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Conserved domains on  [gi|451770402|ref|NP_001263420|]
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E3 ubiquitin-protein ligase TRIM34 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
 299-483 8.48e-137

PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM34, also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1). TRIM34 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. The TRIM21 cDNA possesses at least three kinds of isoforms, due to alternative splicing, of which only the long and medium forms contain the SPRY domain. It is an interferon-induced protein, predominantly expressed in the testis, kidney, and ovary. The SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. While the PRY-SPRY domain provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.


:

Pssm-ID: 293997  Cd Length: 185  Bit Score: 391.89  E-value: 8.48e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 299 WADFTFNPENLNLNLILSEDHRQVTSVPIWPFKCCNNGILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRTLKFDVRRC 378
Cdd:cd15825    1 WVDFTLNPVNLNLNLVLSEDQRQVTSVPIWPFKCYNYGILGSQYFSSGKHYWEVDVSKKTAWILGVYCRKRSRTFKYVRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 379 SKSQPNGYHRYKPQNGYWVIGLQDGSKYSIFEDSSNCGPTVLNPFVATPLHRIGVFLDCEEGIVSFFNVTNHGSLIYKFT 458
Cdd:cd15825   81 GKNHPNVYSRYRPQYGYWVIGLQNKSEYYAFEDSSTSDPKVLTLSVATPPHRVGVFLDYEAGTVSFFNVTNHGSLIYKFS 160

                        170       180
                 ....*....|....*....|....*
gi 451770402 459 QCRFSQPAYPYFNPWDCPAPMTLCP 483
Cdd:cd15825  161 KCCFSQPVYPYFNPWNCPAPMTLCP 185
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 7-78 4.66e-25

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 cd16591:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 72  Bit Score: 97.90  E-value: 4.66e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 451770402   7 TDVQKEATCPVCHVLLIKPLNLGSGHHVSQACLTVKKTAVTNPRGKSLCPMCGNRFSFENLQANKHLADVVE 78
Cdd:cd16591    1 VNIKEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESVNQEGESSCPVCRTSYQPENLRPNRHLANIVE 72
Bbox2_TRIM5-like cd19761
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, ...
 94-131 8.14e-20

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34, TRIM38 and similar proteins; The family includes TRIM5, TRIM6, TRIM22, TRIM34, and TRIM38, all of which belong 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 RING finger, 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. TRIM5, also termed RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also termed RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also termed 50 kDa-stimulated trans-acting factor (Staf-50), or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also termed interferon-responsive finger protein 1, or RING finger protein 21 (RNF21), may function as an antiviral protein that contributes to the defense against retroviral infections. TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates tumor necrosis factor alpha (TNF-alpha) and interleukin-1beta-triggered nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome.


:

Pssm-ID: 380819 [Multi-domain]  Cd Length: 40  Bit Score: 82.54  E-value: 8.14e-20
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 451770402  94 DLCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFL 131
Cdd:cd19761    1 DHCEHHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFL 38
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-247 4.64e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 4.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 131 LRDEAVRECQENLQEALKRLRKEQEKVETFEAD---IKEDRISWKHQIQTERQRIQTGYNQLRRILDKEE--QNELKRLR 205
Cdd:COG4372   28 ALSEQLRKALFELDKLQEELEQLREELEQAREEleqLEEELEQARSELEQLEEELEELNEQLQAAQAELAqaQEELESLQ 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 451770402 206 EEEQMILDSLAGAEAE---LAQQSQLVEELISDLERRCEWSDTEL 247
Cdd:COG4372  108 EEAEELQEELEELQKErqdLEQQRKQLEAQIAELQSEIAEREEEL 152
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
 299-483 8.48e-137

PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM34, also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1). TRIM34 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. The TRIM21 cDNA possesses at least three kinds of isoforms, due to alternative splicing, of which only the long and medium forms contain the SPRY domain. It is an interferon-induced protein, predominantly expressed in the testis, kidney, and ovary. The SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. While the PRY-SPRY domain provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.


Pssm-ID: 293997  Cd Length: 185  Bit Score: 391.89  E-value: 8.48e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 299 WADFTFNPENLNLNLILSEDHRQVTSVPIWPFKCCNNGILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRTLKFDVRRC 378
Cdd:cd15825    1 WVDFTLNPVNLNLNLVLSEDQRQVTSVPIWPFKCYNYGILGSQYFSSGKHYWEVDVSKKTAWILGVYCRKRSRTFKYVRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 379 SKSQPNGYHRYKPQNGYWVIGLQDGSKYSIFEDSSNCGPTVLNPFVATPLHRIGVFLDCEEGIVSFFNVTNHGSLIYKFT 458
Cdd:cd15825   81 GKNHPNVYSRYRPQYGYWVIGLQNKSEYYAFEDSSTSDPKVLTLSVATPPHRVGVFLDYEAGTVSFFNVTNHGSLIYKFS 160

                        170       180
                 ....*....|....*....|....*
gi 451770402 459 QCRFSQPAYPYFNPWDCPAPMTLCP 483
Cdd:cd15825  161 KCCFSQPVYPYFNPWNCPAPMTLCP 185
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
 7-78 4.66e-25

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong 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. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


Pssm-ID: 438253 [Multi-domain]  Cd Length: 72  Bit Score: 97.90  E-value: 4.66e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 451770402   7 TDVQKEATCPVCHVLLIKPLNLGSGHHVSQACLTVKKTAVTNPRGKSLCPMCGNRFSFENLQANKHLADVVE 78
Cdd:cd16591    1 VNIKEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESVNQEGESSCPVCRTSYQPENLRPNRHLANIVE 72
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 345-483 1.32e-22

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 92.74  E-value: 1.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   345 SGKHYWEVDVSEKNAWTLGVysrkrtlkfdvrrCSKSQPNGYHRYKPQN-GYWVIGLQDGSKYSifedssNCGPTVLNPF 423
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGV-------------ATKSVPRGYFALLGEDkGSWGYDGDGGKKYH------NSTGPEYGLP 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 451770402   424 VATPLHRIGVFLDCEEGIVSFFNVTNHgSLIYKFTQCRFSQPAYPYFNPWD-CPAPMTLCP 483
Cdd:smart00449  62 LQEPGDVIGCFLDLEAGTISFYKNGKY-LHGLAFFDVKFSGPLYPAFSLGSgNSVRLNFGP 121
Bbox2_TRIM5-like cd19761
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, ...
 94-131 8.14e-20

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34, TRIM38 and similar proteins; The family includes TRIM5, TRIM6, TRIM22, TRIM34, and TRIM38, all of which belong 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 RING finger, 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. TRIM5, also termed RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also termed RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also termed 50 kDa-stimulated trans-acting factor (Staf-50), or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also termed interferon-responsive finger protein 1, or RING finger protein 21 (RNF21), may function as an antiviral protein that contributes to the defense against retroviral infections. TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates tumor necrosis factor alpha (TNF-alpha) and interleukin-1beta-triggered nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome.


Pssm-ID: 380819 [Multi-domain]  Cd Length: 40  Bit Score: 82.54  E-value: 8.14e-20
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 451770402  94 DLCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFL 131
Cdd:cd19761    1 DHCEHHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFL 38
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 347-470 5.38e-19

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 82.78  E-value: 5.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402  347 KHYWEVDVS--EKNAWTLGVysrkrtlkfdvrrCSKSQPNGYHRYK-PQNGYWVIGLQDGSKYSifedssNCGPTVLNPF 423
Cdd:pfam00622   1 RHYFEVEIFgqDGGGWRVGW-------------ATKSVPRKGERFLgDESGSWGYDGWTGKKYW------ASTSPLTGLP 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 451770402  424 VATPLHRIGVFLDCEEGIVSFFNvtNHGSLIYKFTQCRFSQPAYPYF 470
Cdd:pfam00622  62 LFEPGDVIGCFLDYEAGTISFTK--NGKSLGYAFRDVPFAGPLFPAV 106
BBOX smart00336
B-Box-type zinc finger;
91-131 7.42e-08

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 48.49  E-value: 7.42e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 451770402    91 KKGDLC-VHHGEKLLLFCQEDKKVICWVCERSqEHRGHHTFL 131
Cdd:smart00336   1 QRAPKCdSHGDEPAEFFCEECGALLCRTCDEA-EHRGHTVVL 41
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-247 4.64e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 4.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 131 LRDEAVRECQENLQEALKRLRKEQEKVETFEAD---IKEDRISWKHQIQTERQRIQTGYNQLRRILDKEE--QNELKRLR 205
Cdd:COG4372   28 ALSEQLRKALFELDKLQEELEQLREELEQAREEleqLEEELEQARSELEQLEEELEELNEQLQAAQAELAqaQEELESLQ 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 451770402 206 EEEQMILDSLAGAEAE---LAQQSQLVEELISDLERRCEWSDTEL 247
Cdd:COG4372  108 EEAEELQEELEELQKErqdLEQQRKQLEAQIAELQSEIAEREEEL 152
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
134-256 6.58e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 134 EAVRECQENLQEaLKRLRKEQ-----EKVETFEADIKEDRISwkhQIQTERQRIQTgYnqLRRILDKeeqneLKRLREEE 208
Cdd:PRK02224 609 ERLREKREALAE-LNDERRERlaekrERKRELEAEFDEARIE---EAREDKERAEE-Y--LEQVEEK-----LDELREER 676

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 451770402 209 QMILDSLAGAEAELAQQSQLVEELiSDLERRCE-----WSDTELLQDVSGILK 256
Cdd:PRK02224 677 DDLQAEIGAVENELEELEELRERR-EALENRVEalealYDEAEELESMYGDLR 728
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 138-247 8.39e-05

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: 44.89  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402  138 ECQENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRILDK-----EEQNELKRLREEEQMIL 212
Cdd:pfam07888  38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKheeleEKYKELSASSEELSEEK 117

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 451770402  213 DSLAGAEAELAQQSQLVEELISDLERRCEWSDTEL 247
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 141-265 1.09e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 44.24  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   141 ENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERqriqtgynQLRRILDKEEQNELKRLREE------EQMI--- 211
Cdd:smart00787 154 EGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK--------QLEDELEDCDPTELDRAKEKlkkllqEIMIkvk 225

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 451770402   212 --------LDSLAGAEAELAQQSQLVEELISDLERR------CEWSDTELLQDVSGILKWSQIWTLKK 265
Cdd:smart00787 226 kleeleeeLQELESKIEDLTNKKSELNTEIAEAEKKleqcrgFTFKEIEKLKEQLKLLQSLTGWKITK 293
zf-B_box pfam00643
B-box zinc finger;
91-129 1.29e-04

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 39.38  E-value: 1.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 451770402   91 KKGDLC-VHHGEKLLLFCQEDKKVICWVCERSqEHRGHHT 129
Cdd:pfam00643   1 SKERLCpEHEEEPLTLYCNDCQELLCEECSVG-EHRGHTV 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 134-239 6.37e-04

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   134 EAVRECQENLQEALKRLRKEQEKVETFEADIKEDRISwKHQIQTERQRIQTGYNQLRRILDKEEQNELKRLREEEQMILD 213
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450

                           90       100
                   ....*....|....*....|....*.
gi 451770402   214 SLAGAEAELAQQSQLVEELISDLERR 239
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQA 476
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
 299-483 8.48e-137

PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM34, also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1). TRIM34 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. The TRIM21 cDNA possesses at least three kinds of isoforms, due to alternative splicing, of which only the long and medium forms contain the SPRY domain. It is an interferon-induced protein, predominantly expressed in the testis, kidney, and ovary. The SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. While the PRY-SPRY domain provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.


Pssm-ID: 293997  Cd Length: 185  Bit Score: 391.89  E-value: 8.48e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 299 WADFTFNPENLNLNLILSEDHRQVTSVPIWPFKCCNNGILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRTLKFDVRRC 378
Cdd:cd15825    1 WVDFTLNPVNLNLNLVLSEDQRQVTSVPIWPFKCYNYGILGSQYFSSGKHYWEVDVSKKTAWILGVYCRKRSRTFKYVRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 379 SKSQPNGYHRYKPQNGYWVIGLQDGSKYSIFEDSSNCGPTVLNPFVATPLHRIGVFLDCEEGIVSFFNVTNHGSLIYKFT 458
Cdd:cd15825   81 GKNHPNVYSRYRPQYGYWVIGLQNKSEYYAFEDSSTSDPKVLTLSVATPPHRVGVFLDYEAGTVSFFNVTNHGSLIYKFS 160

                        170       180
                 ....*....|....*....|....*
gi 451770402 459 QCRFSQPAYPYFNPWDCPAPMTLCP 483
Cdd:cd15825  161 KCCFSQPVYPYFNPWNCPAPMTLCP 185
SPRY_PRY_TRIM5_6_22_34 cd15810
PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and ...
 301-482 7.37e-98

PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and TRIM34); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of very close paralogs, TRIM5, TRIM6, TRIM22 and TRIM34. These domains are composed of RING/B-box/coiled-coil core and are also known as RBCC proteins. They form a locus of four closely related TRIM genes within an olfactory receptor-rich region on chromosome 11 of the human genome. Genetic analysis of this locus indicates that these four genes have evolved by gene duplication from a common ancestral gene. All genes in the TRIM6/TRIM34/TRIM5/TRIM22 locus are type I interferon inducible, with TRIM5 and TRIM22 possessing antiviral properties. TRIM5 promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, amplifying these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction. TRIM6 is selectively expressed in embryonic stem (ES) cells and interacts with the proto-oncogene product Myc, maintaining the pluripotency of the ES cells. TRIM6, together with E2 Ubiquitin conjugase (UbE2K) and K48-linked poly-Ub chains, is critical for the IkappaB kinase epsilon (IKKepsilon) branch of type I interferon (IFN-I) signaling pathway and subsequent establishment of a protective antiviral response. TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. While the PRY-SPRY domain of TRIM5a provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.


Pssm-ID: 293982 [Multi-domain]  Cd Length: 189  Bit Score: 292.85  E-value: 7.37e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQVTSVPIWPFKCC------NNGILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRT--LK 372
Cdd:cd15810    1 DVTLNPVNISLNIVISEDQRQVRIVPPQTSGQAltnnnyDFGVLGSQYFSSGKHYWEVDVSKKSAWILGVCSHKRSdaMT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 373 FDVRRcSKSQPNGYHRYKPQNGYWVIGLQDGSKYSIFEDSSNCGPTVLNPFVATPLHRIGVFLDCEEGIVSFFNVTNHGS 452
Cdd:cd15810   81 KSNAN-QINHQNVYSRYQPQYGYWVIGLQNESEYNAFEDSSSFNPHVLTLSVTVPPHRVGVFLDYEAGTVSFFNVTNHGS 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 451770402 453 LIYKFTQCRFSQPAYPYFNPWDCPAPMTLC 482
Cdd:cd15810  160 LIYKFSKCCFSTTVCPYFNPWNCPVPMTLC 189
SPRY_PRY_TRIM5 cd15822
PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger ...
 289-482 4.84e-94

PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger protein 88 (RNF88); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM5 which is also known as RING finger protein 88 (RNF88) or TRIM5alpha (TRIM5a), an antiretroviral restriction factor and a retrovirus capsid sensor in immune signaling. TRIM5 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It blocks retrovirus infection soon after the virion core enters the cell cytoplasm by recognizing the capsid protein lattice that encases the viral genomic RNA; the SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. TRIM5a, an E3 ubiquitin ligase, promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, and amplifies these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction.


Pssm-ID: 293994  Cd Length: 200  Bit Score: 283.35  E-value: 4.84e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 289 FRELTAVRAYWADFTFNPENlNLNLILSEDHRQVTSVPIWPFK-----CCNNGILGSKCFLSGKHYWEVDVSEKNAWTLG 363
Cdd:cd15822    1 FNELTDVQRYWVHVTLDPSN-NKNIVISEDRRQVRYVRKQQRYnsngnNEDYGVLGSPSITSGKHYWEVDVSKKRAWILG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 364 VYSRK---RTLKFDVRRCSKSQPNgYHRYKPQNGYWVIGLQDGSKYSIFEDSSNCGPTVLNPFVATPLHRIGVFLDCEEG 440
Cdd:cd15822   80 VCGGKypnSTLKDFNKQGKNNQKQ-CSNYQPKYGYWVIGLQNKSEYNAFEDSSSSDPLILTLSLTVPPCRVGVFLDYEAG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 451770402 441 IVSFFNVTNHGSLIYKFTQCRFSQPAYPYFNPWDCPAPMTLC 482
Cdd:cd15822  159 TVSFFNVTNHGFLIYKFSSCSFSQEVFPYFNPMKCPVPMTLC 200
SPRY_PRY_TRIM22 cd15824
PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger ...
 298-483 2.96e-91

PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger protein 94 (RNF94) or Stimulated trans-acting factor of 50 kDa (STAF50); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM22, also known as RING finger protein 94 (RNF94) or STAF50 (Stimulated trans-acting factor of 50 kDa). TRIM6 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM22 is an interferon-induced protein, predominantly expressed in peripheral blood leukocytes, in lymphoid tissue such as spleen and thymus, and in the ovary.TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 inhibits influenza A virus (IAV) infection by targeting the viral nucleoprotein for degradation; it represents a novel restriction factor up-regulated upon IAV infection that curtails its replicative capacity in epithelial cells. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. A large number of high-risk non-synonymous (ns)SNPs have been identified in the highly polymorphic TRIM22 gene, most of which are located in the SPRY domain and could possibly alter critical regions of the SPRY structural and functional residues, including several sites that undergo post-translational modification. TRIM22 is a direct p53 target gene and inhibits the clonogenic growth of leukemic cells. Its expression in Wilms tumors is negatively associated with disease relapse. It is greatly under-expressed in breast cancer cells as compared to non-malignant cell lines; p53 dysfunction may be one of the mechanisms for its down-regulation.


