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Conserved domains on  [gi|2102106746|ref|XP_043766069|]
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BRCA1-associated RING domain protein 1 isoform X1 [Cervus elaphus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 28-113 2.30e-47

RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins; BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains at its C-terminus. The BRCT repeats bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage.


:

Pssm-ID: 438159 [Multi-domain]  Cd Length: 86  Bit Score: 162.50  E-value: 2.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746  28 AWAHSRAALDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGSGCPVCYTPAWIQDVKINRQLDSMIQLCSKLR 107
Cdd:cd16496     1 KWARTRAALDELENLLRCSRCASILKEPVTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLR 80


                  ....*.
gi 2102106746 108 NLLHGT 113
Cdd:cd16496    81 NLLNDN 86
BRCT_Bard1_rpt2 cd17720
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ...
 668-768 1.39e-45

second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain.


:

Pssm-ID: 349352  Cd Length: 101  Bit Score: 157.91  E-value: 1.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 668 LFDGCYFYFGGTFKHH-PKDNLIKLVAAGGGQVLIRKPKPDSDVTQTINTVAYhAKPDSDQRFCTQYIIYEDLSNHRPER 746
Cdd:cd17720     1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 2102106746 747 VRQGKVWVAPSSWFIDCVMSFE 768
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-546 1.80e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 1.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVK 500
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2102106746 501 NGHVDIVKLLLAYGASREAVNIFGLRPVDYADSKNMKSLLLLPEKK 546
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 569-640 9.68e-30

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


:

Pssm-ID: 349366  Cd Length: 80  Bit Score: 112.31  E-value: 9.68e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746 569 LIGSGLSSEQQKMLSELAAILKAKKCAEFDSTVTHVIVPGD---TVQSTLKYMLGILSGCWILKFEWVKACLQSK 640
Cdd:cd17734     3 LLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADergVCPRTMKYLMGILAGKWIVSFEWVEACLKAK 77
 
Name Accession Description Interval E-value
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 28-113 2.30e-47

RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins; BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains at its C-terminus. The BRCT repeats bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage.


Pssm-ID: 438159 [Multi-domain]  Cd Length: 86  Bit Score: 162.50  E-value: 2.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746  28 AWAHSRAALDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGSGCPVCYTPAWIQDVKINRQLDSMIQLCSKLR 107
Cdd:cd16496     1 KWARTRAALDELENLLRCSRCASILKEPVTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLR 80


                  ....*.
gi 2102106746 108 NLLHGT 113
Cdd:cd16496    81 NLLNDN 86
BRCT_Bard1_rpt2 cd17720
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ...
 668-768 1.39e-45

second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain.


Pssm-ID: 349352  Cd Length: 101  Bit Score: 157.91  E-value: 1.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 668 LFDGCYFYFGGTFKHH-PKDNLIKLVAAGGGQVLIRKPKPDSDVTQTINTVAYhAKPDSDQRFCTQYIIYEDLSNHRPER 746
Cdd:cd17720     1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 2102106746 747 VRQGKVWVAPSSWFIDCVMSFE 768
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
zf-RING_6 pfam14835
zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer ...
 36-100 1.61e-37

zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer tumour-suppressor BRCA1 interacts with multiple cognate proteins, including the RING protein BARD1. Proper function of the BRCA1 RING domain is critical, as evidenced by the many cancer-predisposing mutations found within this domain. A dimer is formed between the RING domains of BRCA1 and BARD1. The BRCA1-BARD1 structure provides a model for its ubiquitin ligase activity, illustrates how the BRCA1 RING domain can be involved in associations with multiple protein partners and provides a framework for understanding cancer-causing mutations at the molecular level. The corresponding BRCA1-RING domain is on family zf-C3HC4_2, pfam13923.


Pssm-ID: 434253 [Multi-domain]  Cd Length: 65  Bit Score: 134.02  E-value: 1.61e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746  36 LDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGSGCPVCYTPAWIQDVKINRQLDSMI 100
Cdd:pfam14835   1 LDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-546 1.80e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 1.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVK 500
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2102106746 501 NGHVDIVKLLLAYGASREAVNIFGLRPVDYADSKNMKSLLLLPEKK 546
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 569-640 9.68e-30

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


Pssm-ID: 349366  Cd Length: 80  Bit Score: 112.31  E-value: 9.68e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746 569 LIGSGLSSEQQKMLSELAAILKAKKCAEFDSTVTHVIVPGD---TVQSTLKYMLGILSGCWILKFEWVKACLQSK 640
Cdd:cd17734     3 LLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADergVCPRTMKYLMGILAGKWIVSFEWVEACLKAK 77
Ank_2 pfam12796
Ankyrin repeats (3 copies);
429-516 5.44e-27

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 105.20  E-value: 5.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 429 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTgyQNDSPLHDAVKNGHVDIVK 508
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 2102106746 509 LLLAYGAS 516
Cdd:pfam12796  79 LLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 422-521 6.29e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.78  E-value: 6.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 422 NHRGETLLHIA--SIKGDIP----------------SVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKAL 483
Cdd:PHA03100  138 NSDGENLLHLYleSNKIDLKilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2102106746 484 VNTTGYQNDSPLHDAVKNGHVDIVKLLLAYGASREAVN 521
Cdd:PHA03100  218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
BRCT smart00292
breast cancer carboxy-terminal domain;
570-637 1.92e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 51.99  E-value: 1.92e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102106746  570 IGSGLSSEQQKMLSELAAILKAKKCAEFDS-TVTHVIVpGDTVQSTLKYMLGILSGCWILKFEWVKACL 637
Cdd:smart00292  11 ITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIV-GSPEGGKLELLKAIALGIPIVKEEWLLDCL 78
BRCT smart00292
breast cancer carboxy-terminal domain;
666-764 9.05e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 46.98  E-value: 9.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746  666 PKLFDGCYFYFGGTFKHHPKDNLIKLVAAGGGQVLIRKPKPDsdvtqtintvayhakpdsdqrfcTQYIIYEDLSN--HR 743
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVGSPEGgkLE 57

                           90       100
                   ....*....|....*....|.
gi 2102106746  744 PERVRQGKVWVAPSSWFIDCV 764
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 426-516 1.07e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 426 ETLLHIASIKGDIPSVEYLLQNGS-DPNVKDHAGWTPLHEACNHGHLKVVELLLQH-KALVN--TTG--YQNDSPLHDAV 499
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNepMTSdlYQGETALHIAV 97

                          90
                  ....*....|....*..
gi 2102106746 500 KNGHVDIVKLLLAYGAS 516
Cdd:cd22192    98 VNQNLNLVRELIARGAD 114
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 458-485 1.34e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 45.27  E-value: 1.34e-06
                           10        20
                   ....*....|....*....|....*...
gi 2102106746  458 GWTPLHEACNHGHLKVVELLLQHKALVN 485
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 34-84 2.08e-05

