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Conserved domains on  [gi|767994850|ref|XP_011523136|]
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E3 ubiquitin-protein ligase TRIM37 isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MATH_TRIM37 cd03773
Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal ...
 239-372 1.13e-83

Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal protein and is a member of the tripartite motif (TRIM) protein subfamily, also known as the RING-B-box-coiled-coil (RBCC) subfamily of zinc-finger proteins. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction and hepatomegaly. TRIM37, similar to other TRIMs, contains a cysteine-rich, zinc-binding RING-finger domain followed by another cysteine-rich zinc-binding domain, the B-box, and a coiled-coil domain. TRIM37 is autoubiquitinated in a RING domain-dependent manner, indicating that it functions as an ubiquitin E3 ligase. In addition to the tripartite motif, TRIM37 also contains a MATH domain C-terminal to the coiled-coil domain. The MATH domain of TRIM37 has been shown to interact with the TRAF domain of six known TRAFs in vitro, however, it is unclear whether this is physiologically relevant. Eleven TRIM37 mutations have been associated with Mulibrey nanism so far. One mutation, Gly322Val, is located in the MATH domain and is the only mutation that does not affect the length of the protein. It results in the incorrect subcellular localization of TRIM37.


:

Pssm-ID: 239742  Cd Length: 132  Bit Score: 265.43  E-value: 1.13e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850 239 VPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSc 318
Cdd:cd03773    1 IPPYDSATFTLENFSTLRQSADPVYSDPLNVDGLCWRLKVYPDGNGEVRGNFLSVFLELCSGLGEASKYEYRVEMVHQA- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767994850 319 nDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILRFQVRSP 372
Cdd:cd03773   80 -NPTKNIKREFASDFEVGECWGYNRFFRLDLLINEGYLLPENDTLILRFSVRPP 132
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 98-220 1.28e-27

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


:

Pssm-ID: 128778  Cd Length: 127  Bit Score: 108.51  E-value: 1.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850    98 LAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVE----MMIARLDTQLKNKLITLMGQ 173
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNkrkkQLLEDLEEQKENKLKVLEQQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 767994850   174 KTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRK 220
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
Bbox2_TRIM37_C-VIII cd19779
B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar ...
 59-98 7.48e-26

B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as Mulibrey nanism protein, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of 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 RING finger, Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


:

Pssm-ID: 380837  Cd Length: 40  Bit Score: 100.48  E-value: 7.48e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767994850  59 DKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPL 98
Cdd:cd19779    1 DKCETHNEKLSVYCWTCKKCICHQCALWGGTHSGHTFKPL 40
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 6-21 4.85e-03

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 cd16619:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 43  Bit Score: 35.80  E-value: 4.85e-03
                         10
                 ....*....|....*.
gi 767994850   6 VERWLTEQRAQCPHCR 21
Cdd:cd16619   28 IRRWLSEQRSSCPHCR 43
 
Name Accession Description Interval E-value
MATH_TRIM37 cd03773
Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal ...
 239-372 1.13e-83

Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal protein and is a member of the tripartite motif (TRIM) protein subfamily, also known as the RING-B-box-coiled-coil (RBCC) subfamily of zinc-finger proteins. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction and hepatomegaly. TRIM37, similar to other TRIMs, contains a cysteine-rich, zinc-binding RING-finger domain followed by another cysteine-rich zinc-binding domain, the B-box, and a coiled-coil domain. TRIM37 is autoubiquitinated in a RING domain-dependent manner, indicating that it functions as an ubiquitin E3 ligase. In addition to the tripartite motif, TRIM37 also contains a MATH domain C-terminal to the coiled-coil domain. The MATH domain of TRIM37 has been shown to interact with the TRAF domain of six known TRAFs in vitro, however, it is unclear whether this is physiologically relevant. Eleven TRIM37 mutations have been associated with Mulibrey nanism so far. One mutation, Gly322Val, is located in the MATH domain and is the only mutation that does not affect the length of the protein. It results in the incorrect subcellular localization of TRIM37.


Pssm-ID: 239742  Cd Length: 132  Bit Score: 265.43  E-value: 1.13e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850 239 VPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSc 318
Cdd:cd03773    1 IPPYDSATFTLENFSTLRQSADPVYSDPLNVDGLCWRLKVYPDGNGEVRGNFLSVFLELCSGLGEASKYEYRVEMVHQA- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767994850 319 nDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILRFQVRSP 372
Cdd:cd03773   80 -NPTKNIKREFASDFEVGECWGYNRFFRLDLLINEGYLLPENDTLILRFSVRPP 132
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 98-220 1.28e-27

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 108.51  E-value: 1.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850    98 LAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVE----MMIARLDTQLKNKLITLMGQ 173
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNkrkkQLLEDLEEQKENKLKVLEQQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 767994850   174 KTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRK 220
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
Bbox2_TRIM37_C-VIII cd19779
B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar ...
 59-98 7.48e-26

B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as Mulibrey nanism protein, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of 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 RING finger, Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380837  Cd Length: 40  Bit Score: 100.48  E-value: 7.48e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767994850  59 DKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPL 98
Cdd:cd19779    1 DKCETHNEKLSVYCWTCKKCICHQCALWGGTHSGHTFKPL 40
MATH smart00061
meprin and TRAF homology;
250-345 6.18e-11

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 59.62  E-value: 6.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850   250 ENFSTLRqRADPVYSPPLQVSGLCWRLKVYPDGNgvvrgyYLSVFLELSAGLPETSKY--EYRVEMVHQSCNDptKNIIR 327
Cdd:smart00061   7 KNVSRLE-EGESYFSPSEEHFNIPWRLKIYRKNG------FLSLYLHCEKEECDSRKWsiEAEFTLKLVSQNG--KSLSK 77

                           90
                   ....*....|....*...
gi 767994850   328 EFASDFEVGECWGYNRFF 345
Cdd:smart00061  78 KDKHVFEKPSGWGFSKFI 95
zf-B_box pfam00643
B-box zinc finger;
56-98 1.41e-09

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 54.40  E-value: 1.41e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767994850   56 NEKDKCENHH-EKLSVFCWTCKKCICHQCALwgGMHGGHTFKPL 98
Cdd:pfam00643   1 SKERLCPEHEeEPLTLYCNDCQELLCEECSV--GEHRGHTVVPL 42
BBOX smart00336
B-Box-type zinc finger;
57-98 1.94e-09

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 53.88  E-value: 1.94e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 767994850    57 EKDKCENHH-EKLSVFCWTCKKCICHQCALWggMHGGHTFKPL 98
Cdd:smart00336   2 RAPKCDSHGdEPAEFFCEECGALLCRTCDEA--EHRGHTVVLL 42
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 251-364 7.39e-07

MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This domain is hugely expanded in the nematode C. elegans.


Pssm-ID: 425944 [Multi-domain]  Cd Length: 113  Bit Score: 48.79  E-value: 7.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850  251 NFSTLRQRaDPVYSPPLQVSGLCWRLKVYPDGNgvvrgyYLSVFL----ELSAGLPETSKYEYRVEMVHQSCNDPTKNII 326
Cdd:pfam00917   3 NFSKIKEG-ESYYSPVEERFNIPWRLQIYRKGG------FLGLYLhcdkEEELERGWSIETEFTLKLVSSNGKSVTKTDT 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767994850  327 REFASDfevgECWGYNRFFRLDLLANEgYLNpqNDTVI 364
Cdd:pfam00917  76 HVFEKP----KGWGWGKFISWDDLEKD-YLV--DDSIT 106
BAR_GRAF cd07636
The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion kinase; ...
 124-226 3.66e-03

The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion kinase; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. GTPase Regulator Associated with Focal adhesion kinase (GRAF), also called Rho GTPase activating protein 26 (ARHGAP26), is a GAP with activity towards RhoA and Cdc42 and is only weakly active towards Rac1. It influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase (FAK), which is a critical component of integrin signaling. GRAF contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of GRAF directly interacts with its Rho GAP domain and inhibits its activity. Autoinhibited GRAF is capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously.


Pssm-ID: 153320 [Multi-domain]  Cd Length: 207  Bit Score: 40.04  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850 124 ISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELL---------------ESLL 188
Cdd:cd07636   63 ICIARSLQEFAAVLRNLEDERTRMIENASEVLITPLEKFRKEQIGAAKEAKKKYDKETEKYcavlekhlnlsskkkESQL 142

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767994850 189 QEVEHQLRSCsKSELISKSSEILMMFQQVHRKPMASFV 226
Cdd:cd07636  143 HEADSQVDLV-RQHFYEVSLEYVFKVQEVQERKMFEFV 179
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
 6-21 4.85e-03

Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as mulibrey nanism protein, or MUL, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII 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 C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro.


Pssm-ID: 438281 [Multi-domain]  Cd Length: 43  Bit Score: 35.80  E-value: 4.85e-03
                         10
                 ....*....|....*.
gi 767994850   6 VERWLTEQRAQCPHCR 21
Cdd:cd16619   28 IRRWLSEQRSSCPHCR 43
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 242-370 6.60e-03

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 40.62  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850  242 YDSATFVLENFSTLrqrADPVYSPPLQVSGLCWRLKVYPDGNGVVRgyyLSVFLElsaglPETSKYEYRVEMVHQSC--- 318
Cdd:COG5077    38 EMSFTWKVKRWSEL---AKKVESPPFSVGGHTWKIILFPQGNNQCN---VSVYLE-----YEPQELEETGGKYYDCCaqf 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767994850  319 -------NDPTKNIIREFASDF--EVGEcWGYNRFFRLDLLANEGYLNP---QNDTVILRFQVR 370
Cdd:COG5077   107 afdisnpKYPTIEYINKSHHRFsmESTD-WGFTNFIDLNKLIEPSPGRPpflEEGTLVITVYVR 169
 
Name Accession Description Interval E-value
MATH_TRIM37 cd03773
Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal ...
 239-372 1.13e-83

Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal protein and is a member of the tripartite motif (TRIM) protein subfamily, also known as the RING-B-box-coiled-coil (RBCC) subfamily of zinc-finger proteins. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction and hepatomegaly. TRIM37, similar to other TRIMs, contains a cysteine-rich, zinc-binding RING-finger domain followed by another cysteine-rich zinc-binding domain, the B-box, and a coiled-coil domain. TRIM37 is autoubiquitinated in a RING domain-dependent manner, indicating that it functions as an ubiquitin E3 ligase. In addition to the tripartite motif, TRIM37 also contains a MATH domain C-terminal to the coiled-coil domain. The MATH domain of TRIM37 has been shown to interact with the TRAF domain of six known TRAFs in vitro, however, it is unclear whether this is physiologically relevant. Eleven TRIM37 mutations have been associated with Mulibrey nanism so far. One mutation, Gly322Val, is located in the MATH domain and is the only mutation that does not affect the length of the protein. It results in the incorrect subcellular localization of TRIM37.


Pssm-ID: 239742  Cd Length: 132  Bit Score: 265.43  E-value: 1.13e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850 239 VPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSc 318
Cdd:cd03773    1 IPPYDSATFTLENFSTLRQSADPVYSDPLNVDGLCWRLKVYPDGNGEVRGNFLSVFLELCSGLGEASKYEYRVEMVHQA- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767994850 319 nDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILRFQVRSP 372
Cdd:cd03773   80 -NPTKNIKREFASDFEVGECWGYNRFFRLDLLINEGYLLPENDTLILRFSVRPP 132
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 98-220 1.28e-27

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 108.51  E-value: 1.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850    98 LAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVE----MMIARLDTQLKNKLITLMGQ 173
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNkrkkQLLEDLEEQKENKLKVLEQQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 767994850   174 KTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRK 220
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 246-370 1.99e-26

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: 105.15  E-value: 1.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850 246 TFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGvVRGYYLSVFLELSAGLPETS----KYEYRVEMVHQscnDP 321
Cdd:cd00121    2 KHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDG-ESGDYLSLYLELDKGESDLEkwsvRAEFTLKLVNQ---NG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767994850 322 TKNIIREFASDF--EVGECWGYNRFFRLDLLANEGYLNpqNDTVILRFQVR 370
Cdd:cd00121   78 GKSLSKSFTHVFfsEKGSGWGFPKFISWDDLEDSYYLV--DDSLTIEVEVK 126
Bbox2_TRIM37_C-VIII cd19779
B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar ...
 59-98 7.48e-26

B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as Mulibrey nanism protein, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of 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 RING finger, Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380837  Cd Length: 40  Bit Score: 100.48  E-value: 7.48e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767994850  59 DKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPL 98
Cdd:cd19779    1 DKCETHNEKLSVYCWTCKKCICHQCALWGGTHSGHTFKPL 40
MATH smart00061
meprin and TRAF homology;
250-345 6.18e-11

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 59.62  E-value: 6.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850   250 ENFSTLRqRADPVYSPPLQVSGLCWRLKVYPDGNgvvrgyYLSVFLELSAGLPETSKY--EYRVEMVHQSCNDptKNIIR 327
Cdd:smart00061   7 KNVSRLE-EGESYFSPSEEHFNIPWRLKIYRKNG------FLSLYLHCEKEECDSRKWsiEAEFTLKLVSQNG--KSLSK 77

                           90
                   ....*....|....*...
gi 767994850   328 EFASDFEVGECWGYNRFF 345
Cdd:smart00061  78 KDKHVFEKPSGWGFSKFI 95
zf-B_box pfam00643
B-box zinc finger;
56-98 1.41e-09

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 54.40  E-value: 1.41e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767994850   56 NEKDKCENHH-EKLSVFCWTCKKCICHQCALwgGMHGGHTFKPL 98
Cdd:pfam00643   1 SKERLCPEHEeEPLTLYCNDCQELLCEECSV--GEHRGHTVVPL 42
BBOX smart00336
B-Box-type zinc finger;
57-98 1.94e-09

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 53.88  E-value: 1.94e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 767994850    57 EKDKCENHH-EKLSVFCWTCKKCICHQCALWggMHGGHTFKPL 98
Cdd:smart00336   2 RAPKCDSHGdEPAEFFCEECGALLCRTCDEA--EHRGHTVVLL 42
Bbox2 cd19756
B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of ...
 60-98 3.07e-09

B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interaction. Based on different consensus sequence and the spacing of the 7-8 zinc-binding residues, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). The family corresponds to type 2 B-box (Bbox2).


Pssm-ID: 380814 [Multi-domain]  Cd Length: 39  Bit Score: 53.18  E-value: 3.07e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767994850  60 KCENHHEK-LSVFCWTCKKCICHQCALWgGMHGGHTFKPL 98
Cdd:cd19756    1 LCPEHPEEpLKLFCETCQELVCVLCLLS-GEHRGHKVVPL 39
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 251-364 7.39e-07

MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This domain is hugely expanded in the nematode C. elegans.


Pssm-ID: 425944 [Multi-domain]  Cd Length: 113  Bit Score: 48.79  E-value: 7.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850  251 NFSTLRQRaDPVYSPPLQVSGLCWRLKVYPDGNgvvrgyYLSVFL----ELSAGLPETSKYEYRVEMVHQSCNDPTKNII 326
Cdd:pfam00917   3 NFSKIKEG-ESYYSPVEERFNIPWRLQIYRKGG------FLGLYLhcdkEEELERGWSIETEFTLKLVSSNGKSVTKTDT 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767994850  327 REFASDfevgECWGYNRFFRLDLLANEgYLNpqNDTVI 364
Cdd:pfam00917  76 HVFEKP----KGWGWGKFISWDDLEKD-YLV--DDSIT 106
MATH_TRAF_C cd00270
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal ...
 249-369 9.04e-07

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: 49.53  E-value: 9.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850 249 LENFSTLRQRAD-----PVYSPPLQVSG----LCwrLKVYPDGNGVVRGYYLSVFL-----ELSAGLPETSKYEYRVEMV 314
Cdd:cd00270    7 IKDYSRKLQEAVagsntVLYSPPFYTSRygykLC--LRLYLNGDGTGKGTHLSLFVhvmkgEYDALLEWPFRGKITLTLL 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767994850 315 HQSCNDPTKNIIREFASD-----FEVGEC------WGYNRFFRLDLLANEGYLnpQNDTVILRFQV 369
Cdd:cd00270   85 DQSDDSKRKHITETFMPDpnssaFQRPPTgennigFGYPEFVPLEKLESRGYV--KDDTLFIKVEV 148
MATH_Ubp21p cd03775
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ...
 243-370 3.43e-06

Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with similarity to Ubp21p of fission yeast. Ubp21p is a deubiquitinating enzyme that may be involved in the regulation of the protein kinase Prp4p, which controls the formation of active spliceosomes. Members of this family are similar to human HAUSP (Herpesvirus-associated ubiquitin-specific protease) in that they contain an N-terminal MATH domain and a C-terminal catalytic protease (C19 family) domain. HAUSP is also an ubiquitin-specific protease that specifically catalyzes the deubiquitylation of p53 and MDM2. The MATH domain of HAUSP contains the binding site for p53 and MDM2. Similarly, the MATH domain of members in this family may be involved in substrate binding.


Pssm-ID: 239744  Cd Length: 134  Bit Score: 47.35  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850 243 DSATFVLENFSTLRQRadpVYSPPLQVSGLCWRLKVYPDGNGVVRgyYLSVFLE------LSAGLPETSKYEYRVEMVHQ 316
Cdd:cd03775    1 QSFTWRIKNWSELEKK---VHSPKFKCGGFEWRILLFPQGNSQTG--GVSIYLEphpeeeEKAPLDEDWSVCAQFALVIS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767994850 317 SCNDPTKNIIREFASDFEVGEC-WGYNRFFRLDLLANEGYLNP----QNDTVILRFQVR 370
Cdd:cd03775   76 NPGDPSIQLSNVAHHRFNAEDKdWGFTRFIELRKLAHRTPDKPspflENGELNITVYVR 134
Bbox2_TRIM16-like cd19769
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, ...
 60-100 9.25e-06

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, TRIM47 and similar proteins; This family includes a group of tripartite motif-containing proteins, such as TRIM16, TRIM29 and TRIM47. TRIM16, also termed estrogen-responsive B box protein (EBBP), is a regulator that may play a role in the regulation of keratinocyte differentiation. It may also act as a tumor suppressor through affecting cell proliferation and migration or tumorigenicity in carcinogenesis. TRIM29, also termed ataxia telangiectasia group D-associated protein (ATDC), plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. TRIM16 and TRIM29 belong to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. TRIM47 belongs to the C-IV subclass of TRIM family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380827 [Multi-domain]  Cd Length: 46  Bit Score: 43.47  E-value: 9.25e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 767994850  60 KCENHHEKLSVFCWTCKKCICHQCALwgGMHGGHTFKPLAE 100
Cdd:cd19769    2 VCPIHKKPLELFCRTDQMCICELCAK--EEHRGHDVVTVEE 40
Bbox2_TRIM14 cd19768
B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar ...
 59-102 1.81e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar proteins; TRIM14 is a mitochondrial adaptor that facilitates innate immune signaling. It also plays a critical role in tumor development. TRIM14 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. It contains a Bbox2 zinc finger as well as a C-terminal SPRY/B30.2 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380826 [Multi-domain]  Cd Length: 44  Bit Score: 42.80  E-value: 1.81e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767994850  59 DKCENHHE-KLSVFCWTCKKCICHQCALWGGmHGGHTFKPLAEIY 102
Cdd:cd19768    1 RCCPEHKDrPLELFCKTCKRCVCALCPILGQ-HRGHDVRLIDEEA 44
Bbox2_TRIM65-like cd19793
B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65), B box and ...
 59-100 4.12e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65), B box and SPRY domain-containing protein (BSPRY) and similar proteins; The family includes TRIM65 and BSPRY. TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5 enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. BSPRY is a regulatory protein for maintaining calcium homeostasis. It may regulate epithelial calcium transport by inhibiting TRPV5 activity. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380851  Cd Length: 43  Bit Score: 41.52  E-value: 4.12e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767994850  59 DKCENHHEKLSVFCWTCKKCICHQCALWGGMHgGHTFKPLAE 100
Cdd:cd19793    1 ELCPEHGRELELYCRTEKRCVCAQCASKGECR-GHRVTLLEE 41
Bbox2_TRIM9-like cd19764
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM9, TRIM67 and ...
 60-98 6.54e-05

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM9, TRIM67 and similar proteins; This family includes a group of tripartite motif-containing proteins including TRIM9 and TRIM67, both of which belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. It plays an important role in the regulation of neuronal functions and participates in neurodegenerative disorders through its ligase activity. TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis.


Pssm-ID: 380822  Cd Length: 39  Bit Score: 40.84  E-value: 6.54e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767994850  60 KCENH-HEKLSVFCWTCKKCICHQCaLWGGMHGGHTFKPL 98
Cdd:cd19764    1 TCSEHpDEALSMYCLSCKVPVCYLC-LEDGRHSNHDVQAL 39
Bbox2_TRIM67_C-I cd19827
B-box-type 2 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar ...
 61-103 3.58e-04

B-box-type 2 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar proteins; TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis. TRIM67 belongs to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380885  Cd Length: 45  Bit Score: 39.20  E-value: 3.58e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767994850  61 CENHH-EKLSVFCWTCKKCICHQCaLWGGMHGGHTFKPLAEIYE 103
Cdd:cd19827    3 CAEHElENYSMYCASCRTPVCYQC-LEEGKHAKHEVKALGAMWK 45
Bbox2_BSPRY cd19834
B-box-type 2 zinc finger found in B box and SPRY domain-containing protein (BSPRY) and ...
 59-100 4.25e-04

B-box-type 2 zinc finger found in B box and SPRY domain-containing protein (BSPRY) and similar proteins; BSPRY is a regulatory protein for maintaining calcium homeostasis. It may regulate epithelial calcium transport by inhibiting TRPV5 activity. BSPRY is composed of a B-box, an alpha-helical coiled coil and a SPRY domain. The B-box motif shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380892  Cd Length: 43  Bit Score: 38.91  E-value: 4.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767994850  59 DKCENHHEKLSVFCWTCKKCICHQCALWGGMHgGHTFKPLAE 100
Cdd:cd19834    1 DLCPDHELELDWFCSTERRLVCAQCASLGTCR-GHRVTPLEE 41
Bbox2_xNF7-like cd19800
B-box-type 2 zinc finger found in Xenopus laevis nuclear factor 7 (xNF7) and similar proteins; ...
 59-98 5.49e-04

B-box-type 2 zinc finger found in Xenopus laevis nuclear factor 7 (xNF7) and similar proteins; xNF7 is a maternally expressed novel zinc finger nuclear phosphoprotein. It acts as a transcription factor that determines dorsal-ventral body axis. xNF7 harbors a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380858 [Multi-domain]  Cd Length: 39  Bit Score: 38.15  E-value: 5.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767994850  59 DKCENHHEKLSVFCWTCKKCICHQCALwGGMHGGHTFKPL 98
Cdd:cd19800    1 EVCSEHDEPLKLFCKDDKRLICVICRD-SRKHRGHRFLPV 39
Bbox2_TRIM72_C-IV cd19797
B-box-type 2 zinc finger found in tripartite motif-containing protein 72 (TRIM72) and similar ...
 59-100 2.18e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 72 (TRIM72) and similar proteins; TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis via targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 belongs to the C-IV subclass of 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 RING 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. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380855 [Multi-domain]  Cd Length: 42  Bit Score: 36.87  E-value: 2.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767994850  59 DKCENHHEKLSVFCWTCKKCICHQCALWGGmHGGHTFKPLAE 100
Cdd:cd19797    1 GHCEEHLDPLSVYCEQDRALICGVCASLGK-HKGHNIITAAE 41
MATH_HAUSP cd03772
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ...
 247-369 2.91e-03

Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, N-terminal MATH (TRAF-like) domain; composed of proteins similar to human HAUSP, an enzyme that specifically catalyzes the deubiquitylation of p53 and MDM2, hence playing an important role in the p53-MDM2 pathway. It contains an N-terminal TRAF-like domain and a C-terminal catalytic protease (C19 family) domain. The tumor suppressor p53 protein is a transcription factor that responds to many cellular stress signals and is regulated primarily through ubiquitylation and subsequent degradation. MDM2 is a RING-finger E3 ubiquitin ligase that promotes p53 ubiquitinylation. p53 and MDM2 bind to the same site in the N-terminal TRAF-like domain of HAUSP in a mutually exclusive manner. HAUSP also interacts with the Epstein-Barr nuclear antigen 1 (EBNA1) protein of the Epstein-Barr virus (EBV), which efficiently immortalizes infected cells predisposing the host to a variety of cancers. EBNA1 plays several important roles in EBV latent infection and cellular transformation. It binds the same pocket as p53 in the HAUSP TRAF-like domain. Through interactions with p53, MDM2 and EBNA1, HAUSP plays a role in cell proliferation, apoptosis and EBV-mediated immortalization.


Pssm-ID: 239741  Cd Length: 137  Bit Score: 38.97  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850 247 FVLENFSTLRQRadpVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSV--FLELSaglPETSKYEYRV----EMVHQSCND 320
Cdd:cd03772    7 FTVERFSRLSES---VLSPPCFVRNLPWKIMVMPRNYPDRNPHQKSVgfFLQCN---AESDSTSWSChaqaVLRIINYKD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767994850 321 PTKNIIREFASDFEVGEC-WGYNRFFRLDLLANE--GYLnpQNDTVILRFQV 369
Cdd:cd03772   81 DEPSFSRRISHLFFSKENdWGFSNFMTWSEVTDPekGFI--EDDTITLEVYV 130
BAR_GRAF cd07636
The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion kinase; ...
 124-226 3.66e-03

The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion kinase; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. GTPase Regulator Associated with Focal adhesion kinase (GRAF), also called Rho GTPase activating protein 26 (ARHGAP26), is a GAP with activity towards RhoA and Cdc42 and is only weakly active towards Rac1. It influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase (FAK), which is a critical component of integrin signaling. GRAF contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of GRAF directly interacts with its Rho GAP domain and inhibits its activity. Autoinhibited GRAF is capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously.


Pssm-ID: 153320 [Multi-domain]  Cd Length: 207  Bit Score: 40.04  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850 124 ISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELL---------------ESLL 188
Cdd:cd07636   63 ICIARSLQEFAAVLRNLEDERTRMIENASEVLITPLEKFRKEQIGAAKEAKKKYDKETEKYcavlekhlnlsskkkESQL 142

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767994850 189 QEVEHQLRSCsKSELISKSSEILMMFQQVHRKPMASFV 226
Cdd:cd07636  143 HEADSQVDLV-RQHFYEVSLEYVFKVQEVQERKMFEFV 179
Bbox2_TRIM71_C-VII cd19796
B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar ...
 61-104 4.22e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar proteins; TRIM71, also known as protein lineage variant 41 (lin-41), is an E3 ubiquitin-protein ligase that may play essential roles in embryonic stem cells, cellular reprogramming, and the timing of embryonic neurogenesis. It was first identified in the nematode Caenorhabditis elegans as a target of the differentiation-associated microRNA (miRNA) let-7 (lethal 7), and therefore part of a heterochronic gene network that controls larval development. In humans, it regulates let-7 microRNA biogenesis via modulation of Lin28B protein polyubiquitination. TRIM71 localizes to cytoplasmic P-bodies and directly interacts with the miRNA pathway proteins Argonaute 2 (AGO2) and DICER. It represses miRNA activity by promoting degradative ubiquitination of AGO2. Moreover, TRIM71 associates with SHCBP1, a novel component of the fibroblast growth factor (FGF) signaling pathway, and regulates its non-degradative polyubiquitination. It is also involved in the post-transcriptional regulation of the CDKN1A, RBL1 and RBL2 or EGR1 mRNAs through mediating RNA-binding in embryonic stem cells. TRIM71 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380854 [Multi-domain]  Cd Length: 48  Bit Score: 36.13  E-value: 4.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767994850  61 CENH-HEKLSVFCWTCKKCICHQCALwgGMHGGHTFKPLAEIYEQ 104
Cdd:cd19796    4 CEIHeHEVLRLYCDTCSVPICRECTM--GEHRGHSFIYLQEAVQD 46
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
 6-21 4.85e-03

Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as mulibrey nanism protein, or MUL, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII 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 C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro.


Pssm-ID: 438281 [Multi-domain]  Cd Length: 43  Bit Score: 35.80  E-value: 4.85e-03
                         10
                 ....*....|....*.
gi 767994850   6 VERWLTEQRAQCPHCR 21
Cdd:cd16619   28 IRRWLSEQRSSCPHCR 43
Bbox2_TRIM46_C-I cd19786
B-box-type 2 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar ...
 61-103 5.88e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar proteins; TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins, which are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380844 [Multi-domain]  Cd Length: 46  Bit Score: 35.66  E-value: 5.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767994850  61 CENHHEKLSVFCWTCKKCICHQCALwGGMHGGHTFKPLAEIYE 103
Cdd:cd19786    5 CPEHKEEVTHYCKTCQRLVCQLCRV-RRTHAGHKITPVLSAYQ 46
Bbox2_TRIM36_C-I cd19778
B-box-type 2 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar ...
 61-102 6.24e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar proteins; TRIM36, human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation through interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380836  Cd Length: 45  Bit Score: 35.59  E-value: 6.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767994850  61 CENHH-EKLSVFCWTCKKCICHQCALwGGMHGGHTFKPLAEIY 102
Cdd:cd19778    3 CPEHEmEKVNMYCEACRRPVCHLCKL-GGSHANHRVTSMSSAY 44
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 242-370 6.60e-03

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 40.62  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850  242 YDSATFVLENFSTLrqrADPVYSPPLQVSGLCWRLKVYPDGNGVVRgyyLSVFLElsaglPETSKYEYRVEMVHQSC--- 318
Cdd:COG5077    38 EMSFTWKVKRWSEL---AKKVESPPFSVGGHTWKIILFPQGNNQCN---VSVYLE-----YEPQELEETGGKYYDCCaqf 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767994850  319 -------NDPTKNIIREFASDF--EVGEcWGYNRFFRLDLLANEGYLNP---QNDTVILRFQVR 370
Cdd:COG5077   107 afdisnpKYPTIEYINKSHHRFsmESTD-WGFTNFIDLNKLIEPSPGRPpflEEGTLVITVYVR 169
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
 6-31 9.05e-03

Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.


Pssm-ID: 438114 [Multi-domain]  Cd Length: 61  Bit Score: 35.67  E-value: 9.05e-03
                         10        20
                 ....*....|....*....|....*.
gi 767994850   6 VERWLTEQRAQCPHCRAPLQLRELVN 31
Cdd:cd16450   34 IEKWLKGKGKKCPQCNKKAKRSDIRP 59
MATH_SPOP cd03774
Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to ...
 249-353 9.37e-03

Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to human SPOP. SPOP was isolated as a novel antigen recognized by serum from a scleroderma patient, whose overexpression in COS cells results in a discrete speckled pattern in the nuclei. It contains an N-terminal MATH domain and a C-terminal BTB (also called POZ) domain. Together with Cul3, SPOP constitutes an ubiquitin E3 ligase which is able to ubiquitinate the PcG protein BMI1, the variant histone macroH2A1 and the death domain-associated protein Daxx. Therefore, SPOP may be involved in the regulation of these proteins and may play a role in transcriptional regulation, apoptosis and X-chromosome inactivation. Cul3 binds to the BTB domain of SPOP whereas Daxx and the macroH2A1 nonhistone region have been shown to bind to the MATH domain. Both MATH and BTB domains are necessary for the nuclear speckled accumulation of SPOP. There are many proteins, mostly uncharacterized, containing both MATH and BTB domains from C. elegans and plants which are excluded from this family.


Pssm-ID: 239743  Cd Length: 139  Bit Score: 37.53  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994850 249 LENFSTLRQRADPVYSPPLQVSG----LCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHqSCNDPTKN 324
Cdd:cd03774   11 ISNFSFCREEMGEVIKSSTFSSGandkLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSILN-AKGEETKA 89

                         90       100
                 ....*....|....*....|....*....
gi 767994850 325 IIREFASDFEVGECWGYNRFFRLDLLANE 353
Cdd:cd03774   90 MESQRAYRFVQGKDWGFKKFIRRDFLLDE 118
Bbox2_TRIM9_C-I cd19826
B-box-type 2 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar ...
 61-103 9.90e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar proteins; TRIM9 (the human ortholog of rat Spring), also termed RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducer repeat-containing protein (beta-TCP) through its N-terminal degron motif (DSGXXS) depending on the phosphorylation status, and thus negatively regulate nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and exocytosis soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of 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 RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380884  Cd Length: 49  Bit Score: 35.07  E-value: 9.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767994850  61 CENHH-EKLSVFCWTCKKCICHQCaLWGGMHGGHTFKPLAEIYE 103
Cdd:cd19826    7 CTDHElENHSMYCVQCKMPVCYQC-LEEGKHSSHEVKALGAMWK 49
 
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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