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Conserved domains on  [gi|594150400|ref|NP_001277342|]
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TNF receptor-associated factor 2 isoform a [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MATH_TRAF2 cd03778
Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF2 subfamily, TRAF ...
341-504 4.23e-119

Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF2 subfamily, TRAF domain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF2 associates with the receptors TNFR-1, TNFR-2, RANK (which mediates differentiation and maturation of osteoclasts) and CD40 (which is important for the proliferation and activation of B cells), among others. It regulates distinct pathways that lead to the activation of nuclear factor-kappaB and Jun NH2-terminal kinases. TRAF2 also indirectly associates with death receptors through its interaction with TRADD (TNFR-associated death domain protein). It is involved in regulating oxidative stress or ROS-induced cell death and in the preconditioning of cells by sublethal stress for protection from subsequent injury. TRAF2 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


:

Pssm-ID: 239747  Cd Length: 164  Bit Score: 346.60  E-value: 4.23e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 341 AMADLEQKVSELEVSTYDGVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVV 420
Cdd:cd03778    1 A*ADLEQKVLE*EASTYDGVFIWKISDFARKRQEAVAGRIPAIFSPAFYTSRYGYKMCLRIYLNGDGTGRGTHLSLFFVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 421 MKGPNDALLQWPFNQKVTLMLLDHNNREHVIDAFRPDVTSSSFQRPVSDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIK 500
Cdd:cd03778   81 MKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTSSSFQRPVNDMNIASGCPLFCPVSK*EAKNSYVRDDAIFIK 160

                 ....
gi 594150400 501 AIVD 504
Cdd:cd03778  161 AIVD 164
TRAF_BIRC3_bd pfam16673
TNF receptor-associated factor BIRC3 binding domain; This domain is found in TNF ...
274-337 1.95e-32

TNF receptor-associated factor BIRC3 binding domain; This domain is found in TNF receptor-associated factor 1 and 2 (TRAF1 and TRAF2), where it binds to Baculoviral IAP repeat-containing protein 3 (BIRC3) (cIAP2).


:

Pssm-ID: 465226  Cd Length: 64  Bit Score: 118.28  E-value: 1.95e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594150400  274 ELLQRCQILEQKIATFENIVCVLNREVERVAVTAEACSRQHRLDQDKIEALSNKVQQLERSIGL 337
Cdd:pfam16673   1 ELEQKCQALENKVATFENIVAVLNREVERCSTTIEAYERQRRLDQDKIESLENKIRQLERSIAL 64
zf-TRAF pfam02176
TRAF-type zinc finger;
185-242 1.44e-19

TRAF-type zinc finger;


:

Pssm-ID: 280357 [Multi-domain]  Cd Length: 60  Bit Score: 82.12  E-value: 1.44e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400  185 HYEVCPKFPLTC-DGCGKKKIPRETFQDHVR-ACSKCRVLCRFHTVGCSEMVETENLQDH 242
Cdd:pfam02176   1 HLETCPFFPIPCpNGCCKKKILREDLPDHLElDCPKAEVPCPFKVFGCKEDVKREALQRH 60
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
31-80 5.67e-18

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are 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 enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16639:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 43  Bit Score: 77.11  E-value: 5.67e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150400  31 KYLCSACKNILRRPFQAQCGHRYCSFCLTSILrcasilsSSGPQNCAACV 80
Cdd:cd16639    1 KYLCSDCRNILRRPFQAQCGHRYCSYCLKKIL-------SSGPQKCAACI 43
 
Name Accession Description Interval E-value
MATH_TRAF2 cd03778
Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF2 subfamily, TRAF ...
341-504 4.23e-119

Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF2 subfamily, TRAF domain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF2 associates with the receptors TNFR-1, TNFR-2, RANK (which mediates differentiation and maturation of osteoclasts) and CD40 (which is important for the proliferation and activation of B cells), among others. It regulates distinct pathways that lead to the activation of nuclear factor-kappaB and Jun NH2-terminal kinases. TRAF2 also indirectly associates with death receptors through its interaction with TRADD (TNFR-associated death domain protein). It is involved in regulating oxidative stress or ROS-induced cell death and in the preconditioning of cells by sublethal stress for protection from subsequent injury. TRAF2 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239747  Cd Length: 164  Bit Score: 346.60  E-value: 4.23e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 341 AMADLEQKVSELEVSTYDGVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVV 420
Cdd:cd03778    1 A*ADLEQKVLE*EASTYDGVFIWKISDFARKRQEAVAGRIPAIFSPAFYTSRYGYKMCLRIYLNGDGTGRGTHLSLFFVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 421 MKGPNDALLQWPFNQKVTLMLLDHNNREHVIDAFRPDVTSSSFQRPVSDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIK 500
Cdd:cd03778   81 MKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTSSSFQRPVNDMNIASGCPLFCPVSK*EAKNSYVRDDAIFIK 160

                 ....
gi 594150400 501 AIVD 504
Cdd:cd03778  161 AIVD 164
TRAF_BIRC3_bd pfam16673
TNF receptor-associated factor BIRC3 binding domain; This domain is found in TNF ...
274-337 1.95e-32

TNF receptor-associated factor BIRC3 binding domain; This domain is found in TNF receptor-associated factor 1 and 2 (TRAF1 and TRAF2), where it binds to Baculoviral IAP repeat-containing protein 3 (BIRC3) (cIAP2).