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


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 47.69  E-value: 2.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2102106746  34 AALDRLEKLLRCSRCTNILREPVcLGGCEHIFCSNCVSDCIG--SGCPVCYTP 84
Cdd:TIGR00599  18 PSLYPLDTSLRCHICKDFFDVPV-LTSCSHTFCSLCIRRCLSnqPKCPLCRAE 69
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 45-81 1.23e-04

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


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 39.80  E-value: 1.23e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2102106746   45 CSRCTNILREPVCLGGCEHIFCSNCVSDCIGSG---CPVC 81
Cdd:smart00184   1 CPICLEEYLKDPVILPCGHTFCRSCIRKWLESGnntCPIC 40
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 665-774 3.04e-04

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 40.04  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 665 LPKLFDGCYFYFGgTFKHHPKDNLIKLVAAGGGQVlirkpkpdsdvTQTINTVAYHakpdsdqRFCTQYIIYEDLSNHRP 744
Cdd:pfam16589   1 LPNLFEPLRFYIN-AIPSPSRSKLKRLIEANGGTV-----------VDNINPAVYI-------VIAPYNKTDKLAENTKL 61

                          90       100       110
                  ....*....|....*....|....*....|
gi 2102106746 745 ERVRqgkvwvapSSWFIDCVMSFELLPLDN 774
Cdd:pfam16589  62 GVVS--------PQWIFDCVKKGKLLPLEN 83
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
35-84 5.11e-04

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 43.15  E-value: 5.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2102106746  35 ALDRLEKLLRCSRCTNILREPvCLGGCEHIFCSNCVSDCIGS--GCPVCYTP 84
Cdd:COG5432    18 SLKGLDSMLRCRICDCRISIP-CETTCGHTFCSLCIRRHLGTqpFCPVCRED 68
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 572-637 5.50e-04

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 39.20  E-value: 5.50e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2102106746 572 SGLSSEQQKMLSELAAILKAKKCAEFDSTVTHVIVPGDTvqstLKYMLGILSGCWILKFEWVKACL 637
Cdd:pfam00533  14 TGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEART----KKYLKAKELGIPIVTEEWLLDCI 75
 
Name Accession Description Interval E-value
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 28-113 2.30e-47

RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins; BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains at its C-terminus. The BRCT repeats bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage.


Pssm-ID: 438159 [Multi-domain]  Cd Length: 86  Bit Score: 162.50  E-value: 2.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746  28 AWAHSRAALDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGSGCPVCYTPAWIQDVKINRQLDSMIQLCSKLR 107
Cdd:cd16496     1 KWARTRAALDELENLLRCSRCASILKEPVTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLR 80


                  ....*.
gi 2102106746 108 NLLHGT 113
Cdd:cd16496    81 NLLNDN 86
BRCT_Bard1_rpt2 cd17720
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ...
 668-768 1.39e-45

second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain.


Pssm-ID: 349352  Cd Length: 101  Bit Score: 157.91  E-value: 1.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 668 LFDGCYFYFGGTFKHH-PKDNLIKLVAAGGGQVLIRKPKPDSDVTQTINTVAYhAKPDSDQRFCTQYIIYEDLSNHRPER 746
Cdd:cd17720     1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 2102106746 747 VRQGKVWVAPSSWFIDCVMSFE 768
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
zf-RING_6 pfam14835
zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer ...
 36-100 1.61e-37

zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer tumour-suppressor BRCA1 interacts with multiple cognate proteins, including the RING protein BARD1. Proper function of the BRCA1 RING domain is critical, as evidenced by the many cancer-predisposing mutations found within this domain. A dimer is formed between the RING domains of BRCA1 and BARD1. The BRCA1-BARD1 structure provides a model for its ubiquitin ligase activity, illustrates how the BRCA1 RING domain can be involved in associations with multiple protein partners and provides a framework for understanding cancer-causing mutations at the molecular level. The corresponding BRCA1-RING domain is on family zf-C3HC4_2, pfam13923.


Pssm-ID: 434253 [Multi-domain]  Cd Length: 65  Bit Score: 134.02  E-value: 1.61e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746  36 LDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGSGCPVCYTPAWIQDVKINRQLDSMI 100
Cdd:pfam14835   1 LDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-546 1.80e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 1.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVK 500
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2102106746 501 NGHVDIVKLLLAYGASREAVNIFGLRPVDYADSKNMKSLLLLPEKK 546
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-531 4.72e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.30  E-value: 4.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVK 500
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2102106746 501 NGHVDIVKLLLAYGASREAVNIFGLRPVDYA 531
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 569-640 9.68e-30

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


Pssm-ID: 349366  Cd Length: 80  Bit Score: 112.31  E-value: 9.68e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746 569 LIGSGLSSEQQKMLSELAAILKAKKCAEFDSTVTHVIVPGD---TVQSTLKYMLGILSGCWILKFEWVKACLQSK 640
Cdd:cd17734     3 LLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADergVCPRTMKYLMGILAGKWIVSFEWVEACLKAK 77
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-542 1.10e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.67  E-value: 1.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVK 500
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2102106746 501 NGHVDIVKLLLAYGASREAVNIFGLRPVDYADSKNMKSLLLL 542
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
Ank_2 pfam12796
Ankyrin repeats (3 copies);
429-516 5.44e-27

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 105.20  E-value: 5.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 429 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTgyQNDSPLHDAVKNGHVDIVK 508
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 2102106746 509 LLLAYGAS 516
Cdd:pfam12796  79 LLLEKGAD 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
418-535 4.88e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 4.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 418 AVKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHD 497
Cdd:COG0666    47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2102106746 498 AVKNGHVDIVKLLLAYGASREAVNIFGLRPVDYADSKN 535
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-526 9.14e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.40  E-value: 9.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVK 500
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                          90       100
                  ....*....|....*....|....*.
gi 2102106746 501 NGHVDIVKLLLAYGASREAVNIFGLR 526
Cdd:COG0666   262 AGAALIVKLLLLALLLLAAALLDLLT 287
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 422-521 6.29e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.78  E-value: 6.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 422 NHRGETLLHIA--SIKGDIP----------------SVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKAL 483
Cdd:PHA03100  138 NSDGENLLHLYleSNKIDLKilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2102106746 484 VNTTGYQNDSPLHDAVKNGHVDIVKLLLAYGASREAVN 521
Cdd:PHA03100  218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 567-650 5.02e-14

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene 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. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 68.53  E-value: 5.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 567 LALIGSGLSSEQQKMLSELAAILKAKKCAEFDSTVTHVIVPGDT---VQSTLKYMLGILSGCWILKFEWVKACLQSKGYE 643
Cdd:cd17735     1 MSMVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAelvCERTLKYFLGIAGRKWVVSYQWITQSIKEGKIL 80


