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Conserved domains on  [gi|24899214|dbj|BAC23121|]
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KIAA2025 protein, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ROQ_II pfam18386
Roquin II domain; The ROQ domain is composed of three subdomains, I, II and III. This entry ...
 247-302 1.34e-30

Roquin II domain; The ROQ domain is composed of three subdomains, I, II and III. This entry describes the second domain, ROQ II. Structural analysis reveals similarity of domain II to the helix-turn-helix (HTH) fold. Mutagenesis and biochemical studies show that that the HTH fold in domain II contributes to binding dsRNA at the 5'arm.


:

Pssm-ID: 436456  Cd Length: 56  Bit Score: 114.63  E-value: 1.34e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24899214    247 EEFRTYEALRREHDSQIVQIAMEAGLRIAPDQWSSLLYGDQSHKSHMQSIIDKLQT 302
Cdd:pfam18386    1 DEFRSYEALRREHDAQIVQIAFEYGLRISPEQWSALLYGDQAHRSHMQSIIDKLQS 56
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 1-30 5.77e-17

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 cd16638:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 44  Bit Score: 75.46  E-value: 5.77e-17
                         10        20        30
                 ....*....|....*....|....*....|
gi 24899214    1 IRKPISLGCGHTVCKMCLNKLHRKACPFDQ 30
Cdd:cd16638   15 QRKPISLGCGHTVCKTCLSKLHRKQCPFDQ 44
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 470-703 2.39e-05

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.54  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   470 PNGIVSTGNTVTQLIPRGTDPSYDSSLKPGkidhlSSSAPGSPPDLLESVPKSISALPV---NPHSIPPRGPADLPPMPV 546
Cdd:PRK10263  319 PVAVAAAATTATQSWAAPVEPVTQTPPVAS-----VDVPPAQPTVAWQPVPGPQTGEPViapAPEGYPQQSQYAQPAVQY 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   547 TKPLQMVPRGSQLYPAQQTDVYYQDPRGAAPPFEPAPYQQGMYYTPPPQCVSRFVRPPPSAPEPAPPYLDHYPPYlQERV 626
Cdd:PRK10263  394 NEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTY-QQPA 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   627 VNSQYGTQPQQYPPiypshydgrrvypaPSYTREEifresPIPIEIPPAAVPSY----VPESRER-YQQIESYYPVAPHP 701
Cdd:PRK10263  473 AQEPLYQQPQPVEQ--------------QPVVEPE-----PVVEETKPARPPLYyfeeVEEKRAReREQLAAWYQPIPEP 533


                  ..
gi 24899214   702 TQ 703
Cdd:PRK10263  534 VK 535
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
390-416 1.21e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.87  E-value: 1.21e-04
                           10        20
                   ....*....|....*....|....*..
gi 24899214    390 YKTYMCRDMKQRGGCPRGASCTFAHSQ 416
Cdd:pfam00642    1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
 
Name Accession Description Interval E-value
ROQ_II pfam18386
Roquin II domain; The ROQ domain is composed of three subdomains, I, II and III. This entry ...
 247-302 1.34e-30

Roquin II domain; The ROQ domain is composed of three subdomains, I, II and III. This entry describes the second domain, ROQ II. Structural analysis reveals similarity of domain II to the helix-turn-helix (HTH) fold. Mutagenesis and biochemical studies show that that the HTH fold in domain II contributes to binding dsRNA at the 5'arm.


Pssm-ID: 436456  Cd Length: 56  Bit Score: 114.63  E-value: 1.34e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24899214    247 EEFRTYEALRREHDSQIVQIAMEAGLRIAPDQWSSLLYGDQSHKSHMQSIIDKLQT 302
Cdd:pfam18386    1 DEFRSYEALRREHDAQIVQIAFEYGLRISPEQWSALLYGDQAHRSHMQSIIDKLQS 56
mRING-HC-C3HC3D_Roquin cd16638
Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1, Roquin-2, and similar ...
 1-30 5.77e-17

Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1, Roquin-2, and similar proteins; The ROQUIN family includes Roquin-1, Roquin-2, and similar proteins, which localize to the cytoplasm and upon stress, are concentrated in stress granules. They may play essential roles in preventing T-cell-mediated autoimmune disease and in microRNA-mediated repression of inducible costimulator (Icos) mRNA. They function as E3 ubiquitin ligases consisting of an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 activity, a highly conserved ROQ domain required for RNA binding and localization to stress granules, and a CCCH-type zinc finger involved in RNA recognition.