Pssm-ID: 465226  Cd Length: 64  Bit Score: 118.28  E-value: 1.95e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594150400  274 ELLQRCQILEQKIATFENIVCVLNREVERVAVTAEACSRQHRLDQDKIEALSNKVQQLERSIGL 337
Cdd:pfam16673   1 ELEQKCQALENKVATFENIVAVLNREVERCSTTIEAYERQRRLDQDKIESLENKIRQLERSIAL 64
zf-TRAF pfam02176
TRAF-type zinc finger;
185-242 1.44e-19

TRAF-type zinc finger;


Pssm-ID: 280357 [Multi-domain]  Cd Length: 60  Bit Score: 82.12  E-value: 1.44e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400  185 HYEVCPKFPLTC-DGCGKKKIPRETFQDHVR-ACSKCRVLCRFHTVGCSEMVETENLQDH 242
Cdd:pfam02176   1 HLETCPFFPIPCpNGCCKKKILREDLPDHLElDCPKAEVPCPFKVFGCKEDVKREALQRH 60
RING-HC_TRAF2 cd16639
RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 2 ...
31-80 5.67e-18

RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 2 (TRAF2) and similar proteins; TRAF2, also known as tumor necrosis factor type 2 receptor-associated protein 3, is an E3 ubiquitin-protein ligase that was identified as a 75 kDa tumor necrosis factor receptor (TNF-R2)-associated signaling protein. It interacts with members of the TNF receptor superfamily and connects the receptors to downstream signaling proteins. It also mediates K63-linked polyubiquitination of RIP1, a kinase pivotal in TNFalpha-induced NF-kappaB activation. Moreover, TRAF2 regulates peripheral CD8(+) T-cell and NKT-cell homeostasis by modulating sensitivity to IL-15. It also acts as an important biological suppressor of necroptosis. It inhibits TNF-related apoptosis inducing ligand (TRAIL)- and CD95L-induced apoptosis and necroptosis. TRAF2 contains an N-terminal domain with a typical C3HC4-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438301 [Multi-domain]  Cd Length: 43  Bit Score: 77.11  E-value: 5.67e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150400  31 KYLCSACKNILRRPFQAQCGHRYCSFCLTSILrcasilsSSGPQNCAACV 80
Cdd:cd16639    1 KYLCSDCRNILRRPFQAQCGHRYCSYCLKKIL-------SSGPQKCAACI 43
MATH smart00061
meprin and TRAF homology;
360-480 1.34e-14

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 69.25  E-value: 1.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400   360 VFIWKISDFTRkrqeavAGRTPAIFSPAFYtsRYGYKMCLRVYLNGDgtgrgtHLSLFFVVMKGPNDALlQWPFNQKVTL 439
Cdd:smart00061   1 VLSHTFKNVSR------LEEGESYFSPSEE--HFNIPWRLKIYRKNG------FLSLYLHCEKEECDSR-KWSIEAEFTL 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 594150400   440 MLLDHNNREHvidafrPDVTSSSFQRPVSdmniaSGCPLFC 480
Cdd:smart00061  66 KLVSQNGKSL------SKKDKHVFEKPSG-----WGFSKFI 95
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
28-82 1.56e-03

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 40.76  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 594150400   28 LEAKYLCSACKNILRRPFQAQCGHRYCSFCltsILRCasiLSSSGpqNCAACVYE 82
Cdd:TIGR00599  23 LDTSLRCHICKDFFDVPVLTSCSHTFCSLC---IRRC---LSNQP--KCPLCRAE 69
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
247-353 2.54e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 247 LREHLALLLSSFLEAQASPGTLNQVGPELLQrcqiLEQKIATfenivcvLNREVERVAVTAEACSRQHRLDQDKIEALSN 326
Cdd:COG4942    1 MRKLLLLALLLALAAAAQADAAAEAEAELEQ----LQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALAR 69
                         90       100
                 ....*....|....*....|....*..
gi 594150400 327 KVQQLERSIGLKDLAMADLEQKVSELE 353
Cdd:COG4942   70 RIRALEQELAALEAELAELEKEIAELR 96
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
243-377 3.31e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400   243 ELQRLREHLALL---LSSFLEAQASpgtLNQVGPELLQRCQILEQKIATFENIVCVLNREVERVAVTAEACSRQHRLDQD 319
Cdd:TIGR02169  675 ELQRLRERLEGLkreLSSLQSELRR---IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 594150400   320 KIEALSNKVQQLERSIGLKDLAMADLEQKVSELEVStYDGVFIWKISDFTRKRQEAVA 377
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEAR-LSHSRIPEIQAELSKLEEEVS 808
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
34-79 4.19e-03

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 35.02  E-value: 4.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 594150400   34 CSACKNILRRPFQA-QCGHRYCSFCLTSILRcasilssSGPQNCAAC 79
Cdd:pfam00097   1 CPICLEEPKDPVTLlPCGHLFCSKCIRSWLE-------SGNVTCPLC 40
 
Name Accession Description Interval E-value
MATH_TRAF2 cd03778
Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF2 subfamily, TRAF ...
341-504 4.23e-119

Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF2 subfamily, TRAF domain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF2 associates with the receptors TNFR-1, TNFR-2, RANK (which mediates differentiation and maturation of osteoclasts) and CD40 (which is important for the proliferation and activation of B cells), among others. It regulates distinct pathways that lead to the activation of nuclear factor-kappaB and Jun NH2-terminal kinases. TRAF2 also indirectly associates with death receptors through its interaction with TRADD (TNFR-associated death domain protein). It is involved in regulating oxidative stress or ROS-induced cell death and in the preconditioning of cells by sublethal stress for protection from subsequent injury. TRAF2 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239747  Cd Length: 164  Bit Score: 346.60  E-value: 4.23e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 341 AMADLEQKVSELEVSTYDGVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVV 420
Cdd:cd03778    1 A*ADLEQKVLE*EASTYDGVFIWKISDFARKRQEAVAGRIPAIFSPAFYTSRYGYKMCLRIYLNGDGTGRGTHLSLFFVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 421 MKGPNDALLQWPFNQKVTLMLLDHNNREHVIDAFRPDVTSSSFQRPVSDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIK 500
Cdd:cd03778   81 MKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTSSSFQRPVNDMNIASGCPLFCPVSK*EAKNSYVRDDAIFIK 160

                 ....
gi 594150400 501 AIVD 504
Cdd:cd03778  161 AIVD 164
MATH_TRAF1 cd03779
Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF1 subfamily, TRAF ...
359-504 1.03e-81

Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF1 subfamily, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF1 expression is the most restricted among the TRAFs. It is found exclusively in activated lymphocytes, dendritic cells and certain epithelia. TRAF1 associates, directly or indirectly through heterodimerization with TRAF2, with the TNFR family receptors TNFR-2, CD30, RANK, CD40 and LMP1, among others. It also binds the intracellular proteins TRADD, TANK, TRIP, RIP1, RIP2 and FLIP. TRAF1 is unique among the TRAFs in that it lacks a RING domain, which is critical for the activation of nuclear factor-kappaB and Jun NH2-terminal kinase. Studies on TRAF1-deficient mice suggest that TRAF1 has a negative regulatory role in TNFR-mediated signaling events. TRAF1 contains one zinc finger and one TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239748  Cd Length: 147  Bit Score: 250.58  E-value: 1.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 359 GVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVVMKGPNDALLQWPFNQKVT 438
Cdd:cd03779    1 GTFLWKITDVSQKQRESSHGRDVSLCSPAFYTAKYGYKVCLRLYLNGDGAGKGTHISLFFVIMKGEYDALLPWPFRHKVT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594150400 439 LMLLDHNNREHVIDAFRPDVTSSSFQRPVSDMNIASGCPLFCPVSKMEA-KNSYVRDDAIFIKAIVD 504
Cdd:cd03779   81 FMLLDQNNREHVIDAFRPDLSSASFQRPVSDMNVASGCPLFFPLKKLQSpKHAYCKDDTIYIKCVVD 147
MATH_TRAF3 cd03777
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF3 subfamily, TRAF ...
321-506 5.66e-81

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF3 subfamily, TRAF domain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF3 was first described as a molecule that binds the cytoplasmic tail of CD40. However, it is not required for CD40 signaling. More recently, TRAF3 has been identified as a key regulator of type I interferon (IFN) production and the mammalian innate antiviral immunity. It mediates IFN responses in Toll-like receptor (TLR)-dependent as well as TLR-independent viral recognition pathways. It is also a key element in immunological homeostasis through its regulation of the anti-inflammatory cytokine interleukin-10. TRAF3 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239746  Cd Length: 186  Bit Score: 249.86  E-value: 5.66e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 321 IEALSNKVQQLERSIGLKDLAMADLEQKVSELEVSTYDGVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLR 400
Cdd:cd03777    1 TGLLESQLSRHDQMLSVHDIRLADMDLRFQVLETASYNGVLIWKIRDYKRRKQEAVMGKTLSLYSQPFYTGYFGYKMCAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 401 VYLNGDGTGRGTHLSLFFVVMKGPNDALLQWPFNQKVTLMLLDHN-NREHVIDAFRPDVTSSSFQRPVSDMNIASGCPLF 479
Cdd:cd03777   81 VYLNGDGMGKGTHLSLFFVIMRGEYDALLPWPFKQKVTLMLMDQGsSRRHLGDAFKPDPNSSSFKKPTGEMNIASGCPVF 160
                        170       180
                 ....*....|....*....|....*..
gi 594150400 480 CPVSKMEaKNSYVRDDAIFIKAIVDLT 506
Cdd:cd03777  161 VAQTVLE-NGTYIKDDTIFIKVIVDTS 186
MATH_TRAF_C cd00270
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal ...
359-504 5.10e-80

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link cell surface TNFRs and receptors of the interleukin-1/Toll-like family to downstream kinase signaling cascades which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. There are at least six mammalian and three Drosophila proteins containing TRAF domains. The mammalian TRAFs display varying expression profiles, indicating independent and cell type-specific regulation. They display distinct, as well as overlapping functions and interactions with receptors. Most TRAFs, except TRAF1, share N-terminal homology and contain a RING domain, multiple zinc finger domains, and a TRAF domain. TRAFs form homo- and heterotrimers through its TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 238168  Cd Length: 149  Bit Score: 245.98  E-value: 5.10e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 359 GVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVVMKGPNDALLQWPFNQKVT 438
Cdd:cd00270    1 GVLIWKIKDYSRKLQEAVAGSNTVLYSPPFYTSRYGYKLCLRLYLNGDGTGKGTHLSLFVHVMKGEYDALLEWPFRGKIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 439 LMLLDHNN---REHVIDAFRPDVTSSSFQ-RPVSDMNIASGCPLFCPVSKMEAKNsYVRDDAIFIKAIVD 504
Cdd:cd00270   81 LTLLDQSDdskRKHITETFMPDPNSSAFQrPPTGENNIGFGYPEFVPLEKLESRG-YVKDDTLFIKVEVD 149
MATH_TRAF5 cd03780
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF5 subfamily, TRAF ...
359-504 4.46e-68