                  ....*..
gi 2102106746 644 QEEKYEI 650
Cdd:cd17735    81 PEHDFEV 87
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 421-514 9.98e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.23  E-value: 9.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVK 500
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                          90
                  ....*....|....
gi 2102106746 501 NGHVDIVKLLLAYG 514
Cdd:PHA02874  200 YGDYACIKLLIDHG 213
Ank_2 pfam12796
Ankyrin repeats (3 copies);
421-487 1.04e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.04e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGsDPNVKDHaGWTPLHEACNHGHLKVVELLLQHKALVNTT 487
Cdd:pfam12796  26 QDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
427-478 1.39e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 65.76  E-value: 1.39e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2102106746 427 TLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLL 478
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
458-511 4.34e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 64.22  E-value: 4.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2102106746 458 GWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVKNGHVDIVKLLL 511
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 428-513 2.42e-12

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 70.31  E-value: 2.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 428 LLHIASiKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVKNGHVDIV 507
Cdd:PTZ00322   86 LCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                  ....*.
gi 2102106746 508 KLLLAY 513
Cdd:PTZ00322  165 QLLSRH 170
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 572-636 3.70e-12

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 61.99  E-value: 3.70e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746 572 SGLSSEQQKMLSELAAILKAKKCAEFDSTVTHVIVpgDTVQSTLKYMLGILSGCWILKFEWVKAC 636
Cdd:cd00027     6 SGLDDEEREELKKLIEALGGKVSESLSSKVTHLIA--KSPSGEKYYLAALAWGIPIVSPEWLLDC 68
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 433-545 7.49e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 7.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 433 SIKGDIpsVEYLLQNGSDPNVKD-HAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVKNGHVDIVKLLL 511
Cdd:PHA02878  144 IIEAEI--TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL 221

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2102106746 512 AYGASREAVNIFGLRPVDYADS--KNMKSLLLLPEK 545
Cdd:PHA02878  222 ENGASTDARDKCGNTPLHISVGycKDYDILKLLLEH 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 417-542 1.08e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.98  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 417 TAVKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLH 496
Cdd:PHA02878  160 INMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2102106746 497 DAVKN-GHVDIVKLLLAYGASREAVN-IFGLRPVDYADSKNMKSLLLL 542
Cdd:PHA02878  240 ISVGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSERKLKLLL 287
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 572-639 2.01e-11

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 60.30  E-value: 2.01e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102106746 572 SGLSSEQQKMLSELAAILK-AKKCAEFDSTVTHVIVPGDtvQSTLKYMLGILSGCWILKFEWVKACLQS 639
Cdd:cd17736     6 TSVHSEEQELLESVVKKLGgFRVEDSVTEKTTHVVVGSP--RRTLNVLLGIARGCWILSPDWVLESLEA 72
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
416-535 6.00e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 6.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 416 LTAVKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPL 495
Cdd:COG0666    12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2102106746 496 HDAVKNGHVDIVKLLLAYGASREAVNIFGLRPVDYADSKN 535
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
PHA03095 PHA03095
ankyrin-like protein; Provisional
 399-529 1.05e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 399 YRRMMCSPsatklwPVSLTAVKR--------NHRGE---TLLHI---ASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLH- 463
Cdd:PHA03095   16 YDYLLNAS------NVTVEEVRRllaagadvNFRGEygkTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHl 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2102106746 464 EACNHGHLKVVELLLQHKALVNTTGYQNDSPLHD--AVKNGHVDIVKLLLAYGASREAVNIFGLRPVD 529
Cdd:PHA03095   90 YLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 424-527 5.62e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 424 RGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVKNGH 503
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                          90       100
                  ....*....|....*....|....
gi 2102106746 504 VDIVKLLLAYGASreaVNIFGLRP 527
Cdd:PHA02875  181 IAICKMLLDSGAN---IDYFGKNG 201
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 429-531 7.68e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 7.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 429 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACnhGHLK---VVELLLQHKALVNTTGY-QNDSPLHDAVKNGhv 504
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdydILKLLLEHGVDVNAKSYiLGLTALHSSIKSE-- 280

                          90       100
                  ....*....|....*....|....*..
gi 2102106746 505 DIVKLLLAYGASREAVNIFGLRPVDYA 531
Cdd:PHA02878  281 RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 427-531 8.07e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 8.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 427 TLLHIAS-----IKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEA-CNH-GHLKVVELLLQHKALVNTTGYQNDSPLHDAV 499
Cdd:PHA03100   70 TPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAiSKKsNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2102106746 500 KNGHVDI------------------VKLLLAYGASREAVNIFGLRPVDYA 531
Cdd:PHA03100  150 ESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYA 199
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 416-540 3.44e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 416 LTAVK-RNHRGETLLHIASIKGDI--------PSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNT 486
Cdd:PHA02874   73 LTAIKiGAHDIIKLLIDNGVDTSIlpipciekDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2102106746 487 TGYQNDSPLHDAVKNGHVDIVKLLLAYGASREAVNIFGLRP----VDYADSKNMKSLL 540
Cdd:PHA02874  153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPlhnaAEYGDYACIKLLI 210
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 437-554 5.13e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 5.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 437 DIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQN-DSPLHDAVKNGHVDIVKLLLAYGA 515
Cdd:PHA02875   47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGA 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2102106746 516 SREAVNIFGLRPVDYA-DSKNMKSLLLLPEKKESSSTSHC 554
Cdd:PHA02875  127 DPDIPNTDKFSPLHLAvMMGDIKGIELLIDHKACLDIEDC 166
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 421-547 6.74e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 6.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHlKVVELLLQHKAlVNTTGYQNDSPLHDAVK 500
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNAS-INDQDIDGSTPLHHAIN 263

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2102106746 501 NG-HVDIVKLLLAYGASREAVNIFGLRPVDYAdsknMKSLLLLPEKKE 547
Cdd:PHA02874  264 PPcDIDIIDILLYHKADISIKDNKGENPIDTA----FKYINKDPVIKD 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 426-534 1.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 426 ETLLHIASIKGDIPSVEYLLQNGSDPN-VKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVKNGHV 504
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                          90       100       110
                  ....*....|....*....|....*....|
gi 2102106746 505 DIVKLLLAYGASREAVNIFGLRPVDYADSK 534
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAK 178
RING-HC_AtBARD1-like cd23146
RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 ...
 39-91 1.38e-08

RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 (AtBARD1) and similar proteins; AtBARD1, also called protein REPRESSOR OF WUSCHEL 1, binds specifically to H3K4me3 regions of target gene (e.g. WUS and WOX5) promoters to repress their transcription via chromatin remodeling. It is required for the shoot apical meristem (SAM) organization and maintenance, by confining WUS expression to the organizing center, and for the quiescent center (QC) development in the root apical meristem (RAM), by repressing WOX5 expression in the root proximal meristem. AtBARD1 plays a role in DNA repair and in cell-cycle control. It is required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR). AtBARD1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438508 [Multi-domain]  Cd Length: 54  Bit Score: 51.32  E-value: 1.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746  39 LEKLLRCSRCTNILREPVCLGgCEHIFCSNCVSDCI--GSGCPVCYTPAWIQDVK 91
Cdd:cd23146     1 MELELKCPICLKLLNRPVLLP-CDHIFCSSCITDSTkvGSDCPVCKLPYHSQDLR 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
477-531 1.58e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 1.58e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2102106746 477 LLQHK-ALVNTTGYQNDSPLHDAVKNGHVDIVKLLLAYGASREAVNIFGLRPVDYA 531
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 441-541 1.69e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 441 VEYLLQNGSDPNVKDHAGWTPLHEACNHGH-----LKVVELLLQHKALVNTTGYQNDSPLHDAV--KNGHVDIVKLLLAY 513
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDN 130