Pssm-ID: 293996 [Multi-domain]  Cd Length: 198  Bit Score: 276.34  E-value: 2.96e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 298 YWADFTFNPENLNLNLILSEDHRQVTSVPIWPFKCCNN------GILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRTL 371
Cdd:cd15824    1 YWVDVMLNPVNAVSNVVVSADQRQVTVVHICMFRNSNPcdfsafDVLGCQYFSSGKYYWEVDVSGKIAWILGVYSKRNNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 372 K--------FDVrrcSKSQPNGYHRYKPQNGYWVIGLQDGSKYSIFEDSSNCGPTVLNPFVATPLHRIGVFLDCEEGIVS 443
Cdd:cd15824   81 NkrkssgfaFDP---NVNHPNVYSRYRPQNGYWVIGLQNESEYNAFEDSSSSDPKVLTLSMAVPPHRVGVFLDYEAGTVS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 451770402 444 FFNVTNHGSLIYKFTQCRFSQPAYPYFNPWDCPAPMTLCP 483
Cdd:cd15824  158 FFNVTNHGSLIYKFSKCCFSQPVYPYFNPWNCPAPMTLCP 197
SPRY_PRY_TRIM6 cd15823
PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger ...
 298-483 5.61e-56

PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM6, also known as RING finger protein 89 (RNF89). TRIM6 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It is selectively expressed in embryonic stem (ES) cells and interacts with the proto-oncogene product Myc, maintaining the pluripotency of the ES cells. TRIM6, together with E2 Ubiquitin conjugase (UbE2K) and K48-linked poly-Ub chains, is critical for the IkappaB kinase epsilon (IKKepsilon) branch of type I interferon (IFN-I) signaling pathway and subsequent establishment of a protective antiviral response.


Pssm-ID: 293995  Cd Length: 188  Bit Score: 184.68  E-value: 5.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 298 YWADFTFNPENLNLNLILSEDHRQVTSV------PIWPFKCCNNGILGSKCFLSGKHYWEVDVSEKNAWTLGV--YSRKR 369
Cdd:cd15823    1 YWVDVTLNPHTANLNLVLSKNRRQVRFVgaklsgPSYLEEHYDCSVLGSQHFSSGKHYWEVDVTKKTAWILGVcsHSLGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 370 TLKFDVrrcSKSQPNGYHRYKPQNGYWVIGLQDGSKYSIFEDSSncgpTVLNPFVATPLHRIGVFLDCEEGIVSFFNVTN 449
Cdd:cd15823   81 TFSFNQ---YAQNHNAYSRYQPQSGYWVIGLQHNHEYRAYEDSS----TSLLLSMTVPPRRVGVFLDYEAGTVSFYNVTN 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 451770402 450 HGSLIYKFTQCRFSQPAYPYFNPWDCPAPMTL-CP 483
Cdd:cd15823  154 HGFPIYTFSKYYFPTTLCPYFNPCNCVVPMTLrRP 188
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
 301-482 3.76e-54

PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, TRIM10, TRIM11, TRIM17, TRIM20, TRIM21, TRIM27, TRIM35, TRIM38, TRIM41, TRIM50, TRIM58, TRIM60, TRIM62, TRIM69, TRIM72, NF7 and bloodthirsty; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class IV TRIM proteins, including TRIM7, TRIM35, TRIM41, TRIM50, TRIM62, TRIM69, TRIM72, TRIM protein NF7 and bloodthirsty (bty). TRIM7 interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism. TRIM41 is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. TRIM62 is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer. TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis. TRIM72 has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293968 [Multi-domain]  Cd Length: 174  Bit Score: 179.21  E-value: 3.76e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQVTSVPIWP--------FKCCNNgILGSKCFLSGKHYWEVDVSEKNAWTLGVysrkrtlk 372
Cdd:cd13733    1 DVTLDPDTAHPNLILSEDLKSVRYGDKRQnlpdnperFDTCVC-VLGSEGFSSGRHYWEVEVGGKTDWDLGV-------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 373 fdvrrCSKSQP-NGYHRYKPQNGYWVIGLQDGSKYSIFEDSsncgPTVLNpfVATPLHRIGVFLDCEEGIVSFFNVTNhG 451
Cdd:cd13733   72 -----ARESVNrKGKITLSPENGYWTVGLRNGNEYKALTSP----STPLS--LREKPQKVGVFLDYEEGQVSFYNVDD-G 139

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 451770402 452 SLIYKFTQCrFSQPAYPYFNPWD-----CPAPMTLC 482
Cdd:cd13733  140 SHIYTFTDC-FTEKLYPYFSPCLndggkNSAPLIIC 174
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
 302-482 9.83e-37

PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that form a distinct PRY domain structure such that the B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Among the TRIM proteins, also known as the N-terminal RING finger/B-box/coiled coil (RBCC) family, only Classes I and II contain the B30.2 domain that has evolved under positive selection. Class I TRIM proteins include multiple members involved in antiviral immunity at various levels of interferon signaling cascade. Among the 75 human TRIMs, roughly half enhance immune response, which they do at multiple levels in signaling pathways. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293934 [Multi-domain]  Cd Length: 168  Bit Score: 133.20  E-value: 9.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 302 FTFNPENLNLNLILSEDHRQVTSVPIWP--------FKCCNNgILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKrtlkf 373
Cdd:cd12874    1 LTFDPDTAHLNLILSDDLRSVRVGDISQhppeppprFFECWQ-VLGSQSFSSGRHYWEVDVQDDSSWYVGVTYKS----- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 374 dVRRCSKSQPNGyhrykPQNGYWVIGLQDGSkysiFEDSSNCGPTVLNPfvaTPLHRIGVFLDCEEGIVSFFNVTNHGSL 453
Cdd:cd12874   75 -LPRKGKMSNLG-----RNNGSWCLEWRENE----FSAWHNNPETRLPV---TPPRRLGVFLDCDGGSLSFYGVTDGVQL 141

                        170       180
                 ....*....|....*....|....*....
gi 451770402 454 IYKFtQCRFSQPAYPYFNPWDCpAPMTLC 482
Cdd:cd12874  142 LYTF-KAKFTEPLYPAFWLGEG-STLSIC 168
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
 300-483 1.26e-36

PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of pyrin, several tripartite motif-containing proteins (TRIMs), including E3 ubiquitin-protein ligase (TRIM21), RET finger protein (RFP)/tripartite motif protein 27 (TRIM27), as well as butyrophilin (Btns) and butyrophilin-like (Btnl) family members, with the exception of Btnl2. Btn and Btnl family members are novel regulators of immune responses, with many of the genes located within the MHC. They are implicated in T-cell inhibition and modulation of epithelial cell-T cell interactions. TRIM21 (also known as RO52, SSA1 or RNF81) is a major autoantigen in autoimmune diseases such as rheumatoid arthritis, systemic lupus erythematosus, and Sjorgen's syndrome. TRIM27 (also known as Ret finger protein, RFP or RNF76) negatively regulates CD4 T-cells by ubiquitinating and inhibiting the class II phosphatidylinositol 3 kinase C2beta (PI3K-C2beta), a kinase critical for KCa3.1 channel activation. The PRY/SPRY domain of Pyrin, which is mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing.


Pssm-ID: 293979 [Multi-domain]  Cd Length: 177  Bit Score: 133.13  E-value: 1.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 300 ADFTFNPENLNLNLILSEDHRQVT------SVPIWP--FKCCNNgILGSKCFLSGKHYWEVDVSEKNAWTLGV----YSR 367
Cdd:cd13745    3 VDVTLDPDTAHPNLVLSEDRKSVRhgdtrqDLPDNPerFDTYPC-VLGAEGFTGGRHYWEVEVGDKTEWTLGVcresVSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 368 KrtlkfdvrrcsksqpnGYHRYKPQNGYWVIGLQDGsKYSifedssncgpTVLNPFvaTPLH------RIGVFLDCEEGI 441
Cdd:cd13745   82 K----------------GEVTLSPENGYWTVWLRDG-KYE----------ALTSPP--TPLPvsvrpsRVGIFLDYEAGE 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 451770402 442 VSFFNVTNHgSLIYKFTqCRFSQPAYPYFNPWDCP-----APMTLCP 483
Cdd:cd13745  133 VSFYNVTDR-SHLFTFT-DTFSGTLRPYFYPGLNAggknaAPLIICP 177
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
 292-482 1.23e-35

PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM20, which is also known as pyrin or marenostrin. Unlike TRIM domains that are composed of RING/B-box/coiled-coil core, the N-terminal RING domain in TRIM20 is exchanged by a PYRIN domain (PYD), a prime mediator of protein interactions necessary for apoptosis, inflammation and innate immune signaling pathway, and it also harbors a C-terminal B30.2 domain. Mutations in pyrin (TRIM20) are associated with familial Mediterranean fever (FMF), a recessively hereditary periodic fever syndrome, characterized by episodes of inflammation and fever. These mutations cluster in the C-terminal B30.2 domain and therefore it is assumed that pyrin plays a role in the innate immune system by possibly effecting caspase-1-dependent IL-1beta maturation.


Pssm-ID: 293985  Cd Length: 184  Bit Score: 130.65  E-value: 1.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 292 LTAVRAYWADFTFNPENLNLNLILSEDHRQV------TSVPIWP--FKCCNNgILGSKCFLSGKHYWEVDVSEKNAWTLG 363
Cdd:cd15813    1 LRAAQAHAVNVTLDPETAHPNLIFSDDLKSVrlgnkwDRLPDNPerFDSCII-VLGSPSFTSGRHYWEVEVGDKTGWILG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 364 VYsrkrtlKFDVRRcsksqpNGYHRYKPQNGYWVIGLQDGSKYSifedSSNCGPTVLnpFVATPLHRIGVFLDCEEGIVS 443
Cdd:cd15813   80 VC------KASVSR------KGSMTLSPENGYWVVMMTKRNEYQ----ASTSPPTRL--WLREPPRRVGIFLDYEAGDIS 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 451770402 444 FFNVTNHgSLIYKFTQCRFSQPAYPYFnpwdCP---------APMTLC 482
Cdd:cd15813  142 FYNVTAK-SHIYTFTSFSSSGPLQPIF----SPgthdggknmDPLTIC 184
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
 303-483 1.75e-35

PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD Ribonucleoprotein Autoantigen (Ro52); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM21, which is also known as Sjogren Syndrome Antigen A (SSA), SSA1, 52kD Ribonucleoprotein Autoantigen (Ro52, Ro/SSA, SS-A/Ro) or RING finger protein 81 (RNF81). TRIM21 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. As an E3 ligase, TRIM21 mediates target specificity in ubiquitination; it regulates type 1 interferon and proinflammatory cytokines via ubiquitination of interferon regulatory factors (IRFs). It is up-regulated at the site of autoimmune inflammation, such as cutaneous lupus lesions, indicating a central role in the tissue destructive inflammatory process. It interacts with auto-antigens in patients with Sjogren syndrome and systemic lupus erythematosus, a chronic systemic autoimmune disease characterized by the presence of autoantibodies against the protein component of the human intracellular ribonucleoprotein-RNA complexes and more specifically TRIM21, Ro60/TROVE2 and La/SSB proteins. It binds the Fc part of IgG molecules via its PRY-SPRY domain with unexpectedly high affinity.


Pssm-ID: 293957  Cd Length: 180  Bit Score: 130.39  E-value: 1.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 303 TFNPENLNLNLILSEDHRQVtSVPIWPFKCCNNG--------ILGSKCFLSGKHYWEVDVSEKNAWTLGVysrkrtLKFD 374
Cdd:cd12900    6 TLDPDTANPWLILSKDRRQV-RLGDTHQNVPENEerfdnypmVLGAQRFNSGKHYWEVDVTGKEAWDLGV------CRDS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 375 VRRcsksqpNGYHRYKPQNGYWVIGLQDGsKYsifeDSSNCGPTVLNpfVATPLHRIGVFLDCEEGIVSFFNVTNHGSLI 454
Cdd:cd12900   79 VRR------KGQFLLSPENGFWTIWLWNK-KY----EAGTSPQTTLH--LQVPPCQVGIFLDYEAGVVSFYNITDHGSLI 145

                        170       180       190
                 ....*....|....*....|....*....|....
gi 451770402 455 YKFTQCRFSQPAYPYFNP-----WDCPAPMTLCP 483
Cdd:cd12900  146 YTFSECAFTGPLRPFFNPgfndsGGNAAPLTLCP 179
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
 300-483 1.30e-33

PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like 3 (BTNL3); BTN3A also known as CD277; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 3A (BTN3A); duplication events have led to three paralogs in primates: BTN3A1, BTN3A2, and BTN3A3. BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN3 transcripts are ubiquitously present in all immune cells (T cells, B cells, NK cells, monocytes, dendritic cells, and hematopoietic precursors) with different expression levels; BTN3A1 and BTN3A2 are expressed mainly by CD4+ and CD8+ T cells, BTN3A2 is the major form expressed in NK cells, and BTN3A3 is poorly expressed in these immune cells. The PRY/SPRY domain of the BTN3A1 isoform mediates phosphoantigen (pAg)-induced activation by binding directly to the pAg.


Pssm-ID: 293992 [Multi-domain]  Cd Length: 176  Bit Score: 124.85  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 300 ADFTFNPENLNLNLILSEDHRQVT------SVPIWPFKC-CNNGILGSKCFLSGKHYWEVDVSEKNAWTLGVysrkrtlk 372
Cdd:cd15820    4 ADVILDPDTANPILLISEDQRSLQwadepqNLPDNPKRFdWHYCVLGCKSFTSGRHFWEVEVGDRKEWYVGV-------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 373 fdvrrCSKS-QPNGYHRYKPQNGYWVIGLQDGSKYSIFEDSSNcgptvlNPFVATPLHRIGVFLDCEEGIVSFFNVTNhG 451
Cdd:cd15820   76 -----CRENvERKLWVKMAPENGFWTIGLSDGNDYQALTDPRT------KLTIANPPQRVGVFLDYETGEVSFYNAMD-G 143

                        170       180       190
                 ....*....|....*....|....*....|....
gi 451770402 452 SLIYKFTQCRFSQPAYPYFN--PWDcPAPMTLCP 483
Cdd:cd15820  144 SHIYTFPHTSFSGPLYPVFRllSWD-PTALTICP 176
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
 300-482 9.81e-33

zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69 and TRIM proteins NF7 and bloodthirsty (bty). TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis.


Pssm-ID: 293962 [Multi-domain]  Cd Length: 178  Bit Score: 122.52  E-value: 9.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 300 ADFTFNPENLNLNLILSEDHRQVT------SVPIWP--FKCCNNgILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRTL 371
Cdd:cd12905    4 APLTFDPETAHPSLILSRDLTAVTesdemqPYPRSPkrFLQCVN-VLASQGFQSGRHYWEVWVGSKTKWDLGVASESVDR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 372 KFDVRRCsksqpngyhrykPQNGYWVIGLQDGSKYsifedSSNCGP-TVLNPfvATPLHRIGVFLDCEEGIVSFFNVTNH 450
Cdd:cd12905   83 QARVKLC------------PENGYWTLRLRNGDEY-----WAGTQPwTRLRV--TSRPQRIGVFLDCEERKVSFYNADDM 143

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 451770402 451 gSLIYKFTQCRFSQpAYPYFNPwdC-------PAPMTLC 482
Cdd:cd12905  144 -SLLYSFHQGPRGK-VFPFFST--CfsddgqnAEPMRLL 178
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
 300-482 1.39e-32

butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 1A and 2A (BTN1A and BTN2A). BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN1A plays a role in the secretion, formation and stabilization of milk fat globules. The B30.2 domain of BTN1A1 binds the enzyme xanthine oxidoreductase (XOR) in order to participate in milk fat globule secretion; this interaction may lead to the production of reactive oxygen species, which have immunomodulatory and antimicrobial functions. Duplication events have led to three paralogs of BTN2A in primates: BTN2A1, BTN2A2, and BTN2A3. In humans, only BTN2A1 has been functionally characterized; it has been detected on epithelial cells and leukocytes, and identified as a novel ligand of dendritic cell-specific ICAM-3 grabbing nonintegrin (DCSIGN), a C-type lectin receptor that acts as an internalization receptor for HIV-1, HCV, and other pathogens. BTN2A2 mRNA has been shown to be expressed in circulating human immune cells.