Pssm-ID: 438300 [Multi-domain]  Cd Length: 44  Bit Score: 75.46  E-value: 5.77e-17
                         10        20        30
                 ....*....|....*....|....*....|
gi 24899214    1 IRKPISLGCGHTVCKMCLNKLHRKACPFDQ 30
Cdd:cd16638   15 QRKPISLGCGHTVCKTCLSKLHRKQCPFDQ 44
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 470-703 2.39e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.54  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   470 PNGIVSTGNTVTQLIPRGTDPSYDSSLKPGkidhlSSSAPGSPPDLLESVPKSISALPV---NPHSIPPRGPADLPPMPV 546
Cdd:PRK10263  319 PVAVAAAATTATQSWAAPVEPVTQTPPVAS-----VDVPPAQPTVAWQPVPGPQTGEPViapAPEGYPQQSQYAQPAVQY 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   547 TKPLQMVPRGSQLYPAQQTDVYYQDPRGAAPPFEPAPYQQGMYYTPPPQCVSRFVRPPPSAPEPAPPYLDHYPPYlQERV 626
Cdd:PRK10263  394 NEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTY-QQPA 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   627 VNSQYGTQPQQYPPiypshydgrrvypaPSYTREEifresPIPIEIPPAAVPSY----VPESRER-YQQIESYYPVAPHP 701
Cdd:PRK10263  473 AQEPLYQQPQPVEQ--------------QPVVEPE-----PVVEETKPARPPLYyfeeVEEKRAReREQLAAWYQPIPEP 533


                  ..
gi 24899214   702 TQ 703
Cdd:PRK10263  534 VK 535
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
390-416 1.21e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.87  E-value: 1.21e-04
                           10        20
                   ....*....|....*....|....*..
gi 24899214    390 YKTYMCRDMKQRGGCPRGASCTFAHSQ 416
Cdd:pfam00642    1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 1-28 2.33e-03

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


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 36.72  E-value: 2.33e-03
                            10        20        30
                    ....*....|....*....|....*....|.
gi 24899214       1 IRKPISLGCGHTVCKMCLNKL---HRKACPF 28
Cdd:smart00184    9 LKDPVILPCGHTFCRSCIRKWlesGNNTCPI 39
ZnF_C3H1 smart00356
zinc finger;
389-415 5.68e-03

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 35.30  E-value: 5.68e-03
                            10        20
                    ....*....|....*....|....*..
gi 24899214     389 KYKTYMCRDMKqRGGCPRGASCTFAHS 415
Cdd:smart00356    1 KYKTELCKFFK-RGYCPRGDRCKFAHP 26
zf-RING_5 pfam14634
zinc-RING finger domain;
2-31 7.82e-03

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 35.48  E-value: 7.82e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 24899214      2 RKPISLGCGHTVCKMCLNKLHRKA-CPFDQT 31
Cdd:pfam14634   13 RPFYLTSCGHIFCEECLTRLLQERqCPICKK 43
 
Name Accession Description Interval E-value
ROQ_II pfam18386
Roquin II domain; The ROQ domain is composed of three subdomains, I, II and III. This entry ...
 247-302 1.34e-30

Roquin II domain; The ROQ domain is composed of three subdomains, I, II and III. This entry describes the second domain, ROQ II. Structural analysis reveals similarity of domain II to the helix-turn-helix (HTH) fold. Mutagenesis and biochemical studies show that that the HTH fold in domain II contributes to binding dsRNA at the 5'arm.


Pssm-ID: 436456  Cd Length: 56  Bit Score: 114.63  E-value: 1.34e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24899214    247 EEFRTYEALRREHDSQIVQIAMEAGLRIAPDQWSSLLYGDQSHKSHMQSIIDKLQT 302
Cdd:pfam18386    1 DEFRSYEALRREHDAQIVQIAFEYGLRISPEQWSALLYGDQAHRSHMQSIIDKLQS 56
mRING-HC-C3HC3D_Roquin cd16638
Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1, Roquin-2, and similar ...
 1-30 5.77e-17

Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1, Roquin-2, and similar proteins; The ROQUIN family includes Roquin-1, Roquin-2, and similar proteins, which localize to the cytoplasm and upon stress, are concentrated in stress granules. They may play essential roles in preventing T-cell-mediated autoimmune disease and in microRNA-mediated repression of inducible costimulator (Icos) mRNA. They function as E3 ubiquitin ligases consisting of an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 activity, a highly conserved ROQ domain required for RNA binding and localization to stress granules, and a CCCH-type zinc finger involved in RNA recognition.