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2102106746 514 GASREAVNIFGLRPVDYA-----DSKNMKSLLL 541
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYlesnkIDLKILKLLI 163
BRCT smart00292
breast cancer carboxy-terminal domain;
570-637 1.92e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 51.99  E-value: 1.92e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102106746  570 IGSGLSSEQQKMLSELAAILKAKKCAEFDS-TVTHVIVpGDTVQSTLKYMLGILSGCWILKFEWVKACL 637
Cdd:smart00292  11 ITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIV-GSPEGGKLELLKAIALGIPIVKEEWLLDCL 78
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 405-521 1.99e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.77  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 405 SPSATKLWPVSLT----AVKRNHRGETLLHIASIKG-DIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLK-VVELLL 478
Cdd:PHA02876  283 APSLSRLVPKLLErgadVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLL 362

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2102106746 479 QHKALVNTTGYQNDSPLHDAVKNGHVDIVKLLLAYGASREAVN 521
Cdd:PHA02876  363 ELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 421-496 5.02e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.83  E-value: 5.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQH----KALVNTTGYQNDSPLH 496
Cdd:PHA03100  188 KDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNgpsiKTIIETLLYFKDKDLN 267
PHA03095 PHA03095
ankyrin-like protein; Provisional
 438-530 1.20e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 438 IPSVEYLLQNGSDPNVKDHAGWTPLHeACNHG---HLKVVELLLQHKALVNTTGYQNDSPLHDAVKNGHVDI--VKLLLA 512
Cdd:PHA03095   97 LDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLID 175

                          90
                  ....*....|....*...
gi 2102106746 513 YGASREAVNIFGLRPVDY 530
Cdd:PHA03095  176 AGADVYAVDDRFRSLLHH 193
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 427-515 1.32e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 427 TLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQND-SPLHDAVKNGHVD 505
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKID 216

                          90
                  ....*....|
gi 2102106746 506 IVKLLLAYGA 515
Cdd:PHA02875  217 IVRLFIKRGA 226
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 572-640 2.31e-07

seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349370 [Multi-domain]  Cd Length: 75  Bit Score: 48.72  E-value: 2.31e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2102106746 572 SGLSSEQQKMLSELAAILKAKKC--AEFDSTVTHVIVPgdTVQSTLKYMLGILSGCWILKFEWVKACLQSK 640
Cdd:cd17738     7 SGFSEDEKKELISIIEKLGGKVLdsDEFDPKCTHLICG--KPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
 35-101 3.08e-07

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: 48.36  E-value: 3.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746  35 ALDRLEKLLRCSRCTNILREPVCLGgCEHIFCSNCVSDC---IGSGCPVCYTPAWIQDVKINRQLDSMIQ 101
Cdd:cd16596     2 RLTMMWEEVTCPICLDPFVEPVSIE-CGHSFCQECISQVgkgGGSVCPVCRQRFLLKNLRPNRQLANMVN 70
Ank_5 pfam13857
Ankyrin repeats (many copies);
421-465 4.60e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.60e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEA 465
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 427-515 4.62e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 4.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 427 TLLHIAsIKGDIP--SVEYLLQNGSDPNVKDHAGWTPLHEAC-NHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVknGH 503
Cdd:PHA02876  410 TALHFA-LCGTNPymSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EY 486

                          90
                  ....*....|..
gi 2102106746 504 VDIVKLLLAYGA 515
Cdd:PHA02876  487 HGIVNILLHYGA 498
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 440-539 5.25e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 440 SVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVKNGHV-----DIVKLLLAYG 514
Cdd:PHA03100   17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYG 96

                          90       100
                  ....*....|....*....|....*
gi 2102106746 515 ASREAVNIFGLRPVDYADSKNMKSL 539
Cdd:PHA03100   97 ANVNAPDNNGITPLLYAISKKSNSY 121
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 428-510 7.34e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.95  E-value: 7.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 428 LLHIASIkGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVKNGHVDIV 507
Cdd:PLN03192  529 LLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF 607


                  ...
gi 2102106746 508 KLL 510
Cdd:PLN03192  608 RIL 610
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 421-480 8.20e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 8.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQH 480
Cdd:PTZ00322  111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
BRCT smart00292
breast cancer carboxy-terminal domain;
666-764 9.05e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 46.98  E-value: 9.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746  666 PKLFDGCYFYFGGTFKHHPKDNLIKLVAAGGGQVLIRKPKPDsdvtqtintvayhakpdsdqrfcTQYIIYEDLSN--HR 743
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVGSPEGgkLE 57

                           90       100
                   ....*....|....*....|.
gi 2102106746  744 PERVRQGKVWVAPSSWFIDCV 764
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 426-516 1.07e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 426 ETLLHIASIKGDIPSVEYLLQNGS-DPNVKDHAGWTPLHEACNHGHLKVVELLLQH-KALVN--TTG--YQNDSPLHDAV 499
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNepMTSdlYQGETALHIAV 97

                          90
                  ....*....|....*..
gi 2102106746 500 KNGHVDIVKLLLAYGAS 516
Cdd:cd22192    98 VNQNLNLVRELIARGAD 114
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 458-485 1.34e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 45.27  E-value: 1.34e-06
                           10        20
                   ....*....|....*....|....*...
gi 2102106746  458 GWTPLHEACNHGHLKVVELLLQHKALVN 485
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 458-485 1.46e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.36  E-value: 1.46e-06
                          10        20
                  ....*....|....*....|....*....
gi 2102106746 458 GWTPLHEACNH-GHLKVVELLLQHKALVN 485
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 429-531 2.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 429 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVKngHVDIVK 508
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAI 238

                          90       100
                  ....*....|....*....|...
gi 2102106746 509 LLLAYGASREAVNIFGLRPVDYA 531
Cdd:PHA02874  239 ELLINNASINDQDIDGSTPLHHA 261
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
 42-85 2.31e-06

RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; RNF138, also known as Nemo-like kinase-associated RING finger protein (NARF) or NLK-associated RING finger protein, is an E3 ubiquitin-protein ligase that plays an important role in glioma cell proliferation, apoptosis, and cell cycle. It specifically cooperates with the E2 conjugating enzyme E2-25K (Hip-2/UbcH1), regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF), and further suppresses Wnt-beta-catenin signaling. RNF138, together with three closely related proteins: RNF114, RNF125 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438206 [Multi-domain]  Cd Length: 53  Bit Score: 45.09  E-value: 2.31e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2102106746  42 LLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGSG---CPVCYTPA 85
Cdd:cd16544     2 ELTCPVCQEVLKDPVELPPCRHIFCKACILLALRSSgarCPLCRGPV 48
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
 39-96 3.18e-06