Pssm-ID: 293991 [Multi-domain]  Cd Length: 172  Bit Score: 121.95  E-value: 1.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 300 ADFTFNPENLNLNLILSEDHRQVTsvpiWPFKC-----------CNNGILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRk 368
Cdd:cd15819    2 VNVTLDPDTAHPALILSEDGRSVT----WGETRqdlpenperfdSLPCVLGQEGFTSGRHYWEVEVGDRTSWDLGVCRD- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 369 rtlkfDVRRcsksqpNGYHRYKPQNGYWVIGLqDGSKYSIFEDSsncgPTVLnpFVATPLHRIGVFLDCEEGIVSFFNVT 448
Cdd:cd15819   77 -----NVMR------KGRVTLSPENGFWAIRL-YGNEYWALTSP----ETPL--TLKEPPRRVGIFLDYEAGDVSFYNMT 138

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 451770402 449 NhGSLIYKFTQCRFSQPAYPYFNPWDC-PAPMTLC 482
Cdd:cd15819  139 D-GSHIYTFPQTAFSGPLRPFFRLWSSdSGPLTIC 172
SPRY_PRY_RFPL cd15821
Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the ...
 301-482 2.88e-32

Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of RFPL protein family, which includes RFPL1, RFPL2, RFPL3 and RFPL4. In humans, RFPL transcripts can be detected at the onset of neurogenesis in differentiating human embryonic stem cells, and in the developing human neocortex. The human RFPL1, 2, 3 genes have a role in neocortex development. RFPL1 is a primate-specific target gene of Pax6, a key transcription factor for pancreas, eye and neocortex development; human RFPL1 decreases cell number through its RFPL-defining motif (RDM) and SPRY domains. The RFPL4 (also known as RFPL4A) gene encodes a putative E3 ubiquitin-protein ligase expressed in adult germ cells and interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway.


Pssm-ID: 293993 [Multi-domain]  Cd Length: 178  Bit Score: 121.26  E-value: 2.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQVTSVPI----------WPFKCCnngILGSKCFLSGKHYWEVDVSEKNAWTLGVysrkrt 370
Cdd:cd15821    5 DMTLDVDTANNYLIISEDLRSVRCGCFrqnrkelaerFDDALC---VLGSPRFTSGRHYWEVDVGTSTEWDLGV------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 371 lkfdvrrCSKSQP-NGYHRYKPQNGYWVIGLQDGSKYSifedSSNCGPTVLnpFVATPLHRIGVFLDCEEGIVSFFNVTN 449
Cdd:cd15821   76 -------CRESVNrQGPIELSPEHGFWTVSLRDGSVFF----ASTVPLTVL--WVNPRLHRVGIFLDMEMGTISFYDVSD 142

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 451770402 450 hGSLIYKFTQCRFSQPAYPYFNPWDCP----APMTLC 482
Cdd:cd15821  143 -GSHIFTFTKISAEEPLRPFFAPANPYgddqGVLSIC 178
SPRY_PRY_TRIM38 cd15815
PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger ...
 293-470 1.02e-29

PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger protein 15 (RNF15); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM38, which is also known as RING finger protein 15 (RNF15) or RORET. TRIM38 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM38 has been shown to act as a suppressor in TOLL-like receptor (TLR)-mediated interferon (IFN)-beta induction by promoting degradation of TRAF6 and NAP1 through the ubiquitin-proteasome system. Another study has shown that TRIM38 may act as a novel negative regulator for TLR3-mediated IFN-beta signaling by targeting TRIF for degradation. TRIM38 has been identified as a critical negative regulator in TNFalpha- and IL-1beta-triggered activation of NF-kappaB and MAP Kinases (MAPKs); it causes degradation of two essential cellular components, TGFbeta-associated kinase 1 (TAK1)-associating chaperones 2 and 3 (TAB2/3). The degradation is promoted through a lysosomal-dependent pathway, which requires the C-terminal PRY-SPRY of TRIM38. Enterovirus 71 infection induces degradation of TRIM38, suggesting that TRIM38 may play a role in viral infections.


Pssm-ID: 293987 [Multi-domain]  Cd Length: 182  Bit Score: 114.37  E-value: 1.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 293 TAVRAYWADFTFNPENLNLNLILSEDHRQVTsvpiwpFKCCNNG-------------ILGSKCFLSGKHYWEVDVSEKNA 359
Cdd:cd15815    6 KMLRRHQVSVTLDPDTAHPELTLSKDQRQVT------YGRCQENldaspkrftvlpcVLGCEGFTSGRHYFEVDVGEGTG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 360 WTLGVysrkrtlkfdvrrCSKSQPNGYHRYK-PQNGYWVIGLQDGSKYSIFedssNCGPTVLnPFVATPLhRIGVFLDCE 438
Cdd:cd15815   80 WDVGV-------------CLENVQRGFGMKQePEFGFWTIRLCEEDGYVAL----TSPPTPL-PLREKPL-VVGVFLDYE 140

                        170       180       190
                 ....*....|....*....|....*....|..
gi 451770402 439 EGIVSFFNVTNhGSLIYKFTQCRFSQPAYPYF 470
Cdd:cd15815  141 AGLVSFYNMTT-GSHIFTFPKASFSDTLRPYF 171
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
 302-483 1.02e-29

PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is found at the C-terminus of the overall domain architecture of tripartite motif 35, TRIM35 (also known as hemopoietic lineage switch protein), which includes a RING finger domain (RING) and a B-box motif (BBOX). TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism.


Pssm-ID: 293950 [Multi-domain]  Cd Length: 171  Bit Score: 114.27  E-value: 1.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 302 FTFNPENLNLNLILSEDhrqVTSV------PIWP-----FKCCNnGILGSKCFLSGKHYWEVDVSEKNAWTLGV--YSRK 368
Cdd:cd12893    2 VTLDPNTAHPWLSLSED---LTSVryssekQQLPdnperFDPYP-CVLGSEGFTSGKHSWDVEVGDNTSWMLGVakESVQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 369 RTLKFDVRrcsksqpngyhrykPQNGYWVIGLQDGsKYSifEDSSNCGPTVLNpfVATPLHRIGVFLDCEEGIVSFFNVT 448
Cdd:cd12893   78 RKGKFTLS--------------PESGFWTIGFSEG-KYS--ARTSPEPRTPLR--VKQKPQRIRVQLDWDRGKVSFSDPD 138

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 451770402 449 NHgSLIYKFTQcRFSQPAYPYFNPWDCPAPMTLCP 483
Cdd:cd12893  139 TN-THIHTFTH-TFTERVFPYFYTGCKSEPLRILP 171
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
 278-482 7.52e-29

PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM75, also known as Gm794. TRIM75 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM75 has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized.


Pssm-ID: 294001  Cd Length: 187  Bit Score: 112.38  E-value: 7.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 278 QAPDLSGMLQKFREltavraywaDFTFNPENLNLNLILSEDHRQVT------SVPIWP--FKCcNNGILGSKCFLSGKHY 349
Cdd:cd15829    6 QYSALQKIIKKFRV---------DVTLDPETAHPNLLVSEDKKCVTftkkkqRVPDSPkrFTV-NPVVLGFPGFHSGRHF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 350 WEVDVSEKNAWTLGVysrkrtlkfdvrrCSKSQPNGYHRY-KPQNGYWVIGLQDGSkYsifeDSSNCGPTVLnPFVATPl 428
Cdd:cd15829   76 WEVEVGDKPEWAVGV-------------CKDSLSTKARRPpSGQQGCWRIQLQGGD-Y----DAPGAVPPPL-LLEVKP- 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 451770402 429 HRIGVFLDCEEGIVSFFNVTNhGSLIYKFTQcRFSQPAYPYFNPWDCPAPMTLC 482
Cdd:cd15829  136 RGIGVFLDYELGEISFYNMPE-KSHIHTFTD-TFSGPLRPYFYVGPDSKPLRIC 187
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
 301-482 3.85e-27

PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger protein 92 (RNF92); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM11, also known as RING finger protein 92 (RNF92) or BIA1. TRIM11 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It localizes to the nucleus and the cytoplasm; it is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 increases expression of dopamine beta-hydroxylase gene by interacting with the homeodomain transcription factor, PHOX2B, via the B30.2/SPRY domain, thus playing a potential role in the specification of noradrenergic (NA) neuron phenotype. It has also been shown that TRIM11 plays a critical role in the clearance of mutant PHOX2B, which causes congenital central hypoventilation syndrome, via the proteasome. TRIM11 binds a key component of the activator-mediated cofactor complex (ARC105), and destabilizes it, through the ubiquitin-proteasome system; ARC105 mediates chromatin-directed transcription activation and is a key regulatory factor for transforming growth factor beta (TGFbeta) signaling.


Pssm-ID: 293983 [Multi-domain]  Cd Length: 169  Bit Score: 106.97  E-value: 3.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQV------TSVPIWPFK-----CcnngILGSKCFLSGKHYWEVDVSEKNAWTLGVysrkr 369
Cdd:cd15811    1 DVTLDPDTANPELVLSEDRRSVrrgdlrQALPDSPERfdpgpC----VLGRERFTSGRHYWEVEVGDRTSWALGV----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 370 tLKFDVRRCSKSQpngyhrYKPQNGYWVIglqdgskysIFEDSSNCGPTVLNPFVATPLHRIGVFLDCEEGIVSFFNVTN 449
Cdd:cd15811   72 -CKENVNRKEKGE------LSAGNGFWIL---------VFLGNYYSSERRTFAPLRDPPRRVGIFLDYEAGHLSFYSATD 135

                        170       180       190
                 ....*....|....*....|....*....|....
gi 451770402 450 hGSLIYKFTQCRFSQPAYPYFNPWDC-PAPMTLC 482
Cdd:cd15811  136 -GSLLFIFPETPFSGTLRPLFSPLSSsPTPMTIC 168
SPRY_PRY_TRIM27 cd15814
PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger ...
 301-483 9.89e-27

PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger protein 76 (RNF76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM27, also known as RING finger protein 76 (RNF76) or RET finger protein (RFP). TRIM27 domain is composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in the spleen, thymus and in cells of the hematopoietic compartment. TRIM27 exhibits either nuclear or cytosolic localization depending on the cell type. TRIM27 negatively regulates nucleotide-binding oligomerization domain containing 2 (NOD2)-mediated signaling by proteasomal degradation of NOD2, suggesting that TRIM27 could be a new target for therapeutic intervention in NOD2-associated diseases such as Crohn's. High expression of TRIM27 is observed in several human cancers, including breast and endometrial cancer, where elevated TRIM27 expression predicts poor prognosis. Also, TRIM27 forms an oncogenic fusion protein with Ret proto-oncogene. It is involved in different stages of spermatogenesis and its significant expression in male germ cells and seminomas, suggests that TRIM27 may be associated with the regulation of testicular germ cell proliferation and histological-type of germ cell tumors. TRIM27 could also be a predictive marker for chemoresistance in ovarian cancer patients. In the neurotoxin model of Parkinson's disease (PD), deficiency of TRIM27 decreases apoptosis and protects dopaminergic neurons, making TRIM27 an effective potential target during the treatment of PD.


Pssm-ID: 293986 [Multi-domain]  Cd Length: 177  Bit Score: 106.31  E-value: 9.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQV------TSVPIWP-----FKCcnngILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKR 369
Cdd:cd15814    3 DVTLDPDTAYPSLILSDNLRQVrysylqQDLPDNPerfnlFPC----VLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 370 TLKFDVRRCsksqpngyhrykPQNGYWVIGLQDGSKYSIFEDSSNCGPtvlnpfVATPLHRIGVFLDCEEGIVSFFNVTN 449
Cdd:cd15814   79 CRKGGVTSA------------PQNGFWAVSLWYGKEYWALTSPMTALP------LRTPLQRVGIFLDYDAGEVSFYNVTE 140

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 451770402 450 HGSlIYKFTQCRFSQPAYPYF----NPWDCPAPMTLCP 483
Cdd:cd15814  141 RCH-TFTFSHATFCGPVRPYFslsySGGKSAAPLIICP 177
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
 303-472 2.13e-26

PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger protein 36 (RNF36); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69, which is also known as RING finger protein 36 (RNF36) or testis-specific ring finger (Trif). TRIM69 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. The mouse ortholog of this gene is specifically expressed in germ cells at the round spermatid stages during spermatogenesis and, when overexpressed, induces apoptosis. TRIM69 has been shown to be a novel regulator of mitotic spindle assembly in tumor cells; it associates with spindle poles and promotes centrosomal clustering, and is therefore essential for formation of a bipolar spindle.


Pssm-ID: 293990 [Multi-domain]  Cd Length: 187  Bit Score: 105.66  E-value: 2.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 303 TFNPENLNLNLILSEDHRQV------TSVPIWP--FKCCNnGILGSKCFLSGKHYWEVDVSEKNAWTLGVysrkrtLKFD 374
Cdd:cd15818   16 TLDPKTAHPNLILSEDLTCVwhgdtkQMLPDNPerFDSSV-AVLGSEGFTSGKHYWEVEVAKKTKWTLGV------VRES 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 375 VRRcsksqpNGYHRYKPQNGYWVIGLQDGSKYSIFEDSSNCgpTVLNpfvaTPLHRIGVFLDCEEGIVSFFNVtNHGSLI 454
Cdd:cd15818   89 INR------KGNCPLSPEDGFWLLRLRNQNELKALDVPSFS--LTLT----SNLNKVGIYLDYEGGQVSFYNA-NTMSHI 155

                        170
                 ....*....|....*...
gi 451770402 455 YKFTqCRFSQPAYPYFNP 472
Cdd:cd15818  156 YTFS-DTFTEKIYPYFCP 172
SPRY_PRY_TRIM58 cd15816
PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This ...
 301-481 3.17e-26

PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM58, also known as BIA2. TRIM58 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins.It is implicated by genome-wide association studies (GWAS) to regulate erythrocyte traits, including cell size and number. Trim58 facilitates erythroblast enucleation by inducing proteolytic degradation of the microtubule motor dynein.


Pssm-ID: 293988 [Multi-domain]  Cd Length: 168  Bit Score: 104.49  E-value: 3.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQV------TSVP-------IWPfkcCnngILGSKCFLSGKHYWEVDVSEKNAWTLGVysr 367
Cdd:cd15816    1 DVKLDPATAHPSLLLTADLRSVqdgelwRDVPgnperfdTWP---C---VLGLQSFSSGRHYWEVAVGEKAEWGLGV--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 368 krtlkfdvrrCSKSQP-NGYHRYKPQNGYWVIGLQDGSKYSIFedssnCGPTVlnPFVAT--PlHRIGVFLDCEEGIVSF 444
Cdd:cd15816   72 ----------CQDSAPrKGETTPSPENGVWAVWLLKGNEYMVL-----ASPSV--PLLQLrrP-RRVGVFLDYEAGEISF 133

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 451770402 445 FNVTnHGSLIYKFTQCrFSQPAYPYFNPWDcPAPMTL 481
Cdd:cd15816  134 YNVT-AGSHIYTFRQL-FSGILRPYFFVCD-TTPLTL 167
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
 301-483 8.81e-26

PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger protein 33 (RNF33); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60, which is also known as RING finger protein 33 (RNF33) or 129 (RNF129). TRIM60 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites.


Pssm-ID: 294000 [Multi-domain]  Cd Length: 180  Bit Score: 103.52  E-value: 8.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQVTSVPIWPFKCCNN-------GILGSKCFLSGKHYWEVDVSEKNAWTLGV----YSRKR 369
Cdd:cd15828   11 DVTLDPETAHPQLTVSEDRKSVLYGEMKQNVCYNPrrfylcpAVLGSEGFHSGRQYWEVEVGDKPEWTLGVcqdcLPRNW 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 370 tlkfdvrrcsKSQPNgyhrykPQNGYWVIGLQDGSKYSIfedssnCGP--TVLNPfVATPlHRIGVFLDCEEGIVSFFNV 447
Cdd:cd15828   91 ----------SNQPS------VQDGLWAIGRYSESNYVA------LGPkkIQLLP-KVRP-SKIGIFLDYELGEVSFYNM 146

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 451770402 448 tNHGSLIYKFTQCrFSQPAYPYFNPWDCPAPMTLCP 483
Cdd:cd15828  147 -NDRSLLYTFSDS-FTGTLWPYFYTGTDSEPLKICT 180
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
 7-78 4.66e-25

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong 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. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


Pssm-ID: 438253 [Multi-domain]  Cd Length: 72  Bit Score: 97.90  E-value: 4.66e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 451770402   7 TDVQKEATCPVCHVLLIKPLNLGSGHHVSQACLTVKKTAVTNPRGKSLCPMCGNRFSFENLQANKHLADVVE 78
Cdd:cd16591    1 VNIKEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESVNQEGESSCPVCRTSYQPENLRPNRHLANIVE 72
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
 301-482 7.64e-25

PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60 and TRIM75, both composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM60 domain is also known as RING finger protein 33 (RNF33) or 129 (RNF129). Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites. TRIM75, also known as Gm794, has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized.