Pssm-ID: 438300 [Multi-domain]  Cd Length: 44  Bit Score: 75.46  E-value: 5.77e-17
                         10        20        30
                 ....*....|....*....|....*....|
gi 24899214    1 IRKPISLGCGHTVCKMCLNKLHRKACPFDQ 30
Cdd:cd16638   15 QRKPISLGCGHTVCKTCLSKLHRKQCPFDQ 44
mRING-HC-C3HC3D_Roquin1 cd16781
Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1; Roquin-1, also known as ...
 1-30 6.16e-17

Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1; Roquin-1, also known as RING finger and C3H zinc finger protein 1 (RC3H1), or RING finger protein 198 (RNF198), is a ubiquitously expressed RNA-binding protein essential for degradation of inflammation-related mRNAs and maintenance of immune homeostasis. It is localized in cytoplasmic granules and binds to the 3' untranslated region (3'UTR) of inducible costimulator (Icos) mRNA to post-transcriptionally repress its expression. Roquin-1 interacts with the 3'UTR of tumor necrosis factor receptor superfamily member 4 (TNFRSF4) and tumor-necrosis factor-alpha (TNFalpha), and post-transcriptionally regulates A20 mRNA and modulates the activity of the IKK/NF-kappaB pathway. Moreover, Roquin-1 shares functions with its paralog Roquin-2 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation. Roquin-1 contains an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 ubiquitin-ligase function, a highly conserved ROQ domain required for RNA binding and localization to stress granules, and a CCCH-type zinc finger that is involved in RNA recognition, typically contacting AU-rich elements. In addition, both N- and C-terminal to the ROQ domain are combined to form a HEPN (higher eukaryotes and prokaryotes nucleotide-binding) domain that is highly likely to function as an RNA-binding domain.


Pssm-ID: 438436 [Multi-domain]  Cd Length: 49  Bit Score: 75.43  E-value: 6.16e-17
                         10        20        30
                 ....*....|....*....|....*....|
gi 24899214    1 IRKPISLGCGHTVCKMCLNKLHRKACPFDQ 30
Cdd:cd16781   20 IRKPISLGCGHTVCKMCLNKLHRKACPFDQ 49
mRING-HC-C3HC3D_Roquin2 cd16782
Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-2; Roquin-2, also known as ...
 1-31 4.97e-14

Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-2; Roquin-2, also known as membrane-associated nucleic acid-binding protein (MNAB), RING finger and CCCH-type zinc finger domain-containing protein 2 (RC3H2), or RING finger protein 164 (RNF164), is an E3 ubiquitin ligase that is localized to the cytoplasm and upon stress, is concentrated in stress granules. It is required for reactive oxygen species (ROS)-induced ubiquitination and degradation of apoptosis signal-regulating kinase 1 (ASK1, also known as MAP3K5). Roquin-2 interacts with the 3'UTR of tumor necrosis factor receptor superfamily member 4 (TNFRSF4) and tumor-necrosis factor-alpha (TNFalpha), and modulates immune responses. Moreover, Roquin-2 shares functions with its paralog Roquin-1 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation. Roquin-2 contains an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 ubiquitin-ligase function, a highly conserved ROQ domain required for RNA binding and localization to stress granules, a coiled-coil (CC1), and a CCCH-type zinc finger that is involved in RNA recognition.


Pssm-ID: 438437  Cd Length: 49  Bit Score: 67.43  E-value: 4.97e-14
                         10        20        30
                 ....*....|....*....|....*....|.
gi 24899214    1 IRKPISLGCGHTVCKMCLNKLHRKACPFDQT 31
Cdd:cd16782   19 VHKPISLGCSHTVCKTCLNKLHRKACPFDQT 49
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 470-703 2.39e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.54  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   470 PNGIVSTGNTVTQLIPRGTDPSYDSSLKPGkidhlSSSAPGSPPDLLESVPKSISALPV---NPHSIPPRGPADLPPMPV 546
Cdd:PRK10263  319 PVAVAAAATTATQSWAAPVEPVTQTPPVAS-----VDVPPAQPTVAWQPVPGPQTGEPViapAPEGYPQQSQYAQPAVQY 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   547 TKPLQMVPRGSQLYPAQQTDVYYQDPRGAAPPFEPAPYQQGMYYTPPPQCVSRFVRPPPSAPEPAPPYLDHYPPYlQERV 626
Cdd:PRK10263  394 NEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTY-QQPA 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   627 VNSQYGTQPQQYPPiypshydgrrvypaPSYTREEifresPIPIEIPPAAVPSY----VPESRER-YQQIESYYPVAPHP 701
Cdd:PRK10263  473 AQEPLYQQPQPVEQ--------------QPVVEPE-----PVVEETKPARPPLYyfeeVEEKRAReREQLAAWYQPIPEP 533


                  ..
gi 24899214   702 TQ 703
Cdd:PRK10263  534 VK 535
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
390-416 1.21e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.87  E-value: 1.21e-04
                           10        20
                   ....*....|....*....|....*..
gi 24899214    390 YKTYMCRDMKQRGGCPRGASCTFAHSQ 416
Cdd:pfam00642    1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
RING-HC_TRIM32_C-VII cd16587
RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar ...
 2-28 1.72e-03

RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar proteins; TRIM32, also known as 72 kDa Tat-interacting protein, zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation by modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binds specifically to the activation domain of HIV-1 Tat, and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs.