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: 45.15  E-value: 3.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746  39 LEKLLRCSRCTNILREPVCLGgCEHIFCSNCVSD-CIGSG------CPVCYTPAWIQDVKINRQL 96
Cdd:cd16598     1 LEEEVTCSICLDYLRDPVTID-CGHNFCRSCITDyCPISGgherpvCPLCRKPFKKENIRPNWQL 64
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
 38-81 3.27e-06

RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) by binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 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: 438270 [Multi-domain]  Cd Length: 52  Bit Score: 44.80  E-value: 3.27e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2102106746  38 RLEKLLRCSRCTNILREPVCLGgCEHIFCSNCVSDCIGSG----CPVC 81
Cdd:cd16608     2 SLKDELLCSICLSIYQDPVSLG-CEHYFCRQCITEHWSRSehrdCPEC 48
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 414-542 3.83e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 414 VSLTAVKRNHRGETLLHIASIKGDIPS-----VEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTG 488
Cdd:PHA02876  129 ISGNDIHYDKINESIEYMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIA 208

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2102106746 489 YQNDSPLHDAVKNGHVDIVKLLLaygASREAVNIFGLRPVDYADSKNMKSLLLL 542
Cdd:PHA02876  209 LDDLSVLECAVDSKNIDTIKAII---DNRSNINKNDLSLLKAIRNEDLETSLLL 259
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 436-514 4.38e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 436 GDIPSVEYLLQN-GSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVKNGHVDIVKLLLAYG 514
Cdd:PHA02874   12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 43-81 6.04e-06

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: 43.63  E-value: 6.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2102106746  43 LRCSRCTNILREPVCLGgCEHIFCSNCVSDCIGSG---CPVC 81
Cdd:cd16449     1 LECPICLERLKDPVLLP-CGHVFCRECIRRLLESGsikCPIC 41
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 424-579 1.50e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 424 RGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVN------------------ 485
Cdd:PLN03192  557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDphaagdllctaakrndlt 636

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 486 ------TTGYQNDSPLHD-------AVKNGHVDIVKLLLAYGASREAVNIFglrpvDYADSKNMKSLLllpEKKESSST- 551
Cdd:PLN03192  637 amkellKQGLNVDSEDHQgatalqvAMAEDHVDMVRLLIMNGADVDKANTD-----DDFSPTELRELL---QKRELGHSi 708

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2102106746 552 ----SHCSVVNTGQRRDGPLALIGSGLSSEQQ 579
Cdd:PLN03192  709 tivdSVPADEPDLGRDGGSRPGRLQGTSSDNQ 740
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 458-486 1.92e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 1.92e-05
                          10        20
                  ....*....|....*....|....*....
gi 2102106746 458 GWTPLHEACNHGHLKVVELLLQHKALVNT 486
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 34-84 2.08e-05

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


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 47.69  E-value: 2.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2102106746  34 AALDRLEKLLRCSRCTNILREPVcLGGCEHIFCSNCVSDCIG--SGCPVCYTP 84
Cdd:TIGR00599  18 PSLYPLDTSLRCHICKDFFDVPV-LTSCSHTFCSLCIRRCLSnqPKCPLCRAE 69
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 432-514 2.63e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 432 ASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAVKNGHVDIVKLLL 511
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88


                  ...
gi 2102106746 512 AYG 514
Cdd:PHA02875   89 DLG 91
RING-HC_RNF166 cd16549
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; ...
 45-84 2.76e-05

RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; RNF166 is encoded by the gene RNF166 targeted by thyroid hormone receptor alpha1 (TRalpha1), which is important in brain development. It plays an important role in RNA virus-induced interferon-beta production by enhancing the ubiquitination of TRAF3 and TRAF6. RNF166, together with three closely related proteins: RNF114, RNF125 and RNF138, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438211 [Multi-domain]  Cd Length: 47  Bit Score: 42.11  E-value: 2.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2102106746  45 CSRCTNILREPVCLGGCEHIFCSNCVSDCIGSG---CPVCYTP 84
Cdd:cd16549     4 CPICLEVYHKPVVITSCGHTFCGECLQPCLQVAsplCPLCRMP 46
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
 43-94 2.98e-05

RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated (FHA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438166 [Multi-domain]  Cd Length: 55  Bit Score: 41.97  E-value: 2.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746  43 LRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGSG---CPVCYTPawIQDVKINR 94
Cdd:cd16503     3 LTCSICQDLLHDCVSLQPCMHNFCAACYSDWMERSnteCPTCRAT--VQRVNKNH 55
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 490-516 3.33e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.33e-05
                           10        20
                   ....*....|....*....|....*..
gi 2102106746  490 QNDSPLHDAVKNGHVDIVKLLLAYGAS 516
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 425-524 3.34e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.31  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 425 GETLLHIASIKGDIPSVEYLLQNGSD----PNVKD-HAGWTPLHEACNHGHLKVVELLLQHKALVNT---TG-------- 488
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPElvnePMTSDlYQGETALHIAVVNQNLNLVRELIARGADVVSpraTGtffrpgpk 130

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2102106746 489 ---YQNDSPLHDAVKNGHVDIVKLLLAYGASREAVNIFG 524
Cdd:cd22192   131 nliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
 39-89 3.36e-05

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


Pssm-ID: 438192 [Multi-domain]  Cd Length: 54  Bit Score: 41.90  E-value: 3.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2102106746  39 LEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIG--SGCPVCYTPAWIQD 89
Cdd:cd16529     1 LDDLLRCPICFEYFNTAMMITQCSHNYCSLCIRRFLSykTQCPTCRAAVTESD 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
444-496 3.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2102106746 444 LLQNGS-DPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLH 496
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
491-531 4.69e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.69e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2102106746 491 NDSPLHDAVKNGHVDIVKLLLAYGASREAVNIFGLRPVDYA 531
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_2 pfam12796
Ankyrin repeats (3 copies);
418-455 5.18e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 5.18e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2102106746 418 AVKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKD 455
Cdd:pfam12796  54 DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
 43-84 5.78e-05

Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins; RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.