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF5 subfamily, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF5 was identified as an activator of nuclear factor-kappaB and a regulator of lymphotoxin-beta receptor and CD40 signaling. Its interaction with CD40 is indirect, involving hetero-oligomerization with TRAF3. In addition, TRAF5 has been shown to associate with other TNFRs including CD27, CD30, OX40 and GITR (glucocorticoid-induced TNFR). It plays a role in modulating Th2 immune responses (driven by OX40 costimulation) and T-cell activation (triggered by GITR). It is also involved in osteoclastogenesis. TRAF5 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239749 [Multi-domain]  Cd Length: 148  Bit Score: 215.27  E-value: 4.46e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 359 GVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVVMKGPNDALLQWPFNQKVT 438
Cdd:cd03780    1 GKLIWKVTDYKMKKKEAVDGHTVSIFSQPFYTSRCGYRLCARAYLNGDGSGKGTHLSLYFVVMRGEFDSLLQWPFRQRVT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150400 439 LMLLDHNN-REHVIDAFRPDVTSSSFQRPVSDMNIASGCPLFCPVSKME-AKNSYVRDDAIFIKAIVD 504
Cdd:cd03780   81 LMLLDQSGkKNHIMETFKADPNSSSFKRPDGEMNIASGCPRFVAHSVLEnAKNTYIKDDTLFLKVAVD 148
MATH_TRAF4 cd03781
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF4 subfamily, TRAF ...
359-504 1.14e-43

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF4 subfamily, TRAF domain, C-terminal MATH subdomain; composed of proteins with similarity to human TRAF4, including the Drosophila protein DTRAF1. TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF4 is highly expressed during embryogenesis, especially in the central and peripheral nervous system. Studies using TRAF4-deficient mice show that TRAF4 is required for neurogenesis, as well as the development of the trachea and the axial skeleton. In addition, TRAF4 augments nuclear factor-kappaB activation triggered by GITR (glucocorticoid-induced TNFR), a receptor expressed in T-cells, B-cells and macrophages. It also participates in counteracting the signaling mediated by Toll-like receptors through its association with TRAF6 and TRIF. DTRAF1 plays a pivotal role in the development of eye imaginal discs and photosensory neuron arrays in Drosophila. TRAF4 contains a RING finger domain, seven zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239750  Cd Length: 154  Bit Score: 151.50  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 359 GVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVVMKGPNDALLQWPFNQKVT 438
Cdd:cd03781    1 GTLLWKITDYSRKLQEAKGRDNLELFSPPFYTHRYGYKLQVSAFLNGNGSGEGSHLSVYIRVLPGEYDNLLEWPFSHRIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594150400 439 LMLLDHNN-----REHVIDAFRPDVTSSSFQRPVSDMNIAS----GCPLFcpVSKMEAK-NSYVRDDAIFIKAIVD 504
Cdd:cd03781   81 FTLLDQSDpslskPQHITETFTPDPTWKNFQKPSASRLDEStlgfGYPKF--ISHEDLKkRNYIKDDAIFLRASVE 154
MATH_TRAF6 cd03776
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF6 subfamily, TRAF ...
359-503 8.39e-35

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF6 subfamily, TRAF domain, C-terminal MATH subdomain; composed of proteins with similarity to human TRAF6, including the Drosophila protein DTRAF2. TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF6 is the most divergent in its TRAF domain among the mammalian TRAFs. In addition to mediating TNFR family signaling, it is also an essential signaling molecule of the interleukin-1/Toll-like receptor superfamily. Whereas other TRAF molecules display similar and overlapping TNFR-binding specificities, TRAF6 binds completely different sites on receptors such as CD40 and RANK. TRAF6 serves as a molecular bridge between innate and adaptive immunity and plays a central role in osteoimmunology. DTRAF2, as an activator of nuclear factor-kappaB, plays a pivotal role in Drosophila development and innate immunity. TRAF6 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239745  Cd Length: 147  Bit Score: 127.44  E-value: 8.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 359 GVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVVMKGPNDALLQWPFNQKVT 438
Cdd:cd03776    1 GIYVWKIKNFSNLRRSMEAGSPVVIHSPGFYTSPPGYKLCARLNLSLPEARCPNYISLFVHLMQGENDSHLDWPFQGTIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 439 LMLLDHNNREH----VIDAfRPDVtsSSFQRPVSDMNIAS-GCPLFCPVSKMEAKnSYVRDDAIFIKAIV 503
Cdd:cd03776   81 LTLLDQSEPRQniheTMMS-KPEL--LAFQRPTTDRNPKGfGYVEFAHIEDLLQR-GFVKNDTLLIKIEV 146
TRAF_BIRC3_bd pfam16673
TNF receptor-associated factor BIRC3 binding domain; This domain is found in TNF ...
274-337 1.95e-32

TNF receptor-associated factor BIRC3 binding domain; This domain is found in TNF receptor-associated factor 1 and 2 (TRAF1 and TRAF2), where it binds to Baculoviral IAP repeat-containing protein 3 (BIRC3) (cIAP2).