Pssm-ID: 293989 [Multi-domain]  Cd Length: 168  Bit Score: 100.70  E-value: 7.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQVTSVPIWPfKCCNN--------GILGSKCFLSGKHYWEVDVSEKNAWTLGVysrkrtlk 372
Cdd:cd15817    1 DLILDPETAHPNLIVSEDRKAVRYRRMKP-NCPYDprrftvypAVLGSEGFDSGRHFWEVEVGGKGEWILGV-------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 373 fdvrrCSKSQPNGYHRY-KPQNGYWVIGLQDgSKYsifedsSNCGPTVLNPFVATPLHRIGVFLDCEEGIVSFFNVTNHg 451
Cdd:cd15817   72 -----CKDSLPRNAQDPpSPLGGCWQIGRYM-SGY------VASGPKTTQLLPVVKPSRIGIFLDYELGEVSFYNMNDR- 138

                        170       180       190
                 ....*....|....*....|....*....|.
gi 451770402 452 SLIYKFTQCrFSQPAYPYFNPWDCPAPMTLC 482
Cdd:cd15817  139 SHLYTFTDT-FTGKLIPYFYVGPDSEPLTIC 168
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
 303-474 1.80e-24

PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, TRIM16-like, TRIM25-like, TRIM47-like, TRIM65 and RNF135, and stonustoxin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM14, TRIM16 and TRIM25, TRIM47 as well as RING finger protein RNF135 and stonustoxin, a secreted poisonous protein of the stonefish Synanceja horrida. TRIM16 (also known as estrogen-responsive B box protein or EBBP) has E3 ubiquitin ligase activity. It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function. TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100), is highly expressed in kidney tubular cells, but low expressed in most tissue. It is overexpressed in astrocytoma tumor cells and plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. RNF135 ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Stonustoxin (STNX) is a hypotensive and lethal protein factor that also possesses other biological activities such as species-specific hemolysis (due to its ability to form pores in the cell membrane) and platelet aggregation, edema-induction, and endothelium-dependent vasorelaxation (mediated by the nitric oxide pathway and activation of potassium channels). The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293949 [Multi-domain]  Cd Length: 167  Bit Score: 99.63  E-value: 1.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 303 TFNPENLNLNLILSEDHRQVTSVPIW------PFKCCNNGILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRkrtlkfDVR 376
Cdd:cd12891    2 TLDPNTAHNNLALSGDLKTVTCSSENqhypdsPERFTHSQVLSTQSFSSGRHYWEVEVSESGGWSVGVAYP------SIE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 377 RCSksqPNGYHRYKPQNgyWviGLQ-DGSKYSIFEDSSncgPTVLNPfvaTPLHRIGVFLDCEEGIVSFFNVTNHGSLIY 455
Cdd:cd12891   76 RKG---DESRIGRNDKS--W--CLEwQDKSFSAWHNNE---ETPLPS---VSSRRLGVYLDYEAGRLSFYELSDPIRHLH 142

                        170
                 ....*....|....*....
gi 451770402 456 KFTqCRFSQPAYPYFNPWD 474
Cdd:cd12891  143 TFT-ATFTEPLHPAFWVLE 160
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 345-483 1.32e-22

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 92.74  E-value: 1.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   345 SGKHYWEVDVSEKNAWTLGVysrkrtlkfdvrrCSKSQPNGYHRYKPQN-GYWVIGLQDGSKYSifedssNCGPTVLNPF 423
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGV-------------ATKSVPRGYFALLGEDkGSWGYDGDGGKKYH------NSTGPEYGLP 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 451770402   424 VATPLHRIGVFLDCEEGIVSFFNVTNHgSLIYKFTQCRFSQPAYPYFNPWD-CPAPMTLCP 483
Cdd:smart00449  62 LQEPGDVIGCFLDLEAGTISFYKNGKY-LHGLAFFDVKFSGPLYPAFSLGSgNSVRLNFGP 121
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
 303-482 1.42e-22

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, TRIM15, TRIM26, TRIM39, TRIM41; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several tripartite motif-containing (TRIM) proteins, including TRIM7 (also referred to as glycogenin-interacting protein, RING finger protein 90 or RNF90), TRIM10, TRIM15, TRIM26, TRIM39 and TRIM41. TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM10 (also known as hematopoietic RING finger 1 (HERF1) or TRIM10/HERF1) plays a key role in definitive erythroid development; downregulation of the Spi-1/PU.1 oncogene induces the expression of TRIM10/HERF1, a key factor required for terminal erythroid cell differentiation and survival. Antiviral activity of TRIM15 is dependent on the ability of its B-box to interact with the MLV Gag precursor protein; downregulation of TRIM15, along with TRIM11, enhances virus release suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. Tripartite motif-containing 26 (TRIM26) function is as yet unknown; however, since it is localized in the human histocompatibility complex (MHC) class I region, TRIM26 may play a role in immune response although studies show no association between TRIM26 polymorphisms and the risk of aspirin-exacerbated respiratory disease. TRIM39 is a MOAP-1 (Modulator of Apoptosis)-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.


Pssm-ID: 293946 [Multi-domain]  Cd Length: 169  Bit Score: 94.16  E-value: 1.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 303 TFNPENLNLNLILSEDHRQVT------SVPIWP----FKCCnngILGSKCFLSGKHYWEVDVSEKNAWTLGVySRKrtlk 372
Cdd:cd12888    3 TLDPDTAHPRLVLSEDRKSVRwgdtrqDLPDNPerfdTWPC---VLGCEGFTSGRHYWEVEVGDGGGWAVGV-ARE---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 373 fDVRRcsksqpNGYHRYKPQNGYWVIGlQDGSKYSifedssncgpTVLNPFVATPLH----RIGVFLDCEEGIVSFFNVT 448
Cdd:cd12888   75 -SVRR------KGEISFSPEEGIWAVG-QWGGQYW----------ALTSPETPLPLSevprRIRVYLDYEGGQVAFFDAD 136

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 451770402 449 NhGSLIYKFTQCRFS-QPAYPYFnpWDCP-APMTLC 482
Cdd:cd12888  137 N-EAPIFTFPPASFAgERIFPWF--WVGKgSQLKLC 169
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
 332-471 6.38e-22

PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM50. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. It is specifically expressed in gastric parietal cells and may play an essential role in tubulovesicular dynamics. It also interacts with and increases the level of p62, a multifunctional adaptor protein that is implicated in various cellular processes such as the autophagy clearance of polyubiquitinated protein aggregates.


Pssm-ID: 293977  Cd Length: 189  Bit Score: 92.94  E-value: 6.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 332 CCNNGILGSKCFLSGKHYWEVDVSEKNAWTLGVY----SRKRTLkfdvrrcSKSqpngyhrykPQNGYWVIGLQDGSKYS 407
Cdd:cd13743   51 DYSNCVLASRGFSSGKHYWEVVVGSKSKWRLGLIkgttSRKGKL-------NKS---------PENGVWLIGLKEGRVYE 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 451770402 408 IFEDssncgPTVLNPfVATPLHRIGVFLDCEEGIVSFFNVTNHGSL--IYKFtQCRFSQPAYPYFN 471
Cdd:cd13743  115 AFAN-----PRVPLP-LSTRPQRIGVFLDYEKGELTFYNADSPDELvpIYTF-QAEFQGKLYPLLD 173
Bbox2_TRIM5-like cd19761
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, ...
 94-131 8.14e-20

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34, TRIM38 and similar proteins; The family includes TRIM5, TRIM6, TRIM22, TRIM34, and TRIM38, all of which belong 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 RING finger, 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. TRIM5, also termed RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also termed RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also termed 50 kDa-stimulated trans-acting factor (Staf-50), or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also termed interferon-responsive finger protein 1, or RING finger protein 21 (RNF21), may function as an antiviral protein that contributes to the defense against retroviral infections. TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates tumor necrosis factor alpha (TNF-alpha) and interleukin-1beta-triggered nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome.


Pssm-ID: 380819 [Multi-domain]  Cd Length: 40  Bit Score: 82.54  E-value: 8.14e-20
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 451770402  94 DLCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFL 131
Cdd:cd19761    1 DHCEHHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFL 38
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
 301-472 1.52e-19

PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM72. Muscle-specific TRIM72 (also known as Mitsugumin 53 or MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM72 interacts with dysferlin, a sarcolemmal protein whose deficiency causes Miyoshi myopathy (MM) and limb girdle muscular dystrophy type 2B (LGMD2B); this coordination plays an important role in the repair of sarcolemma damage.


Pssm-ID: 293976 [Multi-domain]  Cd Length: 192  Bit Score: 86.45  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQVTSV----PIWP-----FKCCNnGILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRTL 371
Cdd:cd13742   13 NLTFDPDTAHPYLVVSSDGKRVECAdqkqAVSSddpnrFDKAN-CVVSHQSFSEGEHYWEVIVGDKPRWALGVISAEAGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 372 KfdvrrcsksqpnGYHRYKPQNGYWVIGLQDGSKYSIFEDSSNcgPTVLNPfVATPlHRIGVFLDCEEGIVSFFNVTNHG 451
Cdd:cd13742   92 K------------GRLHALPSNGFWLLGCKEGKVYEAHVEHKE--PRALRV-EGRP-TRIGVYLSFSDGVLSFYDASDED 155

                        170       180
                 ....*....|....*....|..
gi 451770402 452 SLIYKFT-QCRFSQPAYPYFNP 472
Cdd:cd13742  156 NLVQLFAfHERFPGPLYPFFDV 177
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
 300-471 2.50e-19

PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several TRIM proteins, including TRIM72 and TRIM50. TRIM72 (also known as MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23.


Pssm-ID: 293954  Cd Length: 191  Bit Score: 85.74  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 300 ADFTFNPENLNLNLILSEDHRQV------TSVPIWPFKC-CNNGILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRTLK 372
Cdd:cd12897   12 ESLTFDPATAHPLLVVSSGGTVVecglqkQRRASQPERFdKSTCVVASQGFSEGEHYWEVVVGDKPRWALGVIKGTASRK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 373 fdvrrcsksqpnGYHRYKPQNGYWVIGLQDGSKYSIFEDSSNcgPTVLNpfVATPLHRIGVFLDCEEGIVSFFNVTNHGS 452
Cdd:cd12897   92 ------------GKLHASPSHGVWLIGLKEGKVYEAHGEPKE--PRPLR--VAGRPHRIGVYLSFEDGVLSFFDASDPDD 155

                        170       180
                 ....*....|....*....|
gi 451770402 453 LIYKFT-QCRFSQPAYPYFN 471
Cdd:cd12897  156 LRTLYTfQERFQGKLYPFFD 175
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
 302-474 2.67e-19

PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67, TRIM76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67 and TRIM76. TRIM1 (also known as MID2) and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. Their coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in TRIM18 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects. TRIM9 is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. Its immunoreactivity is severely decreased in affected brain areas in Parkinson's disease and dementia with Lewy bodies, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM36 interacts with centromere protein-H, one of the kinetochore proteins and possibly associates with chromosome segregation; an excess of TRIM36 may cause chromosomal instability. TRIM46 has not yet been characterized. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It is possibly involved in protein kinase A signaling as well as vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293969 [Multi-domain]  Cd Length: 166  Bit Score: 85.03  E-value: 2.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 302 FTFNPENLNLNLILSEDHRQVTS---------VPIWPFKCCNNGILGSKCFLSGKHYWEVDVSEKNAWTLGVySRKRTLK 372
Cdd:cd13734    1 FKLDPKTAHRKLRLSNDNLTVEYdpegskdqaAVLPRRFTGSPAVLGDVAISSGRHYWEVSVSRSTSYRVGV-AYKSAPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 373 F-DVRRCSKSqpngyhrykpqngyWVIgLQDGSKYSIFEDSSNCGPTVLnpfvaTPLHRIGVFLDCEEGIVSFFNVtNHG 451
Cdd:cd13734   80 DeDLGKNSTS--------------WCL-SRDNNRYTARHDGKVVDLRVT-----GHPARIGVLLDYDNGTLSFYDA-ESK 138

                        170       180
                 ....*....|....*....|...
gi 451770402 452 SLIYKFTqCRFSQPAYPYFNPWD 474
Cdd:cd13734  139 QHLYTFH-VDFEGPVCPAFAVWN 160
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 347-470 5.38e-19

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 82.78  E-value: 5.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402  347 KHYWEVDVS--EKNAWTLGVysrkrtlkfdvrrCSKSQPNGYHRYK-PQNGYWVIGLQDGSKYSifedssNCGPTVLNPF 423
Cdd:pfam00622   1 RHYFEVEIFgqDGGGWRVGW-------------ATKSVPRKGERFLgDESGSWGYDGWTGKKYW------ASTSPLTGLP 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 451770402  424 VATPLHRIGVFLDCEEGIVSFFNvtNHGSLIYKFTQCRFSQPAYPYF 470
Cdd:pfam00622  62 LFEPGDVIGCFLDYEAGTISFTK--NGKSLGYAFRDVPFAGPLFPAV 106
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
 300-472 1.11e-17

PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM62. It is also called DEAR1 ductal epithelium (associated RING chromosome 1) and is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer and thus, making TRIM62 a predictive biomarker. Non-small cell lung cancer lesions show a step-wise loss of TRIM62 levels during disease progression, indicating that it may play a role in the evolution of lung cancer. Decreased levels of TRIM62 also represent an independent adverse prognostic factor in AML.


Pssm-ID: 293978  Cd Length: 188  Bit Score: 80.82  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 300 ADFTFNPENLNLNLILSEDHRQVTSVPIWPFKCCNN--------GILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRTL 371
Cdd:cd13744   12 AALTLDPVTAHQRLILSDDCTIVAYGNLHPQPLQDSpkrfdvevSVLGSEGFSGGVHYWEVVVSEKTQWMIGLAHEAVSR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 372 KfdvrrcsksqpnGYHRYKPQNGYWVIGLQDGSKYSIFEDSSncgpTVLNpfVATPLHRIGVFLDCEEGIVSFFNVTNHg 451
Cdd:cd13744   92 K------------GSIQIQPGRGFYCIVMHDGNQYSACTEPW----TRLN--VKSKLEKVGVYLDYDKGLLIFYNADDM- 152

                        170       180
                 ....*....|....*....|.
gi 451770402 452 SLIYKFTQcRFSQPAYPYFNP 472
Cdd:cd13744  153 SWLYTFRE-KFPGKLCSYFSP 172
SPRY_PRY_TRIM17 cd15812
PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING ...
 338-470 5.15e-17

PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING finger protein (terf); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (terf). TRIM17 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein, expressed almost exclusively in the testis. It exhibits E3 ligase activity, causing protein degradation of ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates proliferation of breast cancer cells. TRIM17 undergoes ubiquitination in COS7 fibroblast-like cells but is inhibited and stabilized by TRIM44.


Pssm-ID: 293984 [Multi-domain]  Cd Length: 176  Bit Score: 78.77  E-value: 5.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 338 LGSKCFLSGKHYWEV--DVSEKNAWTLGV----YSRKRtlkfdvrRCSKSqpngyhrykPQNGYWVIGLQDGSKY-SIFE 410
Cdd:cd15812   45 VGQETFSSGRHYWEVgmNLTGDALWALGVcrdnVSRKD-------RVPKS---------PENGFWVVQLSKGKKYlSAMS 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 411 DSSNCgpTVLNPfvatPLHrIGVFLDCEEGIVSFFNVTNhGSLIYKFTQCRFSQPAYPYF 470
Cdd:cd15812  109 ALTPV--TLTEP----PSH-MGIFLDFEAGEVSFYSVND-GSHLHTYSQAAFPGPLQPFF 160
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
 303-481 9.57e-17

PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 15 (TRIM15), also referred to as RING finger protein 93 (RNF93) or Zinc finger protein B7 or 178 (ZNFB7 or ZNF178). TRIM15 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. The PRY and SPRY/B30.2 domains can function as immune defense components and in pathogen sensing. TRIM15 has been shown to regulate inflammatory and innate immune signaling, in addition to displaying antiviral activities. Down-regulation of TRIM15, as well as TRIM11, enhances virus release, suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. TRIM15 is also a regulatory component of focal adhesion turnover and cell migration.