Pssm-ID: 438282 [Multi-domain]  Cd Length: 55  Bit Score: 41.24  E-value: 5.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2102106746  43 LRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGSG---CPVCYTP 84
Cdd:cd16620     4 LKCPICKDLMKDAVLTPCCGNSFCDECIRTALLEEdftCPTCKEP 48
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 424-456 5.89e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 5.89e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2102106746 424 RGETLLHIASIK-GDIPSVEYLLQNGSDPNVKDH 456
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
RING-HC_RING1-like cd16531
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and ...
 43-84 6.77e-05

RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), is a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. Both RING1 and RING2 are core components of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING2 acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Members of this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 438193 [Multi-domain]  Cd Length: 66  Bit Score: 41.49  E-value: 6.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2102106746  43 LRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGSG---CPVCYTP 84
Cdd:cd16531     2 LMCPICLGIIKNTMTVKECLHRFCAECIEKALRLGnkeCPTCRKH 46
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
 35-84 7.68e-05

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: 42.28  E-value: 7.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746  35 ALDRLEKLLRCSRCTNILREPVCLgGCEHIFCSNCVSDCIGSG-----CPVCYTP 84
Cdd:cd16498     9 VISAMQKNLECPICLELLKEPVST-KCDHQFCRFCILKLLQKKkkpapCPLCKKS 62
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 492-521 8.81e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 8.81e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2102106746 492 DSPLHDAV-KNGHVDIVKLLLAYGASREAVN 521
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 425-543 1.05e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 425 GETLLHI----ASIKGDIpsVEYLLQNGSDPNVKDHAGWTPLH-----EACNhghLKVVELLLQHKALVNTTGYQNDSPL 495
Cdd:PHA03095  117 GRTPLHVylsgFNINPKV--IRLLLRKGADVNALDLYGMTPLAvllksRNAN---VELLRLLIDAGADVYAVDDRFRSLL 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2102106746 496 H---DAVKNgHVDIVKLLLAYGASREAVNIFGLRPVDY-ADSKNMKSLLLLP 543
Cdd:PHA03095  192 HhhlQSFKP-RARIVRELIRAGCDPAATDMLGNTPLHSmATGSSCKRSLVLP 242
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 421-528 1.23e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEA-CNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAV 499
Cdd:PHA02876  371 RDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYAC 450

                          90       100       110
                  ....*....|....*....|....*....|
gi 2102106746 500 KNG-HVDIVKLLLAYGASREAVNIFGLRPV 528
Cdd:PHA02876  451 KKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 45-81 1.23e-04

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


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 39.80  E-value: 1.23e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2102106746   45 CSRCTNILREPVCLGGCEHIFCSNCVSDCIGSG---CPVC 81
Cdd:smart00184   1 CPICLEEYLKDPVILPCGHTFCRSCIRKWLESGnntCPIC 40
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
 45-81 1.32e-04

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


Pssm-ID: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 39.65  E-value: 1.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2102106746  45 CSRCTNILREPVCLGGCEHIFCSNCVSDCIGSG---CPVC 81
Cdd:pfam00097   1 CPICLEEPKDPVTLLPCGHLFCSKCIRSWLESGnvtCPLC 40
mRING-HC-C3HC3D_TRAF7 cd16644
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 43-80 1.70e-04

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 7 (TRAF7) and similar proteins; TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor by promoting K29-linked ubiquitination of several cellular targets, including the NF-kappaB essential modulator (NEMO) and the p65 subunit of NF-kappaB transcription factor. It is also involved in K29-linked polyubiquitination that has been implicated in lysosomal degradation of proteins. Moreover, TRAF7 is required for K48-linked ubiquitination of p53, a key tumor suppressor and a master regulator of various signaling pathways, such as those related to apoptosis, cell cycle and DNA repair. It is also required for tumor necrosis factor alpha (TNFalpha)-induced Jun N-terminal kinase activation and promotes cell death by regulating polyubiquitination and lysosomal degradation of c-FLIP protein. Furthermore, TRAF7 functions as small ubiquitin-like modifier (SUMO) E3 ligase involved in other post-translational modification, such as sumoylation. It binds to and stimulates sumoylation of the proto-oncogene product c-Myb, a transcription factor regulating proliferation and differentiation of hematopoietic cells. It potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. Meanwhile, TRAF7 mediates MyoD1 regulation of the pathway and cell-cycle progression in myoblasts. It also plays a role in Toll-like receptors (TLR) signaling. TRAF7 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and an adjacent zinc finger, and a unique C-terminal domain that comprises a coiled coil domain and seven WD40 repeats.


Pssm-ID: 438306 [Multi-domain]  Cd Length: 47  Bit Score: 39.64  E-value: 1.70e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2102106746  43 LRCSRCTNILREPVcLGGCEHIFCSNCVSDCIGSGCPV 80
Cdd:cd16644     6 LYCPLCQRVFKDPV-ITSCGHTFCRRCALTAPGEKCPV 42
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 424-453 1.72e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 1.72e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2102106746 424 RGETLLHIASIKGDIPSVEYLLQNGSDPNV 453
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
 43-81 1.76e-04

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


Pssm-ID: 438263 [Multi-domain]  Cd Length: 44  Bit Score: 39.78  E-value: 1.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2102106746  43 LRCSRCTNILREPVCLgGCEHIFCSNCVS----DCIGS-GCPVC 81
Cdd:cd16601     2 ASCSLCKEYLKDPVII-ECGHNFCRACITrfweELDGDfPCPQC 44
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
 38-94 1.79e-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: 39.98  E-value: 1.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2102106746  38 RLEKLLRCSRCTNILREPVCLGgCEHIFCSNCVSDCIGSG-----CPVCYTPAWIQDVKINR 94
Cdd:cd16594     1 SLQEELTCPICLDYFTDPVTLD-CGHSFCRACIARCWEEPetsasCPQCRETCPQRNLRPNR 61
RING-HC_ScRAD18-like cd23148
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ...
 40-84 2.64e-04

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


Pssm-ID: 438510 [Multi-domain]  Cd Length: 52  Bit Score: 39.44  E-value: 2.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2102106746  40 EKLLRCSRCTNILREPVcLGGCEHIFCSNCVSDCIG--SGCPVCYTP 84
Cdd:cd23148     1 DHALRCHICKDLLKAPM-RTPCNHTFCSFCIRTHLNndARCPLCKAE 46
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 421-500 2.78e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIK-GDIPSVEYLLQNGSDPNVKDHA-GWTPLHEACNHGhlKVVELLLQHKALVNTTGYQNDSPLHDA 498
Cdd:PHA02878  230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307


                  ..
gi 2102106746 499 VK 500
Cdd:PHA02878  308 VK 309
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 665-774 3.04e-04

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 40.04  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 665 LPKLFDGCYFYFGgTFKHHPKDNLIKLVAAGGGQVlirkpkpdsdvTQTINTVAYHakpdsdqRFCTQYIIYEDLSNHRP 744
Cdd:pfam16589   1 LPNLFEPLRFYIN-AIPSPSRSKLKRLIEANGGTV-----------VDNINPAVYI-------VIAPYNKTDKLAENTKL 61

                          90       100       110
                  ....*....|....*....|....*....|
gi 2102106746 745 ERVRqgkvwvapSSWFIDCVMSFELLPLDN 774
Cdd:pfam16589  62 GVVS--------PQWIFDCVKKGKLLPLEN 83
zf-RING_5 pfam14634
zinc-RING finger domain;
44-81 3.04e-04