Pssm-ID: 465226  Cd Length: 64  Bit Score: 118.28  E-value: 1.95e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594150400  274 ELLQRCQILEQKIATFENIVCVLNREVERVAVTAEACSRQHRLDQDKIEALSNKVQQLERSIGL 337
Cdd:pfam16673   1 ELEQKCQALENKVATFENIVAVLNREVERCSTTIEAYERQRRLDQDKIESLENKIRQLERSIAL 64
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
359-504 9.93e-23

MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains.


Pssm-ID: 238068  Cd Length: 126  Bit Score: 93.60  E-value: 9.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 359 GVFIWKISDFTRKRQEAvagrtpaIFSPAFYtsRYGYKMCLRVYLNGDGTgRGTHLSLFFVVMKGPNDaLLQWPFNQKVT 438
Cdd:cd00121    1 GKHTWKIVNFSELEGES-------IYSPPFE--VGGYKWRIRIYPNGDGE-SGDYLSLYLELDKGESD-LEKWSVRAEFT 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594150400 439 LMLLDHNNREHVIDAFRPDVTSSSfqrpvsdmNIASGCPLFCPVSKMEaKNSYVRDDAIFIKAIVD 504
Cdd:cd00121   70 LKLVNQNGGKSLSKSFTHVFFSEK--------GSGWGFPKFISWDDLE-DSYYLVDDSLTIEVEVK 126
zf-TRAF pfam02176
TRAF-type zinc finger;
185-242 1.44e-19

TRAF-type zinc finger;


Pssm-ID: 280357 [Multi-domain]  Cd Length: 60  Bit Score: 82.12  E-value: 1.44e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400  185 HYEVCPKFPLTC-DGCGKKKIPRETFQDHVR-ACSKCRVLCRFHTVGCSEMVETENLQDH 242
Cdd:pfam02176   1 HLETCPFFPIPCpNGCCKKKILREDLPDHLElDCPKAEVPCPFKVFGCKEDVKREALQRH 60
RING-HC_TRAF2 cd16639
RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 2 ...
31-80 5.67e-18

RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 2 (TRAF2) and similar proteins; TRAF2, also known as tumor necrosis factor type 2 receptor-associated protein 3, is an E3 ubiquitin-protein ligase that was identified as a 75 kDa tumor necrosis factor receptor (TNF-R2)-associated signaling protein. It interacts with members of the TNF receptor superfamily and connects the receptors to downstream signaling proteins. It also mediates K63-linked polyubiquitination of RIP1, a kinase pivotal in TNFalpha-induced NF-kappaB activation. Moreover, TRAF2 regulates peripheral CD8(+) T-cell and NKT-cell homeostasis by modulating sensitivity to IL-15. It also acts as an important biological suppressor of necroptosis. It inhibits TNF-related apoptosis inducing ligand (TRAIL)- and CD95L-induced apoptosis and necroptosis. TRAF2 contains an N-terminal domain with a typical C3HC4-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438301 [Multi-domain]  Cd Length: 43  Bit Score: 77.11  E-value: 5.67e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150400  31 KYLCSACKNILRRPFQAQCGHRYCSFCLTSILrcasilsSSGPQNCAACV 80
Cdd:cd16639    1 KYLCSDCRNILRRPFQAQCGHRYCSYCLKKIL-------SSGPQKCAACI 43
MATH smart00061
meprin and TRAF homology;
360-480 1.34e-14

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 69.25  E-value: 1.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400   360 VFIWKISDFTRkrqeavAGRTPAIFSPAFYtsRYGYKMCLRVYLNGDgtgrgtHLSLFFVVMKGPNDALlQWPFNQKVTL 439
Cdd:smart00061   1 VLSHTFKNVSR------LEEGESYFSPSEE--HFNIPWRLKIYRKNG------FLSLYLHCEKEECDSR-KWSIEAEFTL 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 594150400   440 MLLDHNNREHvidafrPDVTSSSFQRPVSdmniaSGCPLFC 480
Cdd:smart00061  66 KLVSQNGKSL------SKKDKHVFEKPSG-----WGFSKFI 95
MATH_Meprin cd03771
Meprin family, MATH domain; Meprins are multidomain, highly glycosylated extracellular ...
361-445 3.60e-14

Meprin family, MATH domain; Meprins are multidomain, highly glycosylated extracellular metalloproteases, which are either anchored to the membrane or secreted into extracellular spaces. They are expressed in renal and intestinal brush border membranes, leukocytes, and cancer cells, and are capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. Meprin proteases are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. Despite their similarity, the two subunits differ in their ability to self-associate, in proteolytic processing during biosynthesis and in substrate specificity. Both subunits are synthesized as membrane spanning proteins, however, the alpha subunit is cleaved during biosynthesis and loses its transmembrane domain. Meprin beta forms homodimers or heterotetramers while meprin alpha oligomerizes into large complexes containing 10-100 subunits. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen.


Pssm-ID: 239740  Cd Length: 167  Bit Score: 70.51  E-value: 3.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 361 FIWKISDFTRKRQEAVAGRtpAIFSPAFYTSR-YGYKMclRVYLNGdGTGRGTHLSLFFVVMKGPNDALLQWP-FNQKVT 438
Cdd:cd03771    4 AVWRVRNFSQLLETTPKGT--KIYSPRFYSPEgYAFQV--GLYPNG-TESYPGYTGLYFHLCSGENDDVLEWPcPNRQAT 78

                 ....*..
gi 594150400 439 LMLLDHN 445
Cdd:cd03771   79 MTLLDQD 85
MATH_Meprin_Beta cd03782
Meprin family, Beta subunit, MATH domain; Meprins are multidomain extracellular ...
361-445 2.05e-12

Meprin family, Beta subunit, MATH domain; Meprins are multidomain extracellular metalloproteases capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. They are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. The beta subunit is a type I membrane protein, which forms homodimers or heterotetramers (alpha2beta2 or alpha3beta). Meprin beta shows preference for acidic residues at the P1 and P1' sites of its substrate. Among its best substrates are growth factors and chemokines such as gastrin and osteopontin. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen.


Pssm-ID: 239751  Cd Length: 167  Bit Score: 65.27  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 361 FIWKISDFTRKRQEAVAGRTpaIFSPAFYTSRyGYKMCLRVYLNGDgTGRGTHLSLFFVVMKGPNDALLQWPFN-QKVTL 439
Cdd:cd03782    4 HIWHIRNFTQLLATTPPNGK--IYSPPFLSST-GYSFQVGLYLNGT-DDYPGNLAIYLHLTSGPNDDQLQWPCPwQQATM 79

                 ....*.
gi 594150400 440 MLLDHN 445
Cdd:cd03782   80 MLLDQH 85
RING-HC_TRAF1-like cd23125
RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 1 ...
29-64 1.37e-08

RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 1 (TRAF1)-like and similar proteins; TRAF1, also known as Epstein-Barr virus-induced protein 6 (EBI6), is an adapter molecule that regulates the activation of NF-kappa-B and JNK. It plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of an E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This subfamily corresponds a group of TRAF1-like proteins that contains an N-terminal domain with a typical C3HC4-type RING-HC finger.


Pssm-ID: 438487 [Multi-domain]  Cd Length: 51  Bit Score: 50.98  E-value: 1.37e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 594150400  29 EAKYLCSACKNILRRPFQAQCGHRYCSFCLTSILRC 64
Cdd:cd23125    2 EEKYLCCNCKNVLKKAQQTLCGHRYCLACLSWIVRN 37
MATH_Meprin_Alpha cd03783
Meprin family, Alpha subunit, MATH domain; Meprins are multidomain extracellular ...
362-445 1.19e-07

Meprin family, Alpha subunit, MATH domain; Meprins are multidomain extracellular metalloproteases capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. They are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. The alpha subunit is synthesized as a membrane spanning protein, however, it is cleaved during biosynthesis and loses its transmembrane domain. It oligomerizes into large complexes, containing 10-100 subunits (dimers that associate noncovalently), which are secreted as latent proteases and can move through extracellular spaces in a nondestructive manner. This allows delivery of the concentrated protease to sites containing activating enzymes, such as sites of inflammation, infection or cancerous growth. Meprin alpha shows preference for small or hydrophobic residues at the P1 and P1' sites of its substrate. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen.


Pssm-ID: 239752  Cd Length: 167  Bit Score: 51.40  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 362 IWKISDFTRKRQEAVagRTPAIFSPAFYTSRyGYKMCLRVY-LNGDGTGRGTHLSLFFVVMKGPNDALLQWP-FNQKVTL 439
Cdd:cd03783    5 VWRVRNFSQILENTT--KGDVLQSPRFYSPE-GYGYGVSLYpLSNESDYSGNYTGLYFHLCSGENDAVLEWPaLNRQAII 81

                 ....*.
gi 594150400 440 MLLDHN 445
Cdd:cd03783   82 TVLDQD 87
mRING-HC-C3HC3D_TRAF4-like cd23126
Modified RING finger, HC subclass (C3HC3D-type), found in uncharacterized proteins similar to ...
28-63 7.16e-07

Modified RING finger, HC subclass (C3HC3D-type), found in uncharacterized proteins similar to tumor necrosis factor (TNF) receptor-associated factor 4 (TRAF4); This subfamily corresponds to a group of uncharacterized proteins that shows high sequence similarity with tumor necrosis factor (TNF) receptor-associated factor 4 (TRAF4). TRAF4, also known as cysteine-rich domain associated with RING and Traf domains protein 1, or metastatic lymph node gene 62 protein (MLN 62), or RING finger protein 83 (RNF83), is a member of TRAF protein family, which mainly function in the immune system, where they mediate signaling through tumor necrosis factor receptors (TNFRs) and interleukin-1/Toll-like receptors (IL-1/TLRs). It also plays a critical role in the nervous system, as well as in carcinogenesis. Like TRAF4, members of this subfamily contain a modified C3HC3D-type RING-HC finger.


Pssm-ID: 438488 [Multi-domain]  Cd Length: 52  Bit Score: 46.18  E-value: 7.16e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 594150400  28 LEAKYLCSACKNILRRPFQAQ-CGHRYCSFCLTSILR 63
Cdd:cd23126    1 LDKKYECPVCCQVLRYPVQFEeCGHRVCSSCLPELLR 37
mRING-HC-C3HC3D_TRAF5 cd16642
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
28-62 2.66e-06

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 5 (TRAF5) and similar proteins; TRAF5, also known as RING finger protein 84 (RNF84), is an important signal transducer for a wide range of TNF receptor superfamily members, including tumor necrosis factor receptor 1 (TNFR1), TNFR2, CD40, and other lymphocyte costimulatory receptors, RANK/TRANCE-R, ectodysplasin-A Receptor (EDAR), lymphotoxin-beta receptor (LT-betaR), latent membrane protein 1 (LMP1), and IRE1. It functions as an activator of NF-kappaB, MAPK, and JNK, and is involved in both RANKL- and TNFalpha-induced osteoclastogenesis. It mediates CD40 signaling by associating with the cytoplasmic tail of CD40. It also negatively regulates Toll-like receptor (TLR) signaling and functions as a negative regulator of the interleukin 6 (IL-6) receptor signaling pathway that limits the differentiation of inflammatory CD4(+) T cells. TRAF5 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438304 [Multi-domain]  Cd Length: 56  Bit Score: 44.74  E-value: 2.66e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 594150400  28 LEAKYLCSACKNILRRPFQAQCGHRYCSFCLTSIL 62
Cdd:cd16642    1 LEDRYKCATCHFVLHNPHQTGCGHRFCQHCILSLL 35
mRING-HC-C3HC3D_TRAF6 cd16643
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
31-104 1.55e-05

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) and similar proteins; TRAF6, also known as interleukin-1 signal transducer or RING finger protein 85 (RNF85), is a cytoplasmic adapter protein that mediates signals induced by the tumor necrosis factor receptor (TNFR) superfamily and Toll-like receptor (TLR)/interleukin-1 receptor (IL-1R) family. It functions as a mediator involved in the activation of mitogen-activated protein kinase (MAPK), phosphoinositide 3-kinase (PI3K), and interferon regulatory factor pathways, as well as in IL-1R-mediated activation of NF-kappaB. TRAF6 is also an oncogene that plays a vital role in K-RAS-mediated oncogenesis. TRAF6 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438305 [Multi-domain]  Cd Length: 58  Bit Score: 42.37  E-value: 1.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594150400  31 KYLCSACKNILRRPFQAQCGHRYCSFCltsILRCasiLSSSGPQncaaCVYEGlyeegiSILESSSAFPDNAAR 104
Cdd:cd16643    1 KYECPICLMALREPVQTPCGHRFCKAC---ILKS---IREAGHK----CPVDN------EPLLENQLFPDNFAK 58
RING-HC_TRAF3 cd16640
RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 3 ...
32-79 4.31e-04

RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 3 (TRAF3) and similar proteins; TRAF3, also known as CAP-1, CD40 receptor-associated factor 1 (CRAF1), CD40-binding protein (CD40BP), or LMP1-associated protein 1 (LAP1), is a member of the TRAF protein family, which mainly functions in the immune system, where it mediates signaling through tumor necrosis factor receptors (TNFRs) and interleukin-1/Toll-like receptors (IL-1/TLRs). It also plays a unique cell type-specific and critical role in the restraint of B-cell homeostatic survival, a role with important implications for both B-cell differentiation and the pathogenesis of B-cell malignancies. TRAF3 differentially regulates differentiation of specific T cell subsets. It is required for iNKT cell development, restrains Treg cell development in the thymus, and plays an essential role in the homeostasis of central memory CD8+ T cells. TRAF3 contains an N-terminal domain with a typical C3HC4-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain, and a conserved TRAF-C domain.


Pssm-ID: 438302 [Multi-domain]  Cd Length: 42  Bit Score: 37.95  E-value: 4.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 594150400  32 YLCSACKNILRRPFQAQCGHRYCSFCLtsilrcASILSSSGPQnCAAC 79
Cdd:cd16640    1 YKCEKCRLVLCNPKQTECGHRFCESCM------NALLSSSNPQ-CPAC 41
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
28-82 1.56e-03

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 40.76  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 594150400   28 LEAKYLCSACKNILRRPFQAQCGHRYCSFCltsILRCasiLSSSGpqNCAACVYE 82
Cdd:TIGR00599  23 LDTSLRCHICKDFFDVPVLTSCSHTFCSLC---IRRC---LSNQP--KCPLCRAE 69
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
247-353 2.54e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400 247 LREHLALLLSSFLEAQASPGTLNQVGPELLQrcqiLEQKIATfenivcvLNREVERVAVTAEACSRQHRLDQDKIEALSN 326
Cdd:COG4942    1 MRKLLLLALLLALAAAAQADAAAEAEAELEQ----LQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALAR 69
                         90       100
                 ....*....|....*....|....*..
gi 594150400 327 KVQQLERSIGLKDLAMADLEQKVSELE 353
Cdd:COG4942   70 RIRALEQELAALEAELAELEKEIAELR 96
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
243-377 3.31e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400   243 ELQRLREHLALL---LSSFLEAQASpgtLNQVGPELLQRCQILEQKIATFENIVCVLNREVERVAVTAEACSRQHRLDQD 319
Cdd:TIGR02169  675 ELQRLRERLEGLkreLSSLQSELRR---IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 594150400   320 KIEALSNKVQQLERSIGLKDLAMADLEQKVSELEVStYDGVFIWKISDFTRKRQEAVA 377
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEAR-LSHSRIPEIQAELSKLEEEVS 808
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
34-79 4.19e-03

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 35.02  E-value: 4.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 594150400   34 CSACKNILRRPFQA-QCGHRYCSFCLTSILRcasilssSGPQNCAAC 79
Cdd:pfam00097   1 CPICLEEPKDPVTLlPCGHLFCSKCIRSWLE-------SGNVTCPLC 40
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
34-63 4.25e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain.


Pssm-ID: 438230 [Multi-domain]  Cd Length: 54  Bit Score: 35.42  E-value: 4.25e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 594150400  34 CSACKNILRRPFQAQCGHRYCSFCLTSILR 63
Cdd:cd16568    7 CIICHEYLYEPMVTTCGHTYCYTCLNTWFK 36
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
34-79 4.40e-03

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 36.51  E-value: 4.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 594150400  34 CSACKNILRRPFQAQCGHRYCSFCLTSILRcasilSSSGPQNCAAC 79
Cdd:cd16498   19 CPICLELLKEPVSTKCDHQFCRFCILKLLQ-----KKKKPAPCPLC 59
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
243-332 5.06e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150400  243 ELQRLREHLALLLSSFLEAQASPGTLNQVGPELL-------QRCQILEQKIATFENIVCVLNREVERVAVTAEACSRQHR 315
Cdd:pfam07888  88 ELRQSREKHEELEEKYKELSASSEELSEEKDALLaqraaheARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRK 167
                          90
                  ....*....|....*..
gi 594150400  316 LDQDKIEALSNKVQQLE 332
Cdd:pfam07888 168 EEEAERKQLQAKLQQTE 184
RING-HC_ScRAD18-like cd23148
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ...
34-62 5.63e-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: 35.20  E-value: 5.63e-03
                         10        20
                 ....*....|....*....|....*....
gi 594150400  34 CSACKNILRRPFQAQCGHRYCSFCLTSIL 62
Cdd:cd23148    6 CHICKDLLKAPMRTPCNHTFCSFCIRTHL 34
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
33-59 5.75e-03

RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438263 [Multi-domain]  Cd Length: 44  Bit Score: 34.77  E-value: 5.75e-03
                         10        20
                 ....*....|....*....|....*..
gi 594150400  33 LCSACKNILRRPFQAQCGHRYCSFCLT 59
Cdd:cd16601    3 SCSLCKEYLKDPVIIECGHNFCRACIT 29
RING-HC_ORTHRUS_rpt2 cd23139
second RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
27-61 6.88e-03

second RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; This subfamily includes Arabidopsis thaliana ORTHRUS 1-5. They are E3 ubiquitin-protein ligases that may participate in CpG methylation-dependent transcriptional regulation and/or epigenetic transcriptional silencing. ORTHRUS 1 mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. ORTHRUS 2 and 5 mediate ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. ORTHRUS 1 and 2 promote methylation-mediated gene silencing leading, for example, to early flowering. They can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrates. Members of this subfamily contain two typical C3HC4-type RING-HC fingers. This model corresponds to the second one.


Pssm-ID: 438501 [Multi-domain]  Cd Length: 72  Bit Score: 35.51  E-value: 6.88e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 594150400  27 RLEAKYLCSACKNILRRPFQAQCGHRYCSFCLTSI 61
Cdd:cd23139    1 RLLKEFGCQICKKVLSLPVSTPCGHNFCKACLEAK 35
RING-HC_GEFO-like cd16507
RING finger, HC subclass, found in Dictyostelium discoideum Ras guanine nucleotide exchange ...
26-62 8.17e-03

RING finger, HC subclass, found in Dictyostelium discoideum Ras guanine nucleotide exchange factor O (RasGEFO) and similar proteins; RasGEFO, also known as RasGEF domain-containing protein O, functions as a Ras guanine-nucleotide exchange factor (RasGEFs), activating Ras by catalyzing the replacement of GDP with GTP. RasGEFs are particularly important for signaling in development and chemotaxis in many organisms, including Dictyostelium. RasGEFO contains a C3HC4-type RING-HC finger that may be responsible for E3 ubiquitin ligase activity.


Pssm-ID: 438170 [Multi-domain]  Cd Length: 58  Bit Score: 35.02  E-value: 8.17e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 594150400  26 TRLEAKYLCSACKNILRRP-FQAQCGHRYCSFCLTSIL 62
Cdd:cd16507    4 LNLLQSLTCGICQNLFKDPnTLIPCGHAFCLDCLTTNA 41
mRING-HC-C3HC3D_LNX1 cd16779
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 1 (LNX1); ...
33-62 9.92e-03

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 1 (LNX1); LNX1, also known as numb-binding protein 1 or PDZ domain-containing RING finger protein 2, is a PDZ domain-containing RING-type E3 ubiquitin ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX1 contains an N-terminal modified C3HC3D-type RING-HC finger, a NPAY motif for Numb-LNX interaction, and four PDZ domains necessary for the binding of substrates, including CAR, ErbB2, SKIP, JAM4, CAST, c-Src, Claudins, RhoC, KCNA4, PAK6, PLEKHG5, PKC-alpha1, TYK2, PDZ-binding kinase (PBK), LNX2, and itself.


Pssm-ID: 438435 [Multi-domain]  Cd Length: 42  Bit Score: 34.01  E-value: 9.92e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 594150400  33 LCSACKNILRRPFQAQCGHRYCSFCLTSIL 62
Cdd:cd16779    3 ICHICLQALIQPLDTPCGHTYCTLCLTNFL 32
 
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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