Pssm-ID: 438249 [Multi-domain]  Cd Length: 51  Bit Score: 37.38  E-value: 1.72e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 24899214    2 RKPISLGCGHTVCKMCLNKLHRKA------CPF 28
Cdd:cd16587   15 LRPKLLHCGHTICEQCLEKLLASLsingvrCPF 47
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 2-29 1.86e-03

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 37.08  E-value: 1.86e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 24899214    2 RKPISLGCGHTVCKMCLNKL---HRKACPFD 29
Cdd:cd16449   11 KDPVLLPCGHVFCRECIRRLlesGSIKCPIC 41
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 1-28 2.33e-03

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


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 36.72  E-value: 2.33e-03
                            10        20        30
                    ....*....|....*....|....*....|.
gi 24899214       1 IRKPISLGCGHTVCKMCLNKL---HRKACPF 28
Cdd:smart00184    9 LKDPVILPCGHTFCRSCIRKWlesGNNTCPI 39
mRING-HC-C3HC3D_arc-1-like cd23124
Modified RING finger, HC subclass (C3HC3D-type), found in Caenorhabditis elegans putative ...
 8-31 2.39e-03

Modified RING finger, HC subclass (C3HC3D-type), found in Caenorhabditis elegans putative GTP-binding protein trim-23 homolog (arc-1) and similar proteins; arc-1, also called RING-type E3 ubiquitin transferase arc-1, is an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. arc-1 contains a modified C3HC3D-type RING-HC finger.


Pssm-ID: 438486 [Multi-domain]  Cd Length: 55  Bit Score: 37.09  E-value: 2.39e-03
                         10        20
                 ....*....|....*....|....*....
gi 24899214    8 GCGHTVCKMCLNKLHRK-----ACPFDQT 31
Cdd:cd23124   25 ECGHTICTNCAGTILGQssgsiFCPFDRI 53
mRING-HC-C3HC3D_TRAF6 cd16643
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 1-45 5.23e-03

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


Pssm-ID: 438305 [Multi-domain]  Cd Length: 58  Bit Score: 36.20  E-value: 5.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 24899214    1 IRKPISLGCGHTVCKMCLNKLHRKA---CPFDQTTInTDIELLPVNSA 45
Cdd:cd16643   11 LREPVQTPCGHRFCKACILKSIREAghkCPVDNEPL-LENQLFPDNFA 57
RING-HC_LONFs_rpt1 cd16513
first RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
 1-26 5.44e-03

first RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger protein family; The LON peptidase N-terminal domain and RING finger protein family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192, RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and an ATP-dependent protease La (LON) substrate-binding domain at the C-terminus. Their biological functions remain unclear. This model corresponds to the first RING-HC finger.


Pssm-ID: 438176 [Multi-domain]  Cd Length: 47  Bit Score: 35.75  E-value: 5.44e-03
                         10        20
                 ....*....|....*....|....*.
gi 24899214    1 IRKPISLGCGHTVCKMCLNKLHRKAC 26
Cdd:cd16513   12 LFEPVTLPCGHTFCKRCLERDPSSRC 37
RING-HC_KEG-like cd23140
RING finger, HC subclass, found in Arabidopsis thaliana protein KEEP ON GOING (KEG) and ...
 2-31 5.54e-03

RING finger, HC subclass, found in Arabidopsis thaliana protein KEEP ON GOING (KEG) and similar proteins; KEG, also called RING-type E3 ubiquitin transferase KEG, is a RING E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. It is essential for Arabidopsis growth and development. It acts as a negative regulator of abscisic acid signaling. It is required for ABSCISIC ACID-INSENSITIVE5 (ABI5) degradation, by mediating its ubiquitination. Together with EDR1, KEG may regulate endocytic trafficking and/or the formation of signaling complexes on trans-Golgi network (TGN)/ early endosome (EE) vesicles during stress responses. KEG is a multidomain protein that includes a C3HC4-type RING-HC finger, a kinase domain, ankyrin repeats, and 12 HERC2-like (for HECT and RCC1-like) repeats.


Pssm-ID: 438502 [Multi-domain]  Cd Length: 57  Bit Score: 36.08  E-value: 5.54e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 24899214    2 RKPISLGCGHTVCKMCLNKLHRKACPFDQT 31
Cdd:cd23140   16 RVPLLLQCGHTFCKDCLSQMFIRCTDLTLK 45
ZnF_C3H1 smart00356
zinc finger;
389-415 5.68e-03

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 35.30  E-value: 5.68e-03
                            10        20
                    ....*....|....*....|....*..
gi 24899214     389 KYKTYMCRDMKqRGGCPRGASCTFAHS 415
Cdd:smart00356    1 KYKTELCKFFK-RGYCPRGDRCKFAHP 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 447-679 7.66e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   447 LPSAAILPDEGAVDlPSRKPPALPNGIVSTGNTVTQLIPRGTDPSYDSSLKPGKIDHLSSSAPGSPPdllesVPKSISAL 526
Cdd:PHA03247 2762 TTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-----LPPPTSAQ 2835

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   527 PVNPHSIPP--------------------RGPADLPP-MPVTKPLQMVPRGSQLYPAQQTDVYYQDPRGAAPPFEPAPYQ 585
Cdd:PHA03247 2836 PTAPPPPPGppppslplggsvapggdvrrRPPSRSPAaKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP 2915

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   586 QGMYYTPPPQCVSRFVRPPPSAPEpappyldhyPPYLQervvnSQYGTQPQQYP-PIYPSHYDGRRVYPAPSYTREEIFR 664
Cdd:PHA03247 2916 PPQPQPQPPPPPQPQPPPPPPPRP---------QPPLA-----PTTDPAGAGEPsGAVPQPWLGALVPGRVAVPRFRVPQ 2981

                         250
                  ....*....|....*
gi 24899214   665 ESPiPIEIPPAAVPS 679
Cdd:PHA03247 2982 PAP-SREAPASSTPP 2995
zf-RING_5 pfam14634
zinc-RING finger domain;
2-31 7.82e-03

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 35.48  E-value: 7.82e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 24899214      2 RKPISLGCGHTVCKMCLNKLHRKA-CPFDQT 31
Cdd:pfam14634   13 RPFYLTSCGHIFCEECLTRLLQERqCPICKK 43
RING-HC_TRIM41-like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
 1-27 8.17e-03

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins; TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 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. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of the TRIM family that contains only RBCC domains. 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.


Pssm-ID: 438264 [Multi-domain]  Cd Length: 53  Bit Score: 35.67  E-value: 8.17e-03
                         10        20
                 ....*....|....*....|....*..
gi 24899214    1 IRKPISLGCGHTVCKMCLNKLHRKACP 27
Cdd:cd16602   13 FKDPVSIGCGHNFCRVCVTQLWGFTCP 39
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 416-761 8.47e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   416 QEELEKFRKMNKRLVPRRPL----SASLGQLNEVGLPSAAILPDEGAVDLPSRKPPALPNGIVSTGNtvtqlipRGTDPS 491
Cdd:PRK10263  231 QHESRRARILRGALARRKRLaekfINPMGRQTDAALFSGKRMDDDEEITYTARGVAADPDDVLFSGN-------RATQPE 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   492 YDsslkpgKIDHLSSSAPGSPPdlLESVPKSISALPVNPHSIPPRGPAdlPPMPVTKPlqmvprgsqlyPAQQTDVYYQD 571
Cdd:PRK10263  304 YD------EYDPLLNGAPITEP--VAVAAAATTATQSWAAPVEPVTQT--PPVASVDV-----------PPAQPTVAWQP 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   572 ---PRGAAPPFEPAPYQqgmyYTPPPQcvsrfvrPPPSAPEPAPPYLDHYPPYLQERVVNSQYGTQPQQYPPIYPSHYDG 648
Cdd:PRK10263  363 vpgPQTGEPVIAPAPEG----YPQQSQ-------YAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQ 431

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24899214   649 RRVYPAPSYTREEIFRESPiPIEIPPAAVPSYVPESRERYQQIESYYPVAPHPTQIRPSYLREPPYSRLPPPPQPHPSLD 728
Cdd:PRK10263  432 PYYAPAPEQPVAGNAWQAE-EQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFE 510

                         330       340       350
                  ....*....|....*....|....*....|....
gi 24899214   729 ELHRRRKEIMAQLEE-RKVISPPPFAPSPTLPPT 761
Cdd:PRK10263  511 EVEEKRAREREQLAAwYQPIPEPVKEPEPIKSSL 544
 
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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