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 38.95  E-value: 3.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2102106746  44 RCSRCTN--ILREPVCLGGCEHIFCSNCVSDCIGSG-CPVC 81
Cdd:pfam14634   1 HCNKCFKelSKTRPFYLTSCGHIFCEECLTRLLQERqCPIC 41
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
 39-96 3.37e-04

RING finger, HC subclass, 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 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: 438261 [Multi-domain]  Cd Length: 66  Bit Score: 39.37  E-value: 3.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2102106746  39 LEKLLRCSRCTNILREPVCLGgCEHIFCSNCVS----DCIGSGCPVCYTPAWIQDVKINRQL 96
Cdd:cd16599     1 FKEELLCPICYEPFREAVTLR-CGHNFCKGCVSrsweRQPRAPCPVCKEASSSDDLRTNHTL 61
PHA02946 PHA02946
ankyin-like protein; Provisional
 434-515 3.41e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.89  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 434 IKG-DIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLH--DAVKNGHVDIVKLL 510
Cdd:PHA02946   47 IKGlDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLL 126


                  ....*
gi 2102106746 511 LAYGA 515
Cdd:PHA02946  127 VQYGA 131
mRING-HC-C3HC3D_TRAF4-like cd23126
Modified RING finger, HC subclass (C3HC3D-type), found in uncharacterized proteins similar to ...
 39-80 5.04e-04

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


Pssm-ID: 438488 [Multi-domain]  Cd Length: 52  Bit Score: 38.47  E-value: 5.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2102106746  39 LEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCI--GSGCPV 80
Cdd:cd23126     1 LDKKYECPVCCQVLRYPVQFEECGHRVCSSCLPELLrvEPRCPI 44
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
35-84 5.11e-04

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 43.15  E-value: 5.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2102106746  35 ALDRLEKLLRCSRCTNILREPvCLGGCEHIFCSNCVSDCIGS--GCPVCYTP 84
Cdd:COG5432    18 SLKGLDSMLRCRICDCRISIP-CETTCGHTFCSLCIRRHLGTqpFCPVCRED 68
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
 40-85 5.34e-04

RING finger, HC subclass, found in tripartite motif-containing protein 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 the 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 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: 438271 [Multi-domain]  Cd Length: 58  Bit Score: 38.51  E-value: 5.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2102106746  40 EKLLRCSRCTNILREPVCLGgCEHIFCSNCVSDC------IGSGCPVCYTPA 85
Cdd:cd16609     1 EEELTCSICLGLYQDPVTLP-CQHSFCRACIEDHwrqkdeGSFSCPECRAPF 51
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 572-637 5.50e-04

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 39.20  E-value: 5.50e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2102106746 572 SGLSSEQQKMLSELAAILKAKKCAEFDSTVTHVIVPGDTvqstLKYMLGILSGCWILKFEWVKACL 637
Cdd:pfam00533  14 TGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEART----KKYLKAKELGIPIVTEEWLLDCI 75
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 424-453 8.09e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 8.09e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2102106746  424 RGETLLHIASIKGDIPSVEYLLQNGSDPNV 453
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
RING-HC_PRT1-like cd23132
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and ...
 45-84 8.26e-04

RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and similar proteins; PRT1, also called RING-type E3 ubiquitin transferase PRT1, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. It functions in the N-end rule pathway of protein degradation, where it specifically recognizes and ubiquitinates proteins with an N-terminal bulky aromatic amino acid (Phe). It does not act on aliphatic hydrophobic and basic N-terminal residues (Arg or Leu) containing proteins. PRT1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438494 [Multi-domain]  Cd Length: 52  Bit Score: 37.79  E-value: 8.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2102106746  45 CSRCTNILREPVCLGgCEHIFCSNCVSDCIG----SGCPVCYTP 84
Cdd:cd23132     5 CCICLDLLYKPVVLE-CGHVFCFWCVHRCMNgydeSHCPLCRRP 47
RING-HC_RAG1 cd16530
RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar ...
 41-84 9.36e-04

RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar proteins; RAG-1, also known as V(D)J recombination-activating protein 1, RING finger protein 74 (RNF74), or endonuclease RAG1, is the catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. RAG1 is a lymphoid-specific factor that mediates DNA-binding to conserved recombination signal sequences (RSS) and catalyzes DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. It also functions as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3, which is required for the joining step of V(D)J recombination. RAG-1 contains an N-terminal C3HC4-type RING-HC finger that mediates monoubiquitylation of histone H3, an adjacent C2H2-type zinc finger, and a nonamer binding (NBD) DNA-binding domain.


Pssm-ID: 319444 [Multi-domain]  Cd Length: 46  Bit Score: 37.81  E-value: 9.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2102106746  41 KLLRCSRCTNILREPVCLGgCEHIFCSNCVSDCI---GSGCPVCYTP 84
Cdd:cd16530     1 KSVSCQVCEHILADPVQTP-CKHLFCRTCILKCLkvmGSYCPSCRYP 46
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 566-640 1.11e-03

BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage syndrome protein 1 (NBS1), or cell cycle regulatory protein p95, is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The BRCT (Breast Cancer Suppressor Protein BRCA1, carboxy-terminal) domain is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions within DNA strand breaks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is absent in this group.


Pssm-ID: 349372 [Multi-domain]  Cd Length: 74  Bit Score: 38.35  E-value: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746 566 PLALIGSGLSSEQQKMLSELAAILKAKKCAEFDSTVTHVIVPgdTVQSTLKYMLGILSGCWILKFEWVKACLQSK 640
Cdd:cd17741     2 PLVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMS--KIKVTVKVICALISGKPIVTPEYLDALLEAI 74
RING-HC_TRIM77_C-IV cd16543
RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar ...
 43-84 1.73e-03

RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar proteins; TRIM77 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 two consecutive zinc-binding domains, a C3HC4-type RING-HC finger and Bbox2, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438205 [Multi-domain]  Cd Length: 54  Bit Score: 36.99  E-value: 1.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2102106746  43 LRCSRCTNILREPVCLGgCEHIFCSNCVSDC-----IGSGCPVCYTP 84
Cdd:cd16543     4 LTCSICLDLLKDPVTIP-CGHSFCMNCITLLwdrkqGVPSCPQCRES 49
PHA03095 PHA03095
ankyrin-like protein; Provisional
 421-478 1.91e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2102106746 421 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLL 478
Cdd:PHA03095  253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
RING-HC_TRIM41-like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
 45-81 2.16e-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: 36.83  E-value: 2.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2102106746  45 CSRCTNILREPVCLGgCEHIFCSNCVSDCIGSGCPVC 81
Cdd:cd16602     6 CAICLDYFKDPVSIG-CGHNFCRVCVTQLWGFTCPQC 41
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
 43-100 2.31e-03

RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal forkhead-associated (FHA) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438197 [Multi-domain]  Cd Length: 64  Bit Score: 36.99  E-value: 2.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746  43 LRCSRCTNILREPVCLGgCEHIFCSNCVSDCIGSG--CPVCYTPawIQDVKINRQLDSMI 100
Cdd:cd16535     2 LQCSICSELFIEAVTLN-CSHSFCSYCITEWMKRKkeCPICRKP--ITSKTRSLVLDNCI 58
RING-HC_CeBARD1-like cd23143
RING finger, HC subclass, found in Caenorhabditis elegans BRCA1-associated RING domain protein ...
 42-84 2.66e-03

RING finger, HC subclass, found in Caenorhabditis elegans BRCA1-associated RING domain protein 1 (CeBARD1) and similar proteins; CeBARD1, also called Ce-BRD-1, Cebrd-1, or RING-type E3 ubiquitin transferase BARD1, is a constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity. It plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by ionizing radiation. It protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability. CeBARD1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438505 [Multi-domain]  Cd Length: 47  Bit Score: 36.37  E-value: 2.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2102106746  42 LLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGSG--CPVCYTP 84
Cdd:cd23143     1 LIECVICSEPQIDTFLLSSCGHIYCWECFTEFIEKRhmCPSCRFP 45
mRING-HC-C3HC3D_TRAF5 cd16642
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 39-81 3.22e-03

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


Pssm-ID: 438304 [Multi-domain]  Cd Length: 56  Bit Score: 36.26  E-value: 3.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2102106746  39 LEKLLRCSRCTNILREPVcLGGCEHIFCSNCVSDCIG-SGCPVC 81
Cdd:cd16642     1 LEDRYKCATCHFVLHNPH-QTGCGHRFCQHCILSLLElNTTPIC 43
RING-HC_LONFs_rpt2 cd16514
second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
 43-84 3.30e-03

second 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 second RING-HC finger.


Pssm-ID: 438177 [Multi-domain]  Cd Length: 45  Bit Score: 36.09  E-value: 3.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2102106746  43 LRCSRCTNILREPVCLGgCEHIFCSNCVSDCI--GSGCPVCYTP 84
Cdd:cd16514     2 LECSLCLRLLYEPVTTP-CGHTFCRACLERCLdhSPKCPLCRTS 44
PHA03095 PHA03095
ankyrin-like protein; Provisional
 421-512 3.40e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 421 RNHRGETLLHIASIKGDIPS--VEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDA 498
Cdd:PHA03095  218 TDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297

                          90
                  ....*....|....
gi 2102106746 499 VKNGHVDIVKLLLA 512
Cdd:PHA03095  298 VRNNNGRAVRAALA 311
RING-HC_AtBRCA1-like cd23147
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 ...
 39-91 3.54e-03

RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 homolog (AtBRCA1) and similar proteins; AtBRCA1 plays a role in DNA repair and in cell-cycle control. It is required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR). AtBRCA1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438509 [Multi-domain]  Cd Length: 54  Bit Score: 36.29  E-value: 3.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746  39 LEKLLRCSRCTNILREPVCLGgCEHIFCSNCVSDCI--GSGCPVCYTPAWIQDVK 91
Cdd:cd23147     1 LGKELKCPICLSLFKSAANLS-CNHCFCAGCIGESLklSAICPVCKIPATRRDTR 54
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
 39-81 3.62e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 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 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: 438259 [Multi-domain]  Cd Length: 71  Bit Score: 36.52  E-value: 3.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2102106746  39 LEKLLRCSRCTNILREPVCLgGCEHIFCSNCVS----DCIGSG--CPVC 81
Cdd:cd16597     2 LEEELTCSICLELFKDPVTL-PCGHNFCGVCIEktwdSQHGSEysCPQC 49
RING-HC_GEFO-like cd16507
RING finger, HC subclass, found in Dictyostelium discoideum Ras guanine nucleotide exchange ...
 45-81 4.25e-03

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


Pssm-ID: 438170 [Multi-domain]  Cd Length: 58  Bit Score: 36.17  E-value: 4.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2102106746  45 CSRCTNILREPVCLGGCEHIFCSNCVSDCI-GSGCPVC 81
Cdd:cd16507    12 CGICQNLFKDPNTLIPCGHAFCLDCLTTNAsIKNCIQC 49
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
 42-81 4.66e-03

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, followed by a C-terminal transmembrane domain. 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). TRIM59, also known as 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.


Pssm-ID: 438243 [Multi-domain]  Cd Length: 50  Bit Score: 35.95  E-value: 4.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2102106746  42 LLRCSRCTNILREPVCLGgCEHIFCSNCV-SDCIGSG--------CPVC 81
Cdd:cd16581     2 ELTCSICYNIFDDPKILP-CSHTFCKNCLeKLLAASGyyllaslkCPTC 49
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
 45-91 5.42e-03

RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 is an E3 ubiquitin-protein ligase that interacts with mesenchyme Homeobox 2 (MEOX2) transcription factor, a regulator of the proliferation, differentiation and migration of vascular smooth muscle cells and cardiomyocytes; it enhances Meox2 activation of the p21 promoter. It also regulates the expression of myelin-associated glycoprotein (MAG) genes and is required for myelin production in Schwann cells of the peripheral nervous system. Moreover, RNF10 regulates retinoic acid-induced neuronal differentiation and the cell cycle exit of P19 embryonic carcinoma cells. RNF10 contains a C3HC4-type RING-HC finger and three putative nuclear localization signals.


Pssm-ID: 438198 [Multi-domain]  Cd Length: 54  Bit Score: 35.68  E-value: 5.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2102106746  45 CSRCtniLREPVC--LGGCEHIFCSNCV------SDCIGSGCPVCYTPAWIQDVK 91
Cdd:cd16536     3 CPIC---LEPPVAprITRCGHIFCWPCIlrylslSEKKWRKCPICFESIHKKDLR 54
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 576-636 5.68e-03

sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the sixth BRCT domain.


Pssm-ID: 349359 [Multi-domain]  Cd Length: 75  Bit Score: 36.42  E-value: 5.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2102106746 576 SEQQKMLSELAAILKAKKCAEFDSTVTHVIVPGDTVQSTLKYMLGILSGCWILKFEWVKAC 636
Cdd:cd17727    13 SKRQGELNKIAASLGAEYRWTYDESCTHFIYQGKANDTNREYKSAKEQGKFIVSPHWLYAC 73
RING-HC_TRIM58_C-IV cd16606
RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar ...
 44-84 6.96e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar proteins; 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. TRIM58 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 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: 438268 [Multi-domain]  Cd Length: 53  Bit Score: 35.22  E-value: 6.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2102106746  44 RCSRCTNILREPVCLGgCEHIFCSNCVS------DCIGSG---CPVCYTP 84
Cdd:cd16606     4 RCPVCLDFLQEPVSVD-CGHSFCLRCISefceksDSAQGGvyaCPQCRGP 52
RING-HC_TRAF2 cd16639
RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 2 ...
 45-81 7.47e-03

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


Pssm-ID: 438301 [Multi-domain]  Cd Length: 43  Bit Score: 35.13  E-value: 7.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2102106746  45 CSRCTNILREPVcLGGCEHIFCSNCVSDCIGSG---CPVC 81
Cdd:cