inhibitor ICK/KRP proteins.


:

Pssm-ID: 466041  Cd Length: 137  Bit Score: 252.15  E-value: 8.78e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590      1 MAEDSLRVGMISSGLAVLLNGEDAKENSSKARIVPHFDYSGHRPLERTIEFIFGLAEKSVGPLDGQVDSSLIRAVIKNQF 80
Cdd:pfam19322    1 MAEDSLRIGGLSSGLAVILNGEDRKENSSKSRLVSYCDDFGHQSVERTLEYIFDLPNKSIGPLTGPVDSNFIRSIIKNEF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 30681590     81 SKLHGDLDVSVSQREGISVVHHGVGPPIVGLEEFSICGDIRIVKPPLVLESLALFSS 137
Cdd:pfam19322   81 SKFHVNSDSLVSNRDGVCIVDNGCGPNVVGLEESSICGDIRIVKPPLLVESLAMFSS 137
RING-HC_RNF123 cd16541
RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; ...
 1215-1258 2.28e-20

RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; RNF123, also known as Kip1 ubiquitination-promoting complex protein 1 (KPC1), is an E3 ubiquitin-protein ligase that mediates ubiquitination and proteasomal processing of the nuclear factor-kappaB 1 (NF-kappaB1) precursor p105 to the p50 active subunit that restricts tumor growth. It also regulates degradation of heterochromatin protein 1alpha (HP1alpha) and 1beta (HP1beta) in lamin A/C knock-down cells. Moreover, RNF123, together with Kip1 ubiquitylation-promoting complex 2 (KPC2), forms the Kip1 ubiquitination-promoting complex (KPC), acting as a cytoplasmic ubiquitin ligase that regulates degradation of the cyclin-dependent kinase inhibitor p27 (Kip1) at the G1 phase of the cell cycle. RNF123 may also function as a clinically relevant, peripheral state marker of depression. RNF123 contains a C3HC4-type RING-HC finger at the C-terminus.


:

Pssm-ID: 438203 [Multi-domain]  Cd Length: 44  Bit Score: 85.43  E-value: 2.28e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 30681590 1215 NTCCICYAGEANAMIAPCSHRSCYGCITRHLLNCQRCFFCNATV 1258
Cdd:cd16541    1 DLCPICYAHPIDAVFLPCGHKSCRSCINRHLMNNKECFFCKATI 44
Ufd2P_core super family cl37808
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ...
 852-949 3.33e-05

Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.


The actual alignment was detected with superfamily member pfam10408:

Pssm-ID: 463080  Cd Length: 594  Bit Score: 48.34  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590    852 VFVYIPEFYLESLVDCFHVLRKsdppFVPSTTFIKQGLSSFITFVVTHFNDS-RISNTDLKDLLLQSISVLVQYKEYL-- 928
Cdd:pfam10408  255 PFKYLPEYFIEDIVDFLLFVTR----FAPDILESLSQLDELITFCIVFLRSPeYIKNPHLKAKLVEVLFYGTPPRQNGrp 330

                           90       100
                   ....*....|....*....|....*
gi 30681590    929 ----EAFENNEAATRHMPAALLAAF 949
Cdd:pfam10408  331 gvlgDILESHPLALKHLLPALMKFY 355
 
Name Accession Description Interval E-value
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 137-265 1.01e-81

SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1).


Pssm-ID: 293940  Cd Length: 128  Bit Score: 263.03  E-value: 1.01e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  137 SARANACIWKGKWMYEVALETSGIQQLGWATLACPFTDQKGVGDADDSYAFDGRRVSKWNKEAEPYGQSWVAGDVIGCCI 216
Cdd:cd12882    1 SIRANACVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 30681590  217 DLNCDEIYFYRNGVSLGAAFTGIRKlGPGFGYYPAISLSQGERCELNFG 265
Cdd:cd12882   81 DLDKGTISFYRNGRSLGVAFDNVRR-GPGLAYFPAVSLSFGERLELNFG 128
RKP_N pfam19322
E3 ubiquitin-protein ligase RKP N-terminus; This domain represents the N-terminal region of ...
 1-137 8.78e-78

E3 ubiquitin-protein ligase RKP N-terminus; This domain represents the N-terminal region of the E3 ubiquitin-protein ligase RKP from plants. It was demonstrated that RKP is a functional ubiquitin E3 ligase and is able to interact with cell-cycle inhibitor ICK/KRP proteins.


Pssm-ID: 466041  Cd Length: 137  Bit Score: 252.15  E-value: 8.78e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590      1 MAEDSLRVGMISSGLAVLLNGEDAKENSSKARIVPHFDYSGHRPLERTIEFIFGLAEKSVGPLDGQVDSSLIRAVIKNQF 80
Cdd:pfam19322    1 MAEDSLRIGGLSSGLAVILNGEDRKENSSKSRLVSYCDDFGHQSVERTLEYIFDLPNKSIGPLTGPVDSNFIRSIIKNEF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 30681590     81 SKLHGDLDVSVSQREGISVVHHGVGPPIVGLEEFSICGDIRIVKPPLVLESLALFSS 137
Cdd:pfam19322   81 SKFHVNSDSLVSNRDGVCIVDNGCGPNVVGLEESSICGDIRIVKPPLLVESLAMFSS 137
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 148-265 6.55e-33

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 123.61  E-value: 6.55e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590    148 KWMYEVALE--TSGIQQLGWATLACPFTDQKGVGDADDSYAFDGRRVSK-WNKEAEPYGQ-SWVAGDVIGCCIDLNCDEI 223
Cdd:pfam00622    1 RHYFEVEIFgqDGGGWRVGWATKSVPRKGERFLGDESGSWGYDGWTGKKyWASTSPLTGLpLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 30681590    224 YFYRNGVSLGAAFTGIRKLGPgfgYYPAISLSQGERCELNFG 265
Cdd:pfam00622   81 SFTKNGKSLGYAFRDVPFAGP---LFPAVSLGAGEGLKFNFG 119
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 146-265 4.50e-32

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 121.25  E-value: 4.50e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590     146 KGKWMYEVALETSGIQQLGWATLACPFTDQKGVGDADDSYAFDGRRVSKW-NKEAEPYGQSW-VAGDVIGCCIDLNCDEI 223
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKGSWGYDGDGGKKYhNSTGPEYGLPLqEPGDVIGCFLDLEAGTI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 30681590     224 YFYRNGVSLGaaFTGIRKLGPGFGYYPAISLSQGERCELNFG 265
Cdd:smart00449   81 SFYKNGKYLH--GLAFFDVKFSGPLYPAFSLGSGNSVRLNFG 120
RING-HC_RNF123 cd16541
RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; ...
 1215-1258 2.28e-20

RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; RNF123, also known as Kip1 ubiquitination-promoting complex protein 1 (KPC1), is an E3 ubiquitin-protein ligase that mediates ubiquitination and proteasomal processing of the nuclear factor-kappaB 1 (NF-kappaB1) precursor p105 to the p50 active subunit that restricts tumor growth. It also regulates degradation of heterochromatin protein 1alpha (HP1alpha) and 1beta (HP1beta) in lamin A/C knock-down cells. Moreover, RNF123, together with Kip1 ubiquitylation-promoting complex 2 (KPC2), forms the Kip1 ubiquitination-promoting complex (KPC), acting as a cytoplasmic ubiquitin ligase that regulates degradation of the cyclin-dependent kinase inhibitor p27 (Kip1) at the G1 phase of the cell cycle. RNF123 may also function as a clinically relevant, peripheral state marker of depression. RNF123 contains a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 438203 [Multi-domain]  Cd Length: 44  Bit Score: 85.43  E-value: 2.28e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 30681590 1215 NTCCICYAGEANAMIAPCSHRSCYGCITRHLLNCQRCFFCNATV 1258
Cdd:cd16541    1 DLCPICYAHPIDAVFLPCGHKSCRSCINRHLMNNKECFFCKATI 44
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
1213-1261 1.15e-08

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 52.38  E-value: 1.15e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 30681590   1213 EDNTCCICYAGEANAMIAPCSHRS-CYGCITRHLLNCQRCFFCNATVIDV 1261
Cdd:pfam13920    1 EDLLCVICLDRPRNVVLLPCGHLClCEECAERLLRKKKKCPICRQPIESV 50
Ufd2P_core pfam10408
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ...
 852-949 3.33e-05

Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.


Pssm-ID: 463080  Cd Length: 594  Bit Score: 48.34  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590    852 VFVYIPEFYLESLVDCFHVLRKsdppFVPSTTFIKQGLSSFITFVVTHFNDS-RISNTDLKDLLLQSISVLVQYKEYL-- 928
Cdd:pfam10408  255 PFKYLPEYFIEDIVDFLLFVTR----FAPDILESLSQLDELITFCIVFLRSPeYIKNPHLKAKLVEVLFYGTPPRQNGrp 330

                           90       100
                   ....*....|....*....|....*
gi 30681590    929 ----EAFENNEAATRHMPAALLAAF 949
Cdd:pfam10408  331 gvlgDILESHPLALKHLLPALMKFY 355
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 1217-1254 3.24e-04

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 39.41  E-value: 3.24e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 30681590    1217 CCICY-AGEANAMIAPCSHRSCYGCITRHLLNC-QRCFFC 1254
Cdd:smart00184    1 CPICLeEYLKDPVILPCGHTFCRSCIRKWLESGnNTCPIC 40
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
1193-1257 6.17e-03

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


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 40.77  E-value: 6.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30681590 1193 ASSQEPERKEESfnKDTTDIEDNTCCICYAGEANAMIAPCSHRSCYGCITRH--LLNCQRCFFCNAT 1257
Cdd:COG5236   42 NLSAEPNLTTSS--ADDTDEENMNCQICAGSTTYSARYPCGHQICHACAVRLraLYMQKGCPLCRTE 106
 
Name Accession Description Interval E-value
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 137-265 1.01e-81

SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1).


Pssm-ID: 293940  Cd Length: 128  Bit Score: 263.03  E-value: 1.01e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  137 SARANACIWKGKWMYEVALETSGIQQLGWATLACPFTDQKGVGDADDSYAFDGRRVSKWNKEAEPYGQSWVAGDVIGCCI 216
Cdd:cd12882    1 SIRANACVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 30681590  217 DLNCDEIYFYRNGVSLGAAFTGIRKlGPGFGYYPAISLSQGERCELNFG 265
Cdd:cd12882   81 DLDKGTISFYRNGRSLGVAFDNVRR-GPGLAYFPAVSLSFGERLELNFG 128
RKP_N pfam19322
E3 ubiquitin-protein ligase RKP N-terminus; This domain represents the N-terminal region of ...
 1-137 8.78e-78

E3 ubiquitin-protein ligase RKP N-terminus; This domain represents the N-terminal region of the E3 ubiquitin-protein ligase RKP from plants. It was demonstrated that RKP is a functional ubiquitin E3 ligase and is able to interact with cell-cycle inhibitor ICK/KRP proteins.


Pssm-ID: 466041  Cd Length: 137  Bit Score: 252.15  E-value: 8.78e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590      1 MAEDSLRVGMISSGLAVLLNGEDAKENSSKARIVPHFDYSGHRPLERTIEFIFGLAEKSVGPLDGQVDSSLIRAVIKNQF 80
Cdd:pfam19322    1 MAEDSLRIGGLSSGLAVILNGEDRKENSSKSRLVSYCDDFGHQSVERTLEYIFDLPNKSIGPLTGPVDSNFIRSIIKNEF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 30681590     81 SKLHGDLDVSVSQREGISVVHHGVGPPIVGLEEFSICGDIRIVKPPLVLESLALFSS 137
Cdd:pfam19322   81 SKFHVNSDSLVSNRDGVCIVDNGCGPNVVGLEESSICGDIRIVKPPLLVESLAMFSS 137
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 148-265 6.55e-33

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 123.61  E-value: 6.55e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590    148 KWMYEVALE--TSGIQQLGWATLACPFTDQKGVGDADDSYAFDGRRVSK-WNKEAEPYGQ-SWVAGDVIGCCIDLNCDEI 223
Cdd:pfam00622    1 RHYFEVEIFgqDGGGWRVGWATKSVPRKGERFLGDESGSWGYDGWTGKKyWASTSPLTGLpLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 30681590    224 YFYRNGVSLGAAFTGIRKLGPgfgYYPAISLSQGERCELNFG 265
Cdd:pfam00622   81 SFTKNGKSLGYAFRDVPFAGP---LFPAVSLGAGEGLKFNFG 119
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 147-263 1.23e-32

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 122.92  E-value: 1.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  147 GKWMYEVALET--SGIQQLGWATLACPFTDQKGVGDADDSYAFDGRRVSKWNKEAEPYGQS-WVAGDVIGCCIDLNCDEI 223
Cdd:cd11709    1 GKWYWEVRVDSgnGGLIQVGWATKSFSLDGEGGVGDDEESWGYDGSRLRKGHGGSSGPGGRpWKSGDVVGCLLDLDEGTL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 30681590  224 YFYRNGVSLGAAFTGIrkLGPGFGYYPAISLSQGERCELN 263
Cdd:cd11709   81 SFSLNGKDLGVAFTNL--FLKGGGLYPAVSLGSGQGVTIN 118
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 146-265 4.50e-32

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 121.25  E-value: 4.50e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590     146 KGKWMYEVALETSGIQQLGWATLACPFTDQKGVGDADDSYAFDGRRVSKW-NKEAEPYGQSW-VAGDVIGCCIDLNCDEI 223
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKGSWGYDGDGGKKYhNSTGPEYGLPLqEPGDVIGCFLDLEAGTI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 30681590     224 YFYRNGVSLGaaFTGIRKLGPGFGYYPAISLSQGERCELNFG 265
Cdd:smart00449   81 SFYKNGKYLH--GLAFFDVKFSGPLYPAFSLGSGNSVRLNFG 120
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 146-265 1.47e-27

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1


Pssm-ID: 240458  Cd Length: 133  Bit Score: 108.93  E-value: 1.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  146 KGKWMYEVALETSGIQQLGWATLACPftDQKGVGDADDSYAFDGRRVSKWNKEAEPYGQSWVAGDVIGCCIDLNCDEIYF 225
Cdd:cd12878   13 SGKWYFEFEVLTSGYMRVGWARPGFR--PDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCMLDLVDRTISF 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 30681590  226 YRNGV----SLGA--AFTGIrklGPGFGYYPAISLSQGERCELNFG 265
Cdd:cd12878   91 TLNGEllidSSGSevAFKDI---EIGEGFVPACSLGVGQKGRLNLG 133
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 135-265 3.92e-26

SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis.


Pssm-ID: 293932  Cd Length: 150  Bit Score: 105.29  E-value: 3.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  135 FSSARANACIWKGKWMYEVALETSGIQQ-----LGWATLACPFtdQKGVGDADDSYAF---DGRRVSkwNKEAEPYGQSW 206
Cdd:cd12872   16 YRMARANHGVREGKWYFEVKILEGGGTEtghvrVGWSRREASL--QAPVGYDKYSYAIrdkDGSKFH--QSRGKPYGEPG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  207 V-AGDVIGCCIDLncDEIYFYRNGVSLGAAFTGIrkLGPGfGYYPAISLSQGERCELNFG 265
Cdd:cd12872   92 FkEGDVIGFLITL--PKIEFFKNGKSQGVAFEDI--YGTG-GYYPAVSLYKGATVTINFG 146
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 147-265 6.01e-25

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development.


Pssm-ID: 293941  Cd Length: 121  Bit Score: 100.89  E-value: 6.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  147 GKWMYEVALETSGIQQLGWATLACPFTDQKGVGDADDSY--AFDGRRVSKW-NKEAEPYG-QSWVAGDVIGCCIDLNCDE 222
Cdd:cd12883    1 GVWYYEVTVLTSGVMQIGWATKDSKFLNHEGYGIGDDEYscAYDGCRQLIWyNAKSKPHThPRWKPGDVLGCLLDLNKKQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 30681590  223 IYFYRNGVSLGAAFTGIRKLGPGFgyYPAISLSQGERCELNFG 265
Cdd:cd12883   81 MIFSLNGNRLPPERQVFTSAKSGF--FAAASFMSFQQCEFNFG 121
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 138-268 1.93e-22

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay.


Pssm-ID: 293933  Cd Length: 155  Bit Score: 94.95  E-value: 1.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  138 ARANACI-WKGKWMYEVALETSGIQQLGWATLACPF---TDQKGVGdaddsYAFDGRRVskWNKEAEPYGQSWVAGDVIG 213
Cdd:cd12873   30 CRATKGVkGKGKYYYEVTVTDEGLCRVGWSTEDASLdlgTDKFGFG-----YGGTGKKS--HGRQFDDYGEPFGLGDVIG 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30681590  214 CCIDLNCDEIYFYRNGVSLGAAFTgIRKLGPGFGYYPAISLsQGERCELNFGAYP 268
Cdd:cd12873  103 CYLDLDNGTISFSKNGKDLGKAFD-IPPHLRNSALFPAVCL-KNAEVEFNFGDKP 155
RING-HC_RNF123 cd16541
RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; ...
 1215-1258 2.28e-20

RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; RNF123, also known as Kip1 ubiquitination-promoting complex protein 1 (KPC1), is an E3 ubiquitin-protein ligase that mediates ubiquitination and proteasomal processing of the nuclear factor-kappaB 1 (NF-kappaB1) precursor p105 to the p50 active subunit that restricts tumor growth. It also regulates degradation of heterochromatin protein 1alpha (HP1alpha) and 1beta (HP1beta) in lamin A/C knock-down cells. Moreover, RNF123, together with Kip1 ubiquitylation-promoting complex 2 (KPC2), forms the Kip1 ubiquitination-promoting complex (KPC), acting as a cytoplasmic ubiquitin ligase that regulates degradation of the cyclin-dependent kinase inhibitor p27 (Kip1) at the G1 phase of the cell cycle. RNF123 may also function as a clinically relevant, peripheral state marker of depression. RNF123 contains a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 438203 [Multi-domain]  Cd Length: 44  Bit Score: 85.43  E-value: 2.28e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 30681590 1215 NTCCICYAGEANAMIAPCSHRSCYGCITRHLLNCQRCFFCNATV 1258
Cdd:cd16541    1 DLCPICYAHPIDAVFLPCGHKSCRSCINRHLMNNKECFFCKATI 44
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 136-265 2.87e-16

SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate.


Pssm-ID: 293943  Cd Length: 132  Bit Score: 76.55  E-value: 2.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  136 SSARANACI--WKGKWMYEVALETSGIQQ---LGWATLACPftDQKGVGDADDSYAF---DGRrVSKWNKEAEPYGQSWV 207
Cdd:cd12885    1 GSVRADHPIppKVPVFYFEVTILDLGEKGivsIGFCTSGFP--LNRMPGWEDGSYGYhgdDGR-VYLGGGEGENYGPPFG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30681590  208 AGDVIGCCIDLNCDEIYFYRNGVSLGAAFTGIRKLgpgfGYYPAISL-SQGERCELNFG 265
Cdd:cd12885   78 TGDVVGCGINFKTGEVFFTKNGELLGTAFENVVKG----RLYPTVGLgSPGVKVRVNFG 132
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 126-265 7.56e-16

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation.


Pssm-ID: 293942  Cd Length: 177  Bit Score: 76.86  E-value: 7.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  126 PLVLESLA-LFSSARANACIWKGKWMYEV-ALETSGIQ------------QLGWATLACPFTdqkgVGDADDSYAFDGRR 191
Cdd:cd12884   23 PLTDEGFAyLWAGARATYGVTKGKVCFEVkVTENLPVKhlpteetdphvvRVGWSVDSSSLQ----LGEEEFSYGYGSTG 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30681590  192 VSKWNKEAEPYGQSWVAGDVIGCCIDLNCD--EIYFYRNGVSLGAAFTGIRKLGPGFGYYPAIsLSQGERCELNFG 265
Cdd:cd12884   99 KKSTNCKFEDYGEPFGENDVIGCYLDFESEpvEISFSKNGKDLGVAFKISKEELGGKALFPHV-LTKNCAVEVNFG 173
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 182-265 5.02e-14

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


Pssm-ID: 293966  Cd Length: 144  Bit Score: 70.63  E-value: 5.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  182 DDSYAFDGRRVSKwnkeaePYGQSWVAGDVIGCCIDLNCDEIYFYRNGVSLGAAFTGIrklgPGFGYYPAISL-SQGERC 260
Cdd:cd12909   69 DDGHSFCSSGTGK------PYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDI----KKGNLYPTVGLrTPGEHV 138


                 ....*
gi 30681590  261 ELNFG 265
Cdd:cd12909  139 EANFG 143
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 137-265 1.34e-12

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs.


Pssm-ID: 240457  Cd Length: 151  Bit Score: 66.57  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  137 SARANACIWKG-------KWMYEVA---LETSGIQ----QLGWATL----ACPFTDQK----GVGDADDSYAFDG----- 189
Cdd:cd12877    1 SIRPNIFVGVVegsaqykKWYFEVEvdhVEQFTHQpahlRVGWANTsgyvPYPGGGEGwggnGVGDDLYSYGFDGlhlwt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  190 ----RRVSKWNKEAepygqsWVAGDVIGCCIDLNCDEIYFYRNGVSLGAAFTGIRKLGpgfGYYPAISLSQGERCELNFG 265
Cdd:cd12877   81 ggrsRRVTSGTQHL------LKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDG---MFFPVMSFSAGVSCRFLLG 151
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 147-265 3.55e-10

SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in bacterial and are mostly uncharacterized. SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 eukaryotic protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L).


Pssm-ID: 293944  Cd Length: 129  Bit Score: 59.06  E-value: 3.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  147 GKWMYEVALETSG---IQQLGWAT-LACPFTDQKGVGDADDSYAFDGRRVSKWNKEAEP--YGQSWVAGDVIGCCIDLNC 220
Cdd:cd12886    1 GKWYWEVTVVSSAastYAGIGVANaAATGNNGLNGIELSSIGYSLGVYSGNKLSNGSSVatYGAGFTAGDVIGVALDLDA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 30681590  221 DEIYFYRNGVSLGA--AFTGIRKLGPGFGYYPAISL--SQGERCELNFG 265
Cdd:cd12886   81 GKIWFYKNGVWQGGgdPAPGTNPAFAGTAMYPAVTGgsSTGGSFTANFG 129
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
1213-1261 1.15e-08

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 52.38  E-value: 1.15e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 30681590   1213 EDNTCCICYAGEANAMIAPCSHRS-CYGCITRHLLNCQRCFFCNATVIDV 1261
Cdd:pfam13920    1 EDLLCVICLDRPRNVVLLPCGHLClCEECAERLLRKKKKCPICRQPIESV 50
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 196-253 1.79e-05

SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. All four SPSB proteins interact with c-Met, the hepatocyte growth factor receptor, but SOCS3 regulates cellular response to a variety of cytokines such as leukemia inhibitory factor (LIF) and interleukin 6. SOCS3, along with SOCS1, are expressed by immune cells and cells of the central nervous system (CNS) and have the potential to impact immune processes within the CNS. In non-small cell lung cancer (NSCLC), SOCS3 is silenced and proline-rich tyrosine kinase 2 (Pyk2) is over-expressed; it has been suggested that SOCS3 could be an effective way to prevent the progression of NSCLC due to its role in regulating Pyk2 expression.


Pssm-ID: 293936  Cd Length: 185  Bit Score: 46.77  E-value: 1.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30681590  196 NKEAEPYGQSW-VAGDVIGCCIDLNCDEIYFYRNGVSLGAAFTGIRKLGPgfgYYPAIS 253
Cdd:cd12876  101 DGQSRPYTSPFgNQGTIIGVHLDMWRGTLTFYKNGKPLGVAFTGLNGVKP---LYPMVS 156
Ufd2P_core pfam10408
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ...
 852-949 3.33e-05

Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.


Pssm-ID: 463080  Cd Length: 594  Bit Score: 48.34  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590    852 VFVYIPEFYLESLVDCFHVLRKsdppFVPSTTFIKQGLSSFITFVVTHFNDS-RISNTDLKDLLLQSISVLVQYKEYL-- 928
Cdd:pfam10408  255 PFKYLPEYFIEDIVDFLLFVTR----FAPDILESLSQLDELITFCIVFLRSPeYIKNPHLKAKLVEVLFYGTPPRQNGrp 330

                           90       100
                   ....*....|....*....|....*
gi 30681590    929 ----EAFENNEAATRHMPAALLAAF 949
Cdd:pfam10408  331 gvlgDILESHPLALKHLLPALMKFY 355
zf-RING_2 pfam13639
Ring finger domain;
1215-1255 3.36e-05

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 42.39  E-value: 3.36e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 30681590   1215 NTCCIC---YAGEANAMIAPCSHRSCYGCITRHLLNCQRCFFCN 1255
Cdd:pfam13639    1 DECPICleeFEEGDKVVVLPCGHHFHRECLDKWLRSSNTCPLCR 44
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 1216-1254 7.85e-05

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: 41.32  E-value: 7.85e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 30681590 1216 TCCICYAGEANAMIAPCSHRSCYGCITRHL-LNCQRCFFC 1254
Cdd:cd16449    2 ECPICLERLKDPVLLPCGHVFCRECIRRLLeSGSIKCPIC 41
mRING-HC-C3HC5_NEU1 cd16647
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, ...
 1214-1263 7.86e-05

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, NEURL1B, and similar proteins; This subfamily includes Drosophila neuralized (D-neu) protein, and its two mammalian homologs, NEURL1A and NEURL1B. D-neu is a regulator of the developmentally important Notch signaling pathway. NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of D-neu. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in medulloblastoma. NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is another mammalian homolog of D-neu protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling by working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. Members of this subfamily contain two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438309 [Multi-domain]  Cd Length: 53  Bit Score: 41.51  E-value: 7.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30681590 1214 DNTCCICYAGEANAMIAPCSHR-SCYGCITRHLLNCQRCFFCNATVIDVIR 1263
Cdd:cd16647    1 GSECVICYERPVDTVLYRCGHMcMCYDCALQLKRRGGSCPICRAPIKDVIK 51
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
 1214-1258 1.20e-04

RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), is a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3sigma ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger.


Pssm-ID: 438167 [Multi-domain]  Cd Length: 47  Bit Score: 40.69  E-value: 1.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 30681590 1214 DNTCCICYAGEANAMIAPCSHRSCYGCITRHLLNCQRCFFCNATV 1258
Cdd:cd16504    2 DFLCPICFDIIKEAFVTKCGHSFCYKCIVKHLEQKNRCPKCNFYL 46
SPRYD7 cd12880
SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also ...
 137-278 2.46e-04

SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also known as SPRY domain-containing protein 7 or CLL deletion region gene 6 protein homolog or CLLD6 or chronic lymphocytic leukemia deletion region gene 6 protein homolog). In humans, CLLD6 is highly expressed in heart, skeletal muscle, and testis as well as cancer cell lines. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes.


Pssm-ID: 293938  Cd Length: 160  Bit Score: 42.96  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  137 SARANACIWKGKWMYEVALETSGIQQLGWATLACPFTDQKGVGDA-------DDSYAFDGRRVSKWNKEAEpygqswvAG 209
Cdd:cd12880   19 AALANAPIVQDKAYFEVKIQSTGVWGVGLATRKTDLNRVPLGNDAeswvlrsDGTIWHNGEVIHKLKQLVE-------EG 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30681590  210 DVIGCC---IDLNcdeiyFYRNGVSLGAAFTGIRklGPgfgYYPAISLSQGERCELNFGAYpFKYPVDGFQP 278
Cdd:cd12880   92 DVIGVTydhVELN-----FYLNGKPLDCPITGIK--GT---VYPVVYVDDGAILDVQFSNF-YHPPPSGFEE 152
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 1217-1254 3.24e-04

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 39.41  E-value: 3.24e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 30681590    1217 CCICY-AGEANAMIAPCSHRSCYGCITRHLLNC-QRCFFC 1254
Cdd:smart00184    1 CPICLeEYLKDPVILPCGHTFCRSCIRKWLESGnNTCPIC 40
RING-HC_ScRAD18-like cd23148
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ...
 1216-1258 1.37e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 (RAD18) and similar proteins; RAD18, also called RING-type E3 ubiquitin transferase RAD18, acts as a postreplication repair E3 ubiquitin-protein ligase that associates with the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on 'Lys-164' of POL30, which is necessary for PRR. The UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. RAD18 is an E3 RING-finger protein belonging to the UBC2/RAD6 epistasis group. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438510 [Multi-domain]  Cd Length: 52  Bit Score: 37.90  E-value: 1.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 30681590 1216 TCCICYAGEANAMIAPCSHRSCYGCITRHLLNCQRCFFCNATV 1258
Cdd:cd23148    5 RCHICKDLLKAPMRTPCNHTFCSFCIRTHLNNDARCPLCKAEV 47
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
 1215-1263 1.45e-03

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438491 [Multi-domain]  Cd Length: 54  Bit Score: 38.01  E-value: 1.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 30681590 1215 NTCCICYAGEANAMIAPCSHRS-CYGCITRHLLNCQRCFFCNATVIDVIR 1263
Cdd:cd23129    3 DECVVCMDAPRDAVCVPCGHVAgCMSCLKALMQSSPLCPICRAPVRQVIK 52
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
 188-267 2.65e-03

SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor of SHR3 null mutation protein 4) and similar proteins. SSH4 is a component of the endosome-vacuole trafficking pathway that regulates nutrient transport and may be involved in processes determining whether plasma membrane proteins are degraded or routed to the plasma membrane. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. In yeast, SSH4 and the homologous protein EAR1 (endosomal adapter of RSP5) recruit Rsp5p, an essential ubiquitin ligase of the Nedd4 family, and assist it in its function at multivesicular bodies by directing the ubiquitylation of specific cargoes.


Pssm-ID: 293967  Cd Length: 192  Bit Score: 40.42  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  188 DGRRVSKWNKEAEPYGQSWVAGDVIGCCIDLNCDEIYFYRNGVSLGAAFTGI---RKLGPGFGY------YPAISLSQGE 258
Cdd:cd12910  102 DGHRYINDPFGGKDFTPPFREGDTIGIGYRFSSGTIFFTRNGKRLGGWDLGEeldAEDDGVTGLegfhdlYAAIGVFGGE 181

                         90
                 ....*....|.
gi 30681590  259 rCEL--NFGAY 267
Cdd:cd12910  182 -CEVhvNPGQW 191
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
 1214-1256 4.99e-03

RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).


Pssm-ID: 438236 [Multi-domain]  Cd Length: 47  Bit Score: 36.11  E-value: 4.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 30681590 1214 DNTCCICYA--GEANAMIAPCSHRSCYGCITRHLLNCQRCFFCNA 1256
Cdd:cd16574    1 DSSCPICLDrfENEKAFLDGCFHAFCFTCILEWSKVKNECPLCKQ 45
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
 1217-1258 5.42e-03

RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; RAD18, also known as HR18 or RING finger protein 73 (RNF73), is an E3 ubiquitin-protein ligase involved in post replication repair of UV-damaged DNA via its recruitment to stalled replication forks. It associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on K164. It also interacts with another E2 ubiquitin conjugating enzyme RAD6 to form a complex that monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Moreover, Rad18 is a key factor in double-strand break DNA damage response (DDR) pathways via its association with K63-linked polyubiquitylated chromatin proteins. It can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after ionizing radiation (IR) exposure. RAD18 contains a C3HC4-type RING-HC finger, a ubiquitin-binding zinc finger domain (UBZ), a SAP (SAF-A/B, Acinus and PIAS) domain, and a RAD6-binding domain (R6BD).


Pssm-ID: 438192 [Multi-domain]  Cd Length: 54  Bit Score: 36.13  E-value: 5.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 30681590 1217 CCICYAG-EANAMIAPCSHRSCYGCITRHLLNCQRCFFCNATV 1258
Cdd:cd16529    7 CPICFEYfNTAMMITQCSHNYCSLCIRRFLSYKTQCPTCRAAV 49
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
1193-1257 6.17e-03

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


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 40.77  E-value: 6.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30681590 1193 ASSQEPERKEESfnKDTTDIEDNTCCICYAGEANAMIAPCSHRSCYGCITRH--LLNCQRCFFCNAT 1257
Cdd:COG5236   42 NLSAEPNLTTSS--ADDTDEENMNCQICAGSTTYSARYPCGHQICHACAVRLraLYMQKGCPLCRTE 106
SPRYD3 cd12908
SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ...
 181-264 7.85e-03

SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 (SPRYD3). In humans, it is highly expressed in most tissues, including brain, kidney, heart, intestine, skeletal muscle, and testis. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes.


Pssm-ID: 293965  Cd Length: 171  Bit Score: 38.82  E-value: 7.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681590  181 ADDSYAFDGRRVskwnkeAEPYGQSWVAGDVIGCCIDLNCD-----------------EIYFYRNGVSLGAAftgiRKLG 243
Cdd:cd12908   79 ADDGKLFKGSGV------GDQFGPRCTKGDRMGCGIRFPRDydtdsedqgdeeegrtvQVFFTRNGKEVGRT----EVPL 148

                         90       100
                 ....*....|....*....|..
gi 30681590  244 PGFGYYPAIS-LSQGERCELNF 264
Cdd:cd12908  149 PPGGFYPAVGmHSEGEKVRVDL 170
 
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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