Pssm-ID: 293998 [Multi-domain]  Cd Length: 170  Bit Score: 77.60  E-value: 9.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 303 TFNPENLNLNLILSEDHRQVT------SVPIWPFKC-CNNGILGSKCFLSGKHYWEVDV--SEKNAWTLGVysrkrtLKF 373
Cdd:cd15826    3 TLDPQTASGSLVLSEDRKSVRytrqkqNLPDSPLRFdGLPAVLGSPGFSSGRHRWQVEVqlGDGGGCTVGV------AGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 374 DVRRcsKSQPNgyhrYKPQNGYWVIGLqdgSKYSIFEDSSncgPTVLNPFVATPlHRIGVFLDCEEGIVSFFNVTNHgSL 453
Cdd:cd15826   77 SVRR--KGEMG----LSAEDGVWAVIL---SHQQCWASTS---PGTDLPLSEIP-RRVGVALDYEAGTVTLTNAETQ-EP 142

                        170       180
                 ....*....|....*....|....*...
gi 451770402 454 IYKFTqCRFSQPAYPYFNPWDCPAPMTL 481
Cdd:cd15826  143 IFTFT-ASFSGKVFPFFAVWKKGSRLTL 169
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
 303-474 2.49e-16

PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain family contains residues in the N-terminus that form a distinct PRY domain structure such that the B30.2 domain consists of PRY and SPRY subdomains. TRIM14 domains have yet to be characterized. These B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. It belongs to Class IV TRIM protein family which has members involved in antiviral immunity at various levels of interferon signaling cascade.


Pssm-ID: 293973 [Multi-domain]  Cd Length: 173  Bit Score: 76.75  E-value: 2.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 303 TFNPENLNLNLILSEDHRQVTSVpiWPFKCCNNG---------ILGSKCFLSGKHYWEVDVSEKNA-WTLGVYSRKRTLK 372
Cdd:cd13738    2 TLEPDTLHPRLRLSDDRLTVSCG--WLGTLGLCPpqrfdklwqVLSRDSFFSGRHYWEVDLQEAGAgWWVGAAYPSIGRK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 373 FDVRRCS---KSQPNGYHRYKPQngYWVigLQDGSKYSIFEDSsncgptvlNPfvatplHRIGVFLDCEEGIVSFFNVTN 449
Cdd:cd13738   80 GDSEAARlgwNRQSWCLKRYDLE--YWA--FHDGQRSRLRPED--------DP------DRLGVFLDYEAGILSFYDVTG 141

                        170       180
                 ....*....|....*....|....*
gi 451770402 450 HGSLIYKFtQCRFSQPAYPYFNPWD 474
Cdd:cd13738  142 GMTHLHTF-RATFQEPLYPALRLWE 165
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
 301-483 2.69e-14

PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 41 (TRIM41). TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.


Pssm-ID: 240499 [Multi-domain]  Cd Length: 199  Bit Score: 71.33  E-value: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQV------TSVPIWPFK----CCnngILGSKCFLSGKHYWEVDVSEKNAWTLG-----VY 365
Cdd:cd13741    1 DLTLDPDTAHPALLLSPDRRGVrlaerrQEVPEHPKRfsadCC---VLGAQGFRSGRHYWEVEVGGRRGWAVGaaresTH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 366 SRKRTLKFDVRRCSKSQPNGYHRYKP-----------QNGYWVIGlQDGSKYsifEDSSNCGPTVLNPfvATPLHRIGVF 434
Cdd:cd13741   78 HKEKVGSGGSSVSSGDASSSRHHHRRrrlhlpqqpllQREVWCVG-TNGKRY---QAQSSTEQTLLSP--SEKPRRFGVY 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 451770402 435 LDCEEGIVSFFNVTNHGSlIYKFTQCRFSQPAYPYFNPWDCPAPMTLCP 483
Cdd:cd13741  152 LDYEAGRLGFYNAETLAH-VHTFSAAFLGERVFPFFRVLSKGTRIKLCP 199
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
 303-470 2.74e-14

PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of the RING finger protein RNF135 (also known as Riplet/RNF135), which ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Normally, RIG-I is activated by TRIM25 in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. However, RNF135, consisting of an N-terminal RING finger domain, C-terminal SPRY and PRY motifs and showing sequence similarity to TRIM25, acts as an alternative factor that promotes RIG-I activation independent of TRIM25.


Pssm-ID: 293959 [Multi-domain]  Cd Length: 168  Bit Score: 70.62  E-value: 2.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 303 TFNPENLNLNLILSEDHRQVT-SVPIWPFKCCN-----NGILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRTLKFDVR 376
Cdd:cd12902    2 TFDLRSLSCSLEVSEDSRKVTvSHGPQAYAWSPdrfsiSQVLCSQAFSSGQHYWEVDTRQCSHWAVGVASWEMSRDQMLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 377 RCSKSqpngyhrykpqngyWVIGLQDGSKYSIFEDSSNcgpTVLN---PFVatplhrIGVFLDCEEGIVSFFNVTNHGSL 453
Cdd:cd12902   82 RTMDS--------------WCIEWKGTGQLSAWHMNKE---TVLGsdkPRV------VGIWLDLEEGKLAFYSVANQERL 138

                        170
                 ....*....|....*..
gi 451770402 454 IYKFTQcRFSQPAYPYF 470
Cdd:cd12902  139 LHECEV-SASSPLHPAF 154
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
 301-483 9.83e-14

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 7 (TRIM7), also referred to as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90). TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. The GNIP gene encodes at least four distinct isoforms of GNIP, of which three (GNIP1, GNIP2, and GNIP3) have the B30.2 domain.


Pssm-ID: 293975 [Multi-domain]  Cd Length: 169  Bit Score: 69.21  E-value: 9.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQV------TSVPIWPFKC-CNNGILGSKCFLSGKHYWEVDVSEKNAWTLGVysrkrtLKF 373
Cdd:cd13740    1 ELTLDPDSANPRLILSLDLKSVrlgeraQDLPNHPCRFdTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGV------ARE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 374 DVRRcsksqpNGYHRYKPQNGYWVIGLQDGSKYSIFEDSSncgptvlNPFVATPLHRIGVFLDCEEGIVSFFNVTN--Hg 451
Cdd:cd13740   75 SVRR------KGLTPFTPEEGVWALQLNGGQYWAVTSPER-------TPLSCGHLSRVRVALDLEVGAVSFYAAEDmrH- 140

                        170       180       190
                 ....*....|....*....|....*....|..
gi 451770402 452 slIYKFtQCRFSQPAYPYFNPWDCPAPMTLCP 483
Cdd:cd13740  141 --IYTF-RVNFQERVFPLFSVCSTGTYLRIWP 169
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
 299-482 3.00e-13

PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM65 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). The SPRY/PRY combination is a possible component of immune defense. This protein family has not been characterized.


Pssm-ID: 293953 [Multi-domain]  Cd Length: 182  Bit Score: 67.86  E-value: 3.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 299 WADF---TFNPENLNLNLILSEDHRQVT--------------SVPIWPFKCcnngilgSKCFLSGKHYWEVDVSEKNAwT 361
Cdd:cd12896    6 WKDYrnlTFDPRTANKYLELSRQNRRAKhgrsaargvpaspgSFELWQVQC-------TQSFQHGHHYWEVEVSSHSV-T 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 362 LGV----YSRKRtlkfdvrrcsksqpNGYHRYKpqngywvIGLQDGS-KYSIFEDSSNCGPTVLNPFVATPLHR-IGVFL 435
Cdd:cd12896   78 LGVtypgLPRHK--------------QGGHKDN-------IGRNPCSwGLQIQEDSLQAWHNGRAQKLQGVSYRlLGVDL 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 451770402 436 DCEEGIVSFFNVTNHGSLIYKFtQCRFSQPAYPYFnpWDCP-APMTLC 482
Cdd:cd12896  137 DLEAGTLTFYGLEPGTQRLHTF-HAIFTQPLYPVF--WLLEgRTLTLC 181
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
 301-470 3.31e-13

Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of Stonustoxin alpha proteins. Stonustoxin (SNTX) is a multifunctional lethal protein isolated from venom elaborated by the stonefish. It comprises two subunits, termed alpha and beta. SNTX elicits an array of biological responses, particularly a potent hypotension and respiratory difficulties.


Pssm-ID: 294002 [Multi-domain]  Cd Length: 180  Bit Score: 67.90  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 301 DFTFNPENLNLNLILSEDHRQVTSVP---IWP-----FKC-----CNNGilgskcfLSGKHYWEVDVSeKNAWTLGV-Y- 365
Cdd:cd16040   10 QLTLDPNTAHRNLSLSEGNRKVTRVKeeqPYPdhperFDYwpqvlCREG-------LSGRCYWEVEWS-GGGVDIAVaYk 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 366 --SRKRtlkfDVRRCS-----KSqpngyhrykpqngyWVIGLqDGSKYSIFEDSsNCGPTVLNPfvaTPLHRIGVFLDCE 438
Cdd:cd16040   82 giSRKG----DGDDSRfgyndKS--------------WSLEC-SPSGYSFWHNN-KKTEISVPS---SSSSRVGVYLDHS 138

                        170       180       190
                 ....*....|....*....|....*....|..
gi 451770402 439 EGIVSFFNVTNHGSLIYKFtQCRFSQPAYPYF 470
Cdd:cd16040  139 AGTLSFYSVSDTMTLLHTV-QTTFTEPLYPGF 169
Bbox2_TRIM7-like cd19762
B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM7, TRIM27 and ...
 95-136 2.64e-11

B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM7, TRIM27 and similar proteins; The family includes TRIM7 and TRIM27, both of which belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by an 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 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. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM27, also termed RING finger protein 76 (RNF76), or RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. It also inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. Furthermore, TRIM27 promotes non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. In addition, TRIM27 forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is also a component of an estrogen receptor 1 (ESR1) regulatory complex, and is involved in estrogen receptor-mediated transcription in MCF-7 cells. Meanwhile, TRIM27 interacts with the hinge region of chromosome 3 protein (SMC3), a component of the multimeric cohesin complex that holds sister chromatids together and prevents their premature separation during mitosis.


Pssm-ID: 380820 [Multi-domain]  Cd Length: 44  Bit Score: 58.48  E-value: 2.64e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 451770402  95 LCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFLRDEAV 136
Cdd:cd19762    2 VCEKHQEPLKLFCKEDKRPICVVCDRSREHRHHTVLPVEEAA 43
Bbox2_TRIM68_C-IV cd19795
B-box-type 2 zinc finger found in tripartite motif-containing protein 68 (TRIM68) and similar ...
 93-136 5.62e-11

B-box-type 2 zinc finger found in tripartite motif-containing protein 68 (TRIM68) and similar proteins; TRIM68, also known as RING finger protein 137 (RNF137) or SSA protein SS-56 (SS-56), is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems. It also functions as a cofactor for androgen receptor-mediated transcription by regulating ligand-dependent transcription of androgen receptor in prostate cancer cells. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogren's syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE. TRIM68 belongs 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, 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: 380853 [Multi-domain]  Cd Length: 44  Bit Score: 57.46  E-value: 5.62e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 451770402  93 GDLCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFLRDEAV 136
Cdd:cd19795    1 EDLCERHKEKLNLFCEEDQELLCVVCEQSPEHKAHTVVPVEEAA 44
SPRY_PRY_TRIM25-like cd13737
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, ...
 309-468 2.37e-10

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of proteins similar to TRIM25 (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function.


Pssm-ID: 293972  Cd Length: 172  Bit Score: 59.50  E-value: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 309 LNLNLILSEDHRQVTSVPIWPFKCCNNGILgskcflSGKHYWEVDVSekNAWT-LGVYSRKRtlkfdvrrcsksqpngyH 387
Cdd:cd13737   22 LNMGILLESFFGPCQGFNHWPQVLCTRSLC------EGCHYWEAEVS--NSWVcLGVTYSYS-----------------H 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 388 RYKPQNGYWVIGLQ--------DGSKYSIFEDSSNcgpTVLNpfvATPLHRIGVFLDCEEGIVSFFNVTNHGSLIYKFTQ 459
Cdd:cd13737   77 PTGKSCIFYLIGRNpyswclewDSLKFSVWHNNIQ---TVVH---GSYYKTIGVLLDYAAGSLTFYGVANTMNLIYRFLT 150


                 ....*....
gi 451770402 460 CrFSQPAYP 468
Cdd:cd13737  151 T-FTEPLYP 158
SPRY_PRY_TRIM16 cd12890
PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of ...
 298-470 3.05e-10

PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM16 and TRIM-like proteins. TRIM16 (also known as estrogen-responsive B box protein or EBBP) does not possess a RING domain like the other TRIM proteins, but contains two B-box domains and can heterodimerize with other TRIM proteins such as TRIM24, Promyelocytic leukemia (PML) protein and Midline-1 (MID1 or TRIM18). It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. It has been shown that loss of TRIM16 expression plays an important role in the development of cutaneous squamous cell carcinoma (SCC) and is a determinant of retinoid sensitivity. TRIM16 also has E3 ubiquitin ligase activity.


Pssm-ID: 293948  Cd Length: 182  Bit Score: 59.40  E-value: 3.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 298 YWADFTFNPENLNLNLILSEDHRQVTSVPIWP------------FKccnnGILGSKCFLSGKHYWEVDVSEKNAWtLGVy 365
Cdd:cd12890    7 YAYPLTFDPDTAHRYLRLTEDNRKVTNTTPWEhpypdhperfehWR----QVLSQQSLYLGRYYFEVEISGEGTY-VGL- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 366 srkrTLKFDVRRCSKSqpNGyhRYKPQNGYWVIGLqDGSKYSIFEDSSncgPTvlnPFVATPLHRIGVFLDCEEGIVSFF 445
Cdd:cd12890   81 ----TYKSIDRKGSES--NS--CISGNNFSWCLQW-NGKEFSAWHSDV---ET---PLKKGPFTRLGIYLDYPGGTLSFY 145

                        170       180
                 ....*....|....*....|....*.
gi 451770402 446 NVTNHG-SLIYKFtQCRFSQPAYPYF 470
Cdd:cd12890  146 GVEDDGmTLLHKF-QCKFTEPLYPAF 170
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
 330-482 8.41e-10

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM25 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function.


Pssm-ID: 293971 [Multi-domain]  Cd Length: 169  Bit Score: 57.58  E-value: 8.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 330 FKCCNNgILGSKCFLSGKHYWEVDVSEKNAWTLGVYSRKRTLKFDVRRCSKSQPNgyhrykpqngyWVIGLQDgSKYSIF 409
Cdd:cd13736   37 FTYCSQ-VLGLHCFKQGIHYWEVELQKNNFCGVGICYGSMDRQGPESRLGRNSES-----------WCVEWFN-VKISAW 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 451770402 410 EDSSNcgpTVLNPFVATplhRIGVFLDCEEGIVSFFNVTNHGSLIYKFtQCRFSQPAYPYFNPWDCPAPMTLC 482
Cdd:cd13736  104 HNNVE---KTLPSTKAT---RVGVLLNCDHGFVIFFAVQDKVHLMYKF-KVDFTEALYPAFWVFSAGTTLSLC 169
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
 337-476 9.46e-10

PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger protein 87 (RNF87); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM4 which is also known as RING finger protein 87 (RNF87). TRIM4 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It is a positive regulator of RIG-I-mediated interferon (IFN) induction. It regulates virus-induced IFN induction and cellular antiviral innate immunity by targeting RIG-I for K63-linked poly-ubiquitination. Over-expression of TRIM4 enhances virus-triggered activation of transcription factors IRF3 and NF-kappaB, as well as IFN-beta induction. Expression of TRIM4 differs significantly in Huntington's Disease (HD) neural cells when compared with wild-type controls, possibly impacting down-regulation of the Huntingtin (HTT) gene, which is involved in the regulation of diverse cellular activities that are impaired in Huntington's Disease (HD) cells.


Pssm-ID: 293981  Cd Length: 191  Bit Score: 57.92  E-value: 9.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 337 ILGSKCFLSGKHYWEVDvseknawtlgvysRKRTLKFDVRRCSKSqpngyhrykpqngywVIGLQDGSKYS-------IF 409
Cdd:cd15809   66 VLGKNVFTSGKHYWEVE-------------NRDSLEIAVGVCRED---------------VMGITDGSEMSphvgiwaIC 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 451770402 410 EDSSNCGPTVLNPFVAT----PLHRIGVFLDCEEGIVSFFNVTNhGSLIYKFTqCRFSQPAYPYFnpWDCP 476
Cdd:cd15809  118 WSSAGYRPLTSSPVSPTkqepALHRVGVFLDHGAGEVSFYSAVD-GVHLHTFS-CPLVSRLRPFF--WLSP 184
Bbox2_TRIM39-like cd19780
B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM39, TRIM58 and ...
 95-135 1.08e-09

B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM39, TRIM58 and similar proteins; The family includes TRIM39 and TRIM58, both of which belong 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, Bbox2, and a coiled coil region, as well as a 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. TRIM39, also termed 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 and modulates cell cycle progression and DNA damage responses via stabilization of p21. TRIM39 also 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 (TNFalpha). 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. TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization.


Pssm-ID: 380838 [Multi-domain]  Cd Length: 44  Bit Score: 53.62  E-value: 1.08e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 451770402  95 LCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFLRDEA 135
Cdd:cd19780    4 LCARHREALSLFCEEDQEAVCLVCEISHDHRAHTLVPLQDA 44
Bbox2_TRIM21_C-IV cd19772
B-box-type 2 zinc finger found in tripartite motif-containing protein 21 (TRIM21) and similar ...
 96-127 1.56e-09

B-box-type 2 zinc finger found in tripartite motif-containing protein 21 (TRIM21) and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren's syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 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, 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: 380830 [Multi-domain]  Cd Length: 40  Bit Score: 53.27  E-value: 1.56e-09
                         10        20        30
                 ....*....|....*....|....*....|..
gi 451770402  96 CVHHGEKLLLFCQEDKKVICWVCERSQEHRGH 127
Cdd:cd19772    3 CAVHGERLHLFCEEDQKALCLVCAQSQKHRDH 34
SPRY_PRY_TRIM10 cd15827
PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic ...
 300-474 2.11e-09

PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic RING finger 1 (HERF1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM10, also known as RING finger protein 9 (RNF9) or hematopoietic RING finger 1 (HERF1). TRIM10 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM10/HERF1 is predominantly expressed during definitive erythropoiesis and in embryonic liver, and minimally expressed in adult liver, kidney, and colon. It is critical for erythroid cell differentiation and its down-regulation leads to cell death; inhibition of TRIM10 expression blocks terminal erythroid differentiation, while its over-expression in erythroid cells induces beta-major globin expression and erythroid differentiation.


Pssm-ID: 293999 [Multi-domain]  Cd Length: 172  Bit Score: 56.76  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 300 ADFTFNPENLNLNLILSEDHRQVTSVPIWPFKCCN-------NGILGSKCFLSGKHYW--EVDVSEKNAWTLGVYSRkrt 370
Cdd:cd15827    2 AHISLDPQTSHPKLLLSEDHQRARFSYKWQNSPDNpqrfdraTCVLAHDGFTGGRHTWvvSVDLAHGGSCTVGVVSE--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 371 lkfDVRRcsksqpNGYHRYKPQNGYWVIGLQDGskysiFEDSSNCGPTVL----NPfvatplHRIGVFLDCEEGIVSFFN 446
Cdd:cd15827   79 ---DVRR------KGELRLRPEEGVWAVRLAWG-----FVSALGSFPTRLaleeQP------RQVRVSLDYEVGWVTFVN 138

                        170       180
                 ....*....|....*....|....*...
gi 451770402 447 VTNHgSLIYKFTqCRFSQPAYPYFNPWD 474
Cdd:cd15827  139 AVTQ-EPIYTFT-ASFTQKVFPFFGLWG 164
Bbox2_TRIM4-like cd19760
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM4, TRIM17, TRIM41, ...
 94-127 7.81e-09

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM4, TRIM17, TRIM41, TRIM52 and similar proteins; This family includes a group of tripartite motif-containing proteins, including TRIM4, TRIM17, TRIM41 and TRIM52. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at mitochondria. TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain. TRIM4, TRIM17 and TRIM41 belong 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, 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. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of TRIM family that contains only RBCC domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380818 [Multi-domain]  Cd Length: 39  Bit Score: 51.09  E-value: 7.81e-09
                         10        20        30
                 ....*....|....*....|....*....|....
gi 451770402  94 DLCVHHGEKLLLFCQEDKKVICWVCERSQEHRGH 127
Cdd:cd19760    1 GLCEKHQEPLKLFCEEDEALICVICRESRAHRAH 34
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
 11-83 1.07e-08

RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting it may be a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated with uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 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: 438258 [Multi-domain]  Cd Length: 77  Bit Score: 51.82  E-value: 1.07e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 451770402  11 KEATCPVCHVLLIKPLNLGSGHHVSQACLTVkktavTNPRGKSLCPMCGNRFSFENLQANKHLADVVERLREV 83
Cdd:cd16596    8 EEVTCPICLDPFVEPVSIECGHSFCQECISQ-----VGKGGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKEI 75
Bbox2_xNF7-like cd19800
B-box-type 2 zinc finger found in Xenopus laevis nuclear factor 7 (xNF7) and similar proteins; ...
 94-128 2.21e-08

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: 50.09  E-value: 2.21e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 451770402  94 DLCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHH 128
Cdd:cd19800    1 EVCSEHDEPLKLFCKDDKRLICVICRDSRKHRGHR 35
Bbox2_TRIM11_C-IV cd19766
B-box-type 2 zinc finger found in tripartite motif-containing protein 11 (TRIM11) and similar ...
 95-135 5.37e-08

B-box-type 2 zinc finger found in tripartite motif-containing protein 11 (TRIM11) and similar proteins; TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) through mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. Trim11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM11 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, Bbox2, and a coiled coil region, as well as a 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: 380824 [Multi-domain]  Cd Length: 44  Bit Score: 49.05  E-value: 5.37e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 451770402  95 LCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFLRDEA 135
Cdd:cd19766    2 LCGKHREPLKLFCKDHEALLCVVCERSREHWGHRVVPAEEA 42
BBOX smart00336
B-Box-type zinc finger;
91-131 7.42e-08

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 48.49  E-value: 7.42e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 451770402    91 KKGDLC-VHHGEKLLLFCQEDKKVICWVCERSqEHRGHHTFL 131
Cdd:smart00336   1 QRAPKCdSHGDEPAEFFCEECGALLCRTCDEA-EHRGHTVVL 41
Bbox2_TRIM10-like cd19765
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM10, TRIM15, ...
 94-127 1.94e-07

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM10, TRIM15, TRIM26, TRIM31 and similar proteins; This family includes TRIM10, TRIM15, TRIM26 and TRIM31. TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM15, also termed RING finger protein 93 (RNF93), or zinc finger protein 178 (ZNF178), or zinc finger protein B7 (ZNFB7), is a focal adhesion protein that regulates focal adhesion disassembly. It localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. TRIM15 can also associate with coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. As an additional component of the integrin adhesome, it regulates focal adhesion turnover and cell migration. TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM31 is an E3 ubiquitin-protein ligase that primarily localizes to the cytoplasm, but is also associated with the mitochondria. It can negatively regulate cell proliferation and may be a potential biomarker of gastric cancer as it is overexpressed from the early stage of gastric carcinogenesis. TRIM31 is downregulated in non-small cell lung cancer and serves as a potential tumor suppressor. It interacts with p52 (Shc) and inhibits Src-induced anchorage-independent growth. TRIM10, TRIM15 and TRIM26 belong 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, 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. TRIM31 belongs to the C-V subclass of TRIM family of proteins. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380823 [Multi-domain]  Cd Length: 39  Bit Score: 47.08  E-value: 1.94e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 451770402  94 DLCVHHGEKLLLFCQEDKKVICWVCERSQEHRGH 127
Cdd:cd19765    1 TLCEEHGEKIHFFCEDDGKFLCVVCRESREHRTH 34
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 337-473 2.53e-07

Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This domain is part of the fibronectin type III and SPRY domain containing 1 (FSD1) and FSD1-like (FSD1L) proteins. These are centrosome-associated proteins that are characterized by an N-terminal coiled-coil region downstream of B-box (BBC) domain, a central fibronectin type III (FN3) domain, and C-terminal repeats in PRY/SPRY domain. The FSD1 protein associates with a subset of microtubules and may be involved in the stability and organization of microtubules during cytokinesis.


Pssm-ID: 293958  Cd Length: 207  Bit Score: 51.37  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 337 ILGSKCFLSGKHYWEVDVS-EKNAWTLGV-YsrkRTL-KFDvrRCSKSqpngyhrykpqNGYWVIGLQDGSKYSiFEDSS 413
Cdd:cd12901   76 VLGDTLIDGGQHYWEVRAQkDSKAFSVGVaY---RSLgKFD--QLGKT-----------NASWCLHVNNWLQNS-FAAKH 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 414 NCGPTVLNpfVATPlHRIGVFLDCEEGIVSFFNVTNHgSLIYKFtQCRFSQPAYPYFNPW 473
Cdd:cd12901  139 NNKAKTLD--VPVP-DRIGVYCDFDEGQLSFYNARTK-QLLHTF-KMKFTQPVLPAFMVW 193
Bbox2 cd19756
B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of ...
 97-128 4.13e-07

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: 46.25  E-value: 4.13e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 451770402  97 VHHGEKLLLFCQEDKKVICWVCERSQEHRGHH 128
Cdd:cd19756    4 EHPEEPLKLFCETCQELVCVLCLLSGEHRGHK 35
Bbox2_TRIM35_C-IV cd19777
B-box-type 2 zinc finger found in tripartite motif-containing protein 35 (TRIM35) and similar ...
 95-127 6.90e-07

B-box-type 2 zinc finger found in tripartite motif-containing protein 35 (TRIM35) and similar proteins; TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 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, 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: 380835 [Multi-domain]  Cd Length: 44  Bit Score: 45.93  E-value: 6.90e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 451770402  95 LCVHHGEKLLLFCQEDKKVICWVCERSQEHRGH 127
Cdd:cd19777    5 LCRLHGETLKLFCLDDKELLCCACQSSKQHQGH 37
Bbox2_TRIM43-like cd19783
B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, ...
 95-141 1.00e-06

B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51, TRIM64, TRIM77 and similar proteins; The family includes a group of closely related uncharacterized tripartite motif-containing proteins, TRIM43, TRIM43B, TRIM48/RNF101, TRIM49/RNF18, TRIM49B, TRIM49C/TRIM49L2, TRIM49D/TRIM49L, TRIM51/SPRYD5, TRIM64, TRIM64B, TRIM64C, and TRIM77, whose biological functions remain unclear. TRIM49, also known as testis-specific RING-finger protein, has moderate similarity with SS-A/Ro52 antigen, suggesting it may be one of target proteins of autoantibodies in the sera of patients with these autoimmune disorders. All family members (except for TRIM51) belong 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, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM51 belongs to unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380841 [Multi-domain]  Cd Length: 53  Bit Score: 45.62  E-value: 1.00e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 451770402  95 LCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFLRDEAVRECQE 141
Cdd:cd19783    6 ICGTHRETKKLFCEADKSLLCLLCSSSQEHRAHRHYPIEWAAEEHRE 52
Bbox2_TRIM16-like cd19769
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, ...
 95-138 1.19e-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: 45.01  E-value: 1.19e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 451770402  95 LCVHHGEKLLLFCQEDKKVICWVCeRSQEHRGHHTFLRDEAVRE 138
Cdd:cd19769    2 VCPIHKKPLELFCRTDQMCICELC-AKEEHRGHDVVTVEEEREK 44
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-247 4.64e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 4.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 131 LRDEAVRECQENLQEALKRLRKEQEKVETFEAD---IKEDRISWKHQIQTERQRIQTGYNQLRRILDKEE--QNELKRLR 205
Cdd:COG4372   28 ALSEQLRKALFELDKLQEELEQLREELEQAREEleqLEEELEQARSELEQLEEELEELNEQLQAAQAELAqaQEELESLQ 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 451770402 206 EEEQMILDSLAGAEAE---LAQQSQLVEELISDLERRCEWSDTEL 247
Cdd:COG4372  108 EEAEELQEELEELQKErqdLEQQRKQLEAQIAELQSEIAEREEEL 152
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
 313-475 1.56e-05

SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret family, since the protein is composed of a B-box, an alpha-helical coiled coil and a SPRY domain. The gene for BSPRY resides on human chromosome 9 and is specifically expressed in testis. The function of BSPRY is not known, but several related proteins of the RING-Box-coiled-coil (RBCC) family have been implicated in cell transformation.


Pssm-ID: 293961 [Multi-domain]  Cd Length: 171  Bit Score: 45.49  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 313 LILSEDHRQVT--------SVPIWP--FKCCNNGiLGSKCFLSGKHYWEVDVSEKNAWTLGVysrkrtlkfdvrrCSKSQ 382
Cdd:cd12904   12 LSLSEDRRTLTfspkkarqSPPDDPerFDHWPNA-LASLSFSSGTHAWVVDVGKSCAYKVGV-------------CYGSL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 383 PngyhRYKPQN----GY----WVIGLQDGsKYSIFEDSSNcgptvlnpfvaTPLH------RIGVFLDCEEGIVSFFNVT 448
Cdd:cd12904   78 E----RKGSGNearlGYnafsWVFSRYDG-EFSFSHNGQH-----------VPLEllkcpaRVGVLLDWPSQELLFYDPD 141

                        170       180
                 ....*....|....*....|....*..
gi 451770402 449 NhGSLIYKFTQCrFSQPAYPYFNPWDC 475
Cdd:cd12904  142 S-CTVLHSHREA-FAAPLLPVFAVADQ 166
Bbox2_TRIM40_C-V cd19781
B-box-type 2 zinc finger found in tripartite motif-containing protein 40 (TRIM40) and similar ...
 92-135 2.72e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also termed probable E3 NEDD8-protein ligase, or RING finger protein 35, may function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway. It promotes neddylation of IKBKG/NEMO, stabilizing NFKBIA, and inhibiting NF-kappaB nuclear translocation and activity. TRIM40 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380839 [Multi-domain]  Cd Length: 44  Bit Score: 41.25  E-value: 2.72e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 451770402  92 KGDLCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFLRDEA 135
Cdd:cd19781    1 AGYLCQLHEKKVEWFCEEDQVLLCEECLKSPEHQSHHVLTIEDA 44
Bbox2_TRIM20 cd19771
B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM20 and similar ...
 95-127 2.98e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM20 and similar proteins; TRIM20, also termed Pyrin, or Marenostrin (MEFV), is involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. TRIM20 belongs to unclassified TRIM 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 pyrin domain, a Bbox2 zinc finger, and 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: 380829 [Multi-domain]  Cd Length: 39  Bit Score: 40.92  E-value: 2.98e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 451770402  95 LCVHHGEKLLLFCQEDKKVICWVCERSQEHRGH 127
Cdd:cd19771    2 QCKLHLEQLKLFCEDHREPICLICQLSQEHQGH 34
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
 337-480 3.53e-05

PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called cardiomyopathy-associated protein 5; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM76, a Class I TRIM protein. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5 or myospryn or SPRYD2) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It has been suggested that TRIM76 is involved in two distinct processes, protein kinase A signaling and vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease; gene polymorphism of TRIM76 is associated with left ventricular wall thickness in patients with hypertension while its interactions with M-band titin and calpain 3 link it to tibial and limb-girdle muscular dystrophies.


Pssm-ID: 293955  Cd Length: 171  Bit Score: 44.15  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 337 ILGSKCFLSGKHYWEVDVSEKNAWTLGV----YSRKRTLKFD-VRRCSKSQPNgyhrykpqngywviglQDGSKYSIFED 411
Cdd:cd12898   43 VLGEELPSCGQYYWETTVTRCPAYRLGIcsssASQAGALGEGsTSWCLHCVPT----------------SEPCRYTLLHS 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 451770402 412 SsncgpTVLNPFVATPLHRIGVFLDCEEGIVSFFNVTNhGSLIYKFTQcRFSQPAYPYF---NPWDCPAPMT 480
Cdd:cd12898  107 G-----IVSDVFVTERPARVGTLLDYNNGRLIFINAES-GQLLGIFRH-RFAQPCHPAFaleKPGKLELHMG 171
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
 337-474 4.22e-05

PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain and is encoded by the SPRYD4 gene. SPRYD4 (SPRY containing domain 4) is ubiquitously expressed in many human tissues, most strongly in kidney, bladder, brain, thymus and stomach. Subcellular localization demonstrates that SPRYD4 protein is localized in the nucleus when overexpressed in COS-7 green monkey cell. It has remained uncharacterized thus far.


Pssm-ID: 293960  Cd Length: 169  Bit Score: 43.97  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 337 ILGSKCFLSGKHYWEVDVSEKNAWTLGV----YSRKRTLKFDvrRCSksqpngyhrykpqngyWVIGLQDGSKYSIFEds 412
Cdd:cd12903   46 VLGDTPVTSGRHYWEVTVKRSQEFRIGVadvdMSRDECIGTN--ESS----------------WVFAYAQRKWYAMVA-- 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 451770402 413 sncGPTVLNPFVATPlHRIGVFLDCEEGIVSFFNVTNhGSLIYKFtQCRFSQPAYPYFNPWD 474
Cdd:cd12903  106 ---NETVPVPLVGKP-DRVGLLLDYEAGKLSLVDVEK-NSVVHTM-SAEFRGPVVPAFALWD 161
Bbox2_TRIM72_C-IV cd19797
B-box-type 2 zinc finger found in tripartite motif-containing protein 72 (TRIM72) and similar ...
 94-135 4.91e-05

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: 40.73  E-value: 4.91e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 451770402  94 DLCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFLRDEA 135
Cdd:cd19797    1 GHCEEHLDPLSVYCEQDRALICGVCASLGKHKGHNIITAAEA 42
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-250 6.54e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402  131 LRDEAvRECQENLQEALKRLRKEQEKVETFE---------ADIKEDRISWK------HQIQTERQRIQTGYNQLRRILDK 195
Cdd:COG4913   615 LEAEL-AELEEELAEAEERLEALEAELDALQerrealqrlAEYSWDEIDVAsaereiAELEAELERLDASSDDLAALEEQ 693

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 451770402  196 EE--QNELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLERRCEWSDTELLQD 250
Cdd:COG4913   694 LEelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
134-256 6.58e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 134 EAVRECQENLQEaLKRLRKEQ-----EKVETFEADIKEDRISwkhQIQTERQRIQTgYnqLRRILDKeeqneLKRLREEE 208
Cdd:PRK02224 609 ERLREKREALAE-LNDERRERlaekrERKRELEAEFDEARIE---EAREDKERAEE-Y--LEQVEEK-----LDELREER 676

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 451770402 209 QMILDSLAGAEAELAQQSQLVEELiSDLERRCE-----WSDTELLQDVSGILK 256
Cdd:PRK02224 677 DDLQAEIGAVENELEELEELRERR-EALENRVEalealYDEAEELESMYGDLR 728
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
 9-73 8.29e-05

RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs 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, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438260 [Multi-domain]  Cd Length: 64  Bit Score: 40.53  E-value: 8.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 451770402   9 VQKEATCPVCHVLLIKPLNLGSGHHVSQACLTvKKTAVTNPRGKSLCPMCGNRFSFENLQANKHL 73
Cdd:cd16598    1 LEEEVTCSICLDYLRDPVTIDCGHNFCRSCIT-DYCPISGGHERPVCPLCRKPFKKENIRPNWQL 64
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 138-247 8.39e-05

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: 44.89  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402  138 ECQENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRILDK-----EEQNELKRLREEEQMIL 212
Cdd:pfam07888  38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKheeleEKYKELSASSEELSEEK 117

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 451770402  213 DSLAGAEAELAQQSQLVEELISDLERRCEWSDTEL 247
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
PRY smart00589
associated with SPRY domains;
299-343 9.59e-05

associated with SPRY domains;


Pssm-ID: 128857  Cd Length: 52  Bit Score: 39.87  E-value: 9.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 451770402   299 WADFTFNPENLNLNLILSEDHRQVTSVPIWP--------FKCCNNgILGSKCF 343
Cdd:smart00589   1 AVDVTLDPDTAHPYLLLSEDRRSVRYGDLKQslpdnperFDSYPC-VLGSQGF 52
Bbox2_TRIM44 cd19784
B-box-type 2 zinc finger found in tripartite motif-containing protein 44 (TRIM44) and similar ...
 96-127 9.81e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 44 (TRIM44) and similar proteins; TRIM44, also termed protein DIPB, functions as a critical regulator in tumor metastasis and progression. TRIM44 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 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380842 [Multi-domain]  Cd Length: 39  Bit Score: 39.76  E-value: 9.81e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 451770402  96 CVHHGEKLLLFCQEDKKVICWVCERSQEHRGH 127
Cdd:cd19784    3 CPEHGQELSLYCKEDEKIICVLCAVIGAHRQH 34
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 140-239 1.04e-04

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: 44.37  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 140 QENLQEALKRL-------RKEQEKVETFEADIKEDRISwKHQIQTERQRIQTGYNQLrrildKEEQNELKRLREEEQMIL 212
Cdd:COG4942  128 PEDFLDAVRRLqylkylaPARREQAEELRADLAELAAL-RAELEAERAELEALLAEL-----EEERAALEALKAERQKLL 201

                         90       100       110
                 ....*....|....*....|....*....|....
gi 451770402 213 DSLAGAE-------AELAQQSQLVEELISDLERR 239
Cdd:COG4942  202 ARLEKELaelaaelAELQQEAEELEALIARLEAE 235
Bbox2_TRIM50-like cd19787
B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 ...
 96-127 1.05e-04

B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins; TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with the histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 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, 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. The family also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins and may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by the N-terminal RBCC domains only.


Pssm-ID: 380845 [Multi-domain]  Cd Length: 39  Bit Score: 39.39  E-value: 1.05e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 451770402  96 CVHHGEKLLLFCQEDKKVICWVCERSQEHRGH 127
Cdd:cd19787    3 CPHHHNPLSLFCEKDQEVICGLCGLIGSHRQH 34
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 141-265 1.09e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 44.24  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   141 ENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERqriqtgynQLRRILDKEEQNELKRLREE------EQMI--- 211
Cdd:smart00787 154 EGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK--------QLEDELEDCDPTELDRAKEKlkkllqEIMIkvk 225

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 451770402   212 --------LDSLAGAEAELAQQSQLVEELISDLERR------CEWSDTELLQDVSGILKWSQIWTLKK 265
Cdd:smart00787 226 kleeleeeLQELESKIEDLTNKKSELNTEIAEAEKKleqcrgFTFKEIEKLKEQLKLLQSLTGWKITK 293
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
 13-63 1.18e-04

RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; RNF168 is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. It, together with RNF8, functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates, such as H2A and H2AX with H2AK13/15 ubiquitylation, facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. Moreover, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF168 contains an N-terminal C3HC4-type RING-HC finger that catalyzes H2A-K15ub and interacts with H2A, and two MIU (motif interacting with ubiquitin) domains responsible for the interaction with K63 linked poly-ubiquitin.


Pssm-ID: 438212 [Multi-domain]  Cd Length: 48  Bit Score: 39.67  E-value: 1.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 451770402  13 ATCPVCHVLLIKPLNLGSGHHVSQAC--LTVKKTAVTnprgkslCPMCGNRFS 63
Cdd:cd16550    1 CLCPICLEILVEPVTLPCNHTLCMPCfqSTVEKASLC-------CPLCRLRIS 46
zf-B_box pfam00643
B-box zinc finger;
91-129 1.29e-04

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 39.38  E-value: 1.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 451770402   91 KKGDLC-VHHGEKLLLFCQEDKKVICWVCERSqEHRGHHT 129
Cdd:pfam00643   1 SKERLCpEHEEEPLTLYCNDCQELLCEECSVG-EHRGHTV 39
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
133-238 1.30e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 43.28  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 133 DEAVRECQENLQEALKRLrkeqekvetfeADIKEDRISWKHQIQTERQRIQTGYNQLRRILDKEEQNELKRLREEEQMIL 212
Cdd:COG1842   29 DQAIRDMEEDLVEARQAL-----------AQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELE 97

                         90       100
                 ....*....|....*....|....*.
gi 451770402 213 DSLAGAEAELAQQSQLVEELISDLER 238
Cdd:COG1842   98 AQAEALEAQLAQLEEQVEKLKEALRQ 123
PRK12704 PRK12704
phosphodiesterase; Provisional
 131-238 1.37e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 131 LRDEAVRECQE---NLQEALKRLRKEQEKVETFEADIkEDRiswKHQIQTERQRIqtgyNQLRRILDKEEQnELKRLREE 207
Cdd:PRK12704  69 LRNEFEKELRErrnELQKLEKRLLQKEENLDRKLELL-EKR---EEELEKKEKEL----EQKQQELEKKEE-ELEELIEE 139

                         90       100       110
                 ....*....|....*....|....*....|.
gi 451770402 208 EQMILDSLAGAEAELAQQsQLVEELISDLER 238
Cdd:PRK12704 140 QLQELERISGLTAEEAKE-ILLEKVEEEARH 169
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 141-250 1.40e-04

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 41.48  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   141 ENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRILDKEEQ---NELKRLREEEQMILDSLAg 217
Cdd:smart00502   3 EALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKqllEDLEEQKENKLKVLEQQL- 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 451770402   218 aeAELAQQSQLVEELISDLERRCEWSD-TELLQD 250
Cdd:smart00502  82 --ESLTQKQEKLSHAINFTEEALNSGDpTELLLS 113
PRK12704 PRK12704
phosphodiesterase; Provisional
 133-253 1.59e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 133 DEAVRECQENLQEALKRLRKE-QEKVETFEADIKEdriswkhqiqtERQRIQtgyNQLRRILDKEEQ--NELKRLREEEQ 209
Cdd:PRK12704  45 EEAKKEAEAIKKEALLEAKEEiHKLRNEFEKELRE-----------RRNELQ---KLEKRLLQKEENldRKLELLEKREE 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 451770402 210 MILDSlagaEAELAQQSQLVEELISDLERRCEWSDTElLQDVSG 253
Cdd:PRK12704 111 ELEKK----EKELEQKQQELEKKEEELEELIEEQLQE-LERISG 149
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 134-239 1.63e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 134 EAVRECQENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRILDKEE--QNELKRLREEEQMI 211
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEelEEELEELEEELEEA 349

                         90       100
                 ....*....|....*....|....*...
gi 451770402 212 LDSLAGAEAELAQQSQLVEELISDLERR 239
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEA 377
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
 10-70 1.66e-04

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and TRIM27, and similar proteins; TRIM7, TRIM11 and TRIM27, closely related tripartite motif-containing proteins, belong 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, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) by mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. TRIM11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. TRIM27 promotes a non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. TRIM27 also forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is a component of an estrogen receptor 1 (ESR1) regulatory complex that is involved in estrogen receptor-mediated transcription in MCF-7 cells.


Pssm-ID: 438256 [Multi-domain]  Cd Length: 61  Bit Score: 39.59  E-value: 1.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 451770402  10 QKEATCPVCHVLLIKPLNLGSGHHVSQACLTvkkTAVTNPRGKSLCPMCGNRFSFENLQAN 70
Cdd:cd16594    3 QEELTCPICLDYFTDPVTLDCGHSFCRACIA---RCWEEPETSASCPQCRETCPQRNLRPN 60
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 143-239 1.72e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 42.74  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402  143 LQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRILDKEEQNELKRLREEEQMILDSLAGAEAEL 222
Cdd:pfam04012  27 LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSLEKQAEALETQL 106

                          90       100
                  ....*....|....*....|
gi 451770402  223 AQQSQLVEEL---ISDLERR 239
Cdd:pfam04012 107 AQQRSAVEQLrkqLAALETK 126
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 119-238 2.00e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 119 ERSQEHRGHHTFLRDEAVrecQENLQEALKRLRKEQEKVETFEADIKEDRiswkHQIQTERQRIQtgynqlrrildkEEQ 198
Cdd:COG1196  220 EELKELEAELLLLKLREL---EAELEELEAELEELEAELEELEAELAELE----AELEELRLELE------------ELE 280

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 451770402 199 NELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLER 238
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
Bbox2_TRIM60-like cd19791
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM60, TRIM61, ...
 95-128 2.30e-04

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM60, TRIM61, TRIM75 and similar proteins; This family includes a group of tripartite motif-containing proteins, including TRIM60, TRIM61 and TRIM75. TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. TRIM60 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM61 is closely related to TRIM60, but its biological function remains unclear. TRIM75 could be the product of a pseudogene. Its biological function remains unclear. TRIM60 and TRIM75 belong 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 RING finger, 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. In contrast, TRIM61 belongs to the C-V subclass of TRIM family that contains RBCC domains only. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380849 [Multi-domain]  Cd Length: 39  Bit Score: 38.67  E-value: 2.30e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 451770402  95 LCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHH 128
Cdd:cd19791    2 LCEKHNQPLTKFCKKDLEPLCPQCSQSTDHQHHV 35
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 140-248 2.65e-04

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: 43.21  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 140 QENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRIldkeeQNELKRLREEEQMILDSLAGAE 219
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-----EQELAALEAELAELEKEIAELR 96

                         90       100
                 ....*....|....*....|....*....
gi 451770402 220 AELAQQSQLVEELISDLERRCEWSDTELL 248
Cdd:COG4942   97 AELEAQKEELAELLRALYRLGRQPPLALL 125
RING-HC_TRIM10_C-IV cd16593
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ...
 8-62 3.90e-04

RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins; TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 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: 438255 [Multi-domain]  Cd Length: 61  Bit Score: 38.74  E-value: 3.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 451770402   8 DVQKEATCPVCHVLLIKPLNLGSGHHVSQACLT-VKKTAVTNPRGKSLCPMCGNRF 62
Cdd:cd16593    1 SLADEVNCPICQGTLREPVTIDCGHNFCRACLTrYCEIPGPDLEEPPTCPLCKEPF 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 133-239 4.04e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 133 DEAVRECQENLQEALKRLRKEQEKVETFEADIK---EDRISWKHQIQTERQRIQTGYNQLrrildKEEQNELKRLREEEQ 209
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELEEELEELEEEL-----EELEEELEEAEEELE 354

                         90       100       110
                 ....*....|....*....|....*....|
gi 451770402 210 MILDSLAGAEAELAQQSQLVEELISDLERR 239
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEEL 384
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 141-219 4.18e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 40.64  E-value: 4.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 451770402  141 ENLQEALKRLRKEQEKVETFEADIKEDRiswKHQIQTERQRIQTGYNQLRRILDKEEQNELKRLREEEQMILDSLAGAE 219
Cdd:pfam03938  36 EAKQKELQKLYEELQKDGALLEEEREEK---EQELQKKEQELQQLQQKAQQELQKKQQELLQPIQDKINKAIKEVAKEK 111
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 346-470 4.43e-04

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


Pssm-ID: 293931  Cd Length: 118  Bit Score: 40.11  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 346 GKHYWEVDV--SEKNAWTLGVYSrkrtlkfdvrrcSKSQPNGYHRYKPQNGYWVIG---LQDGSKYSIFEDSSNCgptvl 420
Cdd:cd11709    1 GKWYWEVRVdsGNGGLIQVGWAT------------KSFSLDGEGGVGDDEESWGYDgsrLRKGHGGSSGPGGRPW----- 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 451770402 421 npfvaTPLHRIGVFLDCEEGIVSFFNVtnhGSLIYKFTQCRFSQPA--YPYF 470
Cdd:cd11709   64 -----KSGDVVGCLLDLDEGTLSFSLN---GKDLGVAFTNLFLKGGglYPAV 107
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
143-237 4.81e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 143 LQEALKRLRKEQEKVETFEADIKEdriswkhqIQTERQRIQTGYNQLRRILDKEEQNELKRLREEEQMildSLAGAEAEL 222
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAE--------TEKRLEELRKELEELEKKYSEEEYEELREEYLELSR---ELAGLRAEL 682

                         90
                 ....*....|....*
gi 451770402 223 AQQSQLVEELISDLE 237
Cdd:PRK03918 683 EELEKRREEIKKTLE 697
RING-HC_RNF39 cd16592
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ...
 10-62 5.24e-04

RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, also called protein HZFw, may play a role in prolonged long term-potentiation (LTP) maintenance. It is involved in the etiology of Behcet's disease (BD). It may also be involved in HIV-1 replication. RNF39 acts as an E3 ubiquitin ligase that inhibits retinoic acid-inducible gene-I (RIG-I)-like receptor (RLR) pathways by mediating K48-linked ubiquitination and proteasomal degradation of DDX3X (DEAD-box RNA helicase 3, X-linked). RNF39 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438254 [Multi-domain]  Cd Length: 58  Bit Score: 38.20  E-value: 5.24e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 451770402  10 QKEATCPVCHVLLIKPLNLGSGHHVSQACLT----VKKTAVTNPRGKSlCPMCGNRF 62
Cdd:cd16592    2 QEETTCPICLGYFKDPVILDCEHSFCRACIArhwgQEAMEGNGAEGVF-CPQCGEPC 57
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
133-252 6.25e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 133 DEAVRECQEnLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQtgYNQLRRILdKEEQNELKRLREEEQMI- 211
Cdd:COG4717   84 EEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE--LEALEAEL-AELPERLEELEERLEELr 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 451770402 212 --LDSLAGAEAELAQQSQLVEELISDLERRCEWSDTELLQDVS 252
Cdd:COG4717  160 elEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 134-239 6.37e-04

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   134 EAVRECQENLQEALKRLRKEQEKVETFEADIKEDRISwKHQIQTERQRIQTGYNQLRRILDKEEQNELKRLREEEQMILD 213
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450

                           90       100
                   ....*....|....*....|....*.
gi 451770402   214 SLAGAEAELAQQSQLVEELISDLERR 239
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQA 476
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 133-261 7.90e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 133 DEAVRECQENLQEALKRLRKEQEKVETFEADIKEDRISwKHQIQTERQRIQTGYNQLRRILD------KEEQNELKRLRE 206
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIArleerrRELEERLEELEE 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 451770402 207 EEQMILDSLAGAEAELA---QQSQLVEELISDLERRCEWSDTELLQDVSGILKWSQIW 261
Cdd:COG1196  324 ELAELEEELEELEEELEeleEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 134-247 8.93e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 8.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 134 EAVRECQENLQEALKRLRKEQEKVETFEADIKEDriswKHQIQTERQRIQTGYNQLRRI--------LDKEEQNELKRLR 205
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIKKYEEQLGNVrnnkeyeaLQKEIESLKRRIS 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 451770402 206 EEEQMILD----------SLAGAEAELAQQSQLVEELISDLERRCEWSDTEL 247
Cdd:COG1579  107 DLEDEILElmerieeleeELAELEAELAELEAELEEKKAELDEELAELEAEL 158
Bbox2_TRIM14 cd19768
B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar ...
 97-136 9.64e-04

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: 37.02  E-value: 9.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 451770402  97 VHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFLRDEAV 136
Cdd:cd19768    5 EHKDRPLELFCKTCKRCVCALCPILGQHRGHDVRLIDEEA 44
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 134-239 9.94e-04

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: 41.98  E-value: 9.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   134 EAVRECQENLQ-------EALKRLRKEQEKVETFEA--DIKEDRISWK--HQIQTERQRIQTGYNQLRRIldKEEQNELK 202
Cdd:TIGR02169  180 EEVEENIERLDliidekrQQLERLRREREKAERYQAllKEKREYEGYEllKEKEALERQKEAIERQLASL--EEELEKLT 257

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 451770402   203 RLREEeqmILDSLAGAEAELAQQSQLVEELISDLERR 239
Cdd:TIGR02169  258 EEISE---LEKRLEEIEQLLEELNKKIKDLGEEEQLR 291
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 141-241 1.04e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402  141 ENLQEALKRLRKEQEKVETFEADIKEDRiswkhQIQTER-QRIQTGY-----------NQLRRIldKEEQNELKR----L 204
Cdd:pfam07926   4 SSLQSEIKRLKEEAADAEAQLQKLQEDL-----EKQAEIaREAQQNYerelvlhaediKALQAL--REELNELKAeiaeL 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 451770402  205 REEEQMILDSLAGAEAELAQQSQLVEELISDLERRCE 241
Cdd:pfam07926  77 KAEAESAKAELEESEESWEEQKKELEKELSELEKRIE 113
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
 292-456 1.07e-03

PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM9 proteins. TRIM9 protein is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. It has been shown that TRIM9 is localized to the neurons in the normal human brain and its immunoreactivity in affected brain areas in Parkinson's disease and dementia with Lewy bodies is severely decreased, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis.


Pssm-ID: 293947  Cd Length: 172  Bit Score: 39.92  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 292 LTAVRAYWadFTFNPENLNLNLILSEDHRQVTsvpiwpfkcCNNG----ILGSKCFLSGKHYWEVDVSEKNAWT---LGV 364
Cdd:cd12889    2 LQTAEVAW--FTFDPSTSHPDIILSNDNMTVT---------CNSYedrvVLGSVGFSRGVHYWEVTIDRYDGHPdpaFGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 365 ysrkrtLKFDVRRCSK--SQPNGYHRYKPQNGYWVigLQDGSKYSIFEDSSNCGPTvlnpfvatplhrIGVFLDCEEGIV 442
Cdd:cd12889   71 ------ARIDVNKDKMlgKDDKGWSMYIDNNRSWF--LHNNEHSNRTEGGITVGSV------------VGVLLDLDRHTL 130

                        170
                 ....*....|....*
gi 451770402 443 SFF-NVTNHGSLIYK 456
Cdd:cd12889  131 SFYvNDEPQGPIAFR 145
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 134-225 1.10e-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: 41.29  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 134 EAVRECQENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRIldkeeQNELKRLREEEQMILD 213
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-----EAELAELEKEIAELRA 97

                         90
                 ....*....|..
gi 451770402 214 SLAGAEAELAQQ 225
Cdd:COG4942   98 ELEAQKEELAEL 109
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 140-239 1.28e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 140 QENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRILDKEEQNELKRLREEEQMILDSLAGAE 219
Cdd:COG1196  677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756

                         90       100
                 ....*....|....*....|
gi 451770402 220 AELAQQSQLvEELISDLERR 239
Cdd:COG1196  757 PEPPDLEEL-ERELERLERE 775
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
140-256 1.45e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 140 QENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRILDKEEQNELKRLREE-EQMILDSLAGA 218
Cdd:COG4372  124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEaNRNAEKEEELA 203

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 451770402 219 EAELAQQSQLVEELISDLERRCEWSDTELLQDVSGILK 256
Cdd:COG4372  204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
125-256 1.78e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 125 RGHHTFLRDEAVRECQENLQEA------LKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQ-----TGYNQLRRIL 193
Cdd:COG4717   62 QGRKPELNLKELKELEEELKEAeekeeeYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAEL 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 451770402 194 dKEEQNELKRLREEEQmildSLAGAEAELAQQSQLVEELISDLERRCEWSDTELLQDVSGILK 256
Cdd:COG4717  142 -AELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
 10-83 1.96e-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: 37.66  E-value: 1.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 451770402  10 QKEATCPVCHVLLIKPLNLGSGHHVSQACLTvkkTAVTNPRGKSLCPMCGNRFSFENLQANKHLADVVERLREV 83
Cdd:cd16498   14 QKNLECPICLELLKEPVSTKCDHQFCRFCIL---KLLQKKKKPAPCPLCKKSVTKRSLQESTRFKQLVEAVKKL 84
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-239 2.15e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402  131 LRDEAVRECQENLQEALKRLRKEQEKVETFEADIKE--------------DRI-SWKHQIQT------ERQRIQTGYNQL 189
Cdd:COG4913   288 RRLELLEAELEELRAELARLEAELERLEARLDALREeldeleaqirgnggDRLeQLEREIERlereleERERRRARLEAL 367

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 451770402  190 RRILD---KEEQNELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLERR 239
Cdd:COG4913   368 LAALGlplPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 118-238 2.25e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   118 CERSQEHRGHHTFLRD---EAVRECQENLQEALKRLRKEQEKVETFEADIKEDRISwKHQIQTERQRIQtgyNQLRRILD 194
Cdd:TIGR02168  868 IEELESELEALLNERAsleEALALLRSELEELSEELRELESKRSELRRELEELREK-LAQLELRLEGLE---VRIDNLQE 943

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 451770402   195 keeqnelkRLREEEQMILDSLAGAEAELAQQSQLVEELISDLER 238
Cdd:TIGR02168  944 --------RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
119-238 2.34e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 119 ERSQEHRGHHTFLRD-EAVRECQENLQEALKRLRKEQEKVETFEADIKEdRISWKHQIQTERQRIQTGYNQLRRILD--- 194
Cdd:COG4717  109 AELEELREELEKLEKlLQLLPLYQELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLEqls 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 451770402 195 -------KEEQNELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLER 238
Cdd:COG4717  188 lateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 301-356 2.57e-03

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


Pssm-ID: 293936  Cd Length: 185  Bit Score: 39.07  E-value: 2.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 451770402 301 DFTFNPENLNLNLILSEDHRQVTSVPIWpfKCCNNGILGSKCFLSGKHYWEVDVSE 356
Cdd:cd12876    1 EWTWDERDKSPAVQLSDNNREVYFHPDY--SCGTAAVRGTKPLTNGQHYWEIKMSS 54
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 140-237 2.84e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 140 QENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRILDKEEQNELKRLREEEQmiLDSLAGAE 219
Cdd:COG1196  409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--LAELLEEL 486

                         90
                 ....*....|....*...
gi 451770402 220 AELAQQSQLVEELISDLE 237
Cdd:COG1196  487 AEAAARLLLLLEAEADYE 504
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 133-252 3.36e-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: 40.05  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   133 DEAVRECQENLQEALKRLRK-------EQEKVETFEADIKE---DRISWKHQIQTERQRIQTGYNQL------------- 189
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKleaeidkLLAEIEELEREIEEerkRRDKLTEEYAELKEELEDLRAELeevdkefaetrde 386

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 451770402   190 ----RRILD--KEEQNELK----RLREEEQMILDSLAGAEAELAQQSQLVEELISDLE------RRCEWSDTELLQDVS 252
Cdd:TIGR02169  387 lkdyREKLEklKREINELKreldRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdkaleiKKQEWKLEQLAADLS 465
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 134-241 3.39e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 3.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   134 EAVRECQENLQEALKRLRKEQEKVETFEADIKEDRiswkHQIQTERQRIQTGYNQLRRIldKEEQNELKRLREEEQMILD 213
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQLE----LQIASLNNEIERLEARLERL--EDRRERLQQEIEELLKKLE 431

                           90       100       110
                   ....*....|....*....|....*....|
gi 451770402   214 SLAGAE--AELAQQSQLVEELISDLERRCE 241
Cdd:TIGR02168  432 EAELKElqAELEELEEELEELQEELERLEE 461
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
118-247 3.44e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 118 CERSQEHRGHHTFLRDEAVRECQENLQEALKRL---RKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQ---LR- 190
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAgldDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaesLRe 349

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 191 RILDKEEQNelKRLREEEQMILDSLAGAEAELAQQSQLVEEL---ISDLERRCEWSDTEL 247
Cdd:PRK02224 350 DADDLEERA--EELREEAAELESELEEAREAVEDRREEIEELeeeIEELRERFGDAPVDL 407
Bbox2_TRIM65-like cd19793
B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65), B box and ...
 94-134 3.57e-03

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: 35.36  E-value: 3.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 451770402  94 DLCVHHGEKLLLFCQEDKKVICWVCERSQEHRGHHTFLRDE 134
Cdd:cd19793    1 ELCPEHGRELELYCRTEKRCVCAQCASKGECRGHRVTLLEE 41
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 134-227 3.60e-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: 39.75  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 134 EAVRECQENLQEALKRLRKEQEKVETFEADIKEDriswKHQIQTERQRIQTGYNQLRRILD------KEEQNELKRLREE 207
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEAL----LAELEEERAALEALKAERQKLLArlekelAELAAELAELQQE 221

                         90       100
                 ....*....|....*....|
gi 451770402 208 EQMILDSLAGAEAELAQQSQ 227
Cdd:COG4942  222 AEELEALIARLEAEAAAAAE 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 119-249 3.69e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 3.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402   119 ERSQEHRghhtfLRDEAVRECQENLQEALKRLRKEQEKVETFEADIKEDRiswkHQIQTERQRIQTGYNQLRRILDkEEQ 198
Cdd:TIGR02168  267 EKLEELR-----LEVSELEEEIEELQKELYALANEISRLEQQKQILRERL----ANLERQLEELEAQLEELESKLD-ELA 336

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 451770402   199 NELKRLREEEQMILDSLAGAEAELAQQSQLVEElisdLERRCEWSDTELLQ 249
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELEE----LESRLEELEEQLET 383
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 134-252 3.80e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.94  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 134 EAVRECQENLQEALKRLRKEQEKVETFEADIKEDRI----------------SWKHQIQTERQRI----QTGYNQLRRIL 193
Cdd:COG5185  329 ESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIEnivgevelsksseeldSFKDTIESTKESLdeipQNQRGYAQEIL 408

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 451770402 194 DKEEQNELKRLREEEQMILDsLAGAEAELAQQSQLVEELISDLERRCEWSDTELLQDVS 252
Cdd:COG5185  409 ATLEDTLKAADRQIEELQRQ-IEQATSSNEEVSKLLNELISELNKVMREADEESQSRLE 466
Bbox2_TRIM65_C-IV cd19835
B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65) and similar ...
 95-134 5.00e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65) and similar proteins; 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. TRIM65 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, 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: 380893 [Multi-domain]  Cd Length: 42  Bit Score: 34.71  E-value: 5.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 451770402  95 LCVHHGEKLLLFCQEDKKVICWVCErSQEHRGHHTFLRDE 134
Cdd:cd19835    2 LCQRHGRPLELYCRTEKRCVCCKCT-VKECRNHNRVLLEE 40
Bbox2_TRIM13_C-XI cd19767
B-box-type 2 zinc finger found in tripartite motif-containing protein 13 (TRIM13) and similar ...
 97-127 5.42e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 13 (TRIM13) and similar proteins; TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane-anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). It also targets the known ER proteolytic substrate CD3-delta, but not the N-end rule substrate Ub-R-YFP (yellow fluorescent protein) for its degradation. Moreover, TRIM13 regulates ubiquitination and degradation of NEMO to suppress tumor necrosis factor (TNF) induced nuclear factor-kappaB (NF- kappa B) activation. It is also involved in NF-kappaB p65 activation and nuclear factor of activated T-cells (NFAT)-dependent activation of c-Rel upon T-cell receptor engagement. Furthermore, TRIM13 negatively regulates lanoma differentiation-associated gene 5 (MDA5)-mediated type I interferon production. It also regulates caspase-8 ubiquitination, translocation to autophagosomes, and activation during ER stress induced cell death. Meanwhile, TRIM13 enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. TRIM13 belongs to the C-XI subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region. In addition, TRIM13 contains a C-terminal transmembrane domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380825  Cd Length: 42  Bit Score: 34.81  E-value: 5.42e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 451770402  97 VHHGEKLLLFCQEDKKVICWVCERSQEHRGH 127
Cdd:cd19767    5 VHSGQPLNIFCSTDLKLICGFCATMGDHKKH 35
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 132-231 5.84e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.29  E-value: 5.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 132 RDEAVRECQENLQEALKRLRKEqekvetfEADIKEDRISWKHQIQTERQRIQtgynQLRRILDKEEQNELKRLREEEQmi 211
Cdd:COG0542  427 KEALKKEQDEASFERLAELRDE-------LAELEEELEALKARWEAEKELIE----EIQELKEELEQRYGKIPELEKE-- 493

                         90       100
                 ....*....|....*....|
gi 451770402 212 ldsLAGAEAELAQQSQLVEE 231
Cdd:COG0542  494 ---LAELEEELAELAPLLRE 510
Bbox2_TRIM59_C-XI cd19790
B-box-type 2 zinc finger found in tripartite motif-containing protein 59 (TRIM59) and similar ...
 98-127 5.93e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 59 (TRIM59) and similar proteins; TRIM59, also known as TRIM57, or RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis. It is upregulated in gastric cancer and promotes gastric carcinogenesis by interacting with and targeting the P53 tumor suppressor for its ubiquitination and degradation. It also acts as a novel accessory molecule involved in cytotoxicity of BCG-activated macrophages (BAM). Moreover, TRIM59 may serve as a multifunctional regulator for innate immune signaling pathways. It interacts with ECSIT and negatively regulates nuclear factor-kappaB (NF- kappa B) and interferon regulatory factor (IRF)-3/7-mediated signal pathways. TRIM59 belongs to the C-XI subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region. In addition, TRIM59 contains a C-terminal transmembrane domain.


Pssm-ID: 380848 [Multi-domain]  Cd Length: 40  Bit Score: 34.74  E-value: 5.93e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 451770402  98 HHGEKLLLFCQEDKKVICWVCERSQEHRGH 127
Cdd:cd19790    6 HYRQPLNLFCLLDRKLICGQCLTVGQHQGH 35
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 131-237 7.05e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 37.62  E-value: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 131 LRDEAVRECQENLQEALKRLRKEQEK-VETFEADIKEDRiswkhqiqteRQRIQTGYNQLRRILDKEEQNELKRLREEEQ 209
Cdd:COG1390   22 ILEEAEEEAEKILEEAEEEAEEIKEEiLEKAEREAEREK----------RRIISSAELEARKELLEAKEELIEEVFEEAL 91

                         90       100
                 ....*....|....*....|....*...
gi 451770402 210 MILDSLAGAEAELAQQSQLVEELISDLE 237
Cdd:COG1390   92 EKLKNLPKDPEYKELLKKLLKEAAEELG 119
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 134-247 7.50e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 134 EAVRECQENLQEALKRLRKEQEKVETFEADIKEDRISwKHQIQTERQRIQTgynQLRRILDKEEQNELKRLREEEQMILd 213
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEE---ELAELEEELEELEEELEELEEELEE- 348

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 451770402 214 slAGAEAELAQQ--SQLVEELISDLERRCEWSDTEL 247
Cdd:COG1196  349 --AEEELEEAEAelAEAEEALLEAEAELAEAEEELE 382
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
134-239 7.80e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 7.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451770402 134 EAVRECQENLQEALKRLRKEQEKVETFEADIKEDRISWKHQIQTERQRIQTGYNQLRRILDKEEQNELKRLREEEQMILD 213
Cdd:COG4372  104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183

                         90       100
                 ....*....|....*....|....*.
gi 451770402 214 SLAGAEAELAQQSQLVEELISDLERR 239
Cdd:COG4372  184 ALDELLKEANRNAEKEEELAEAEKLI 209
 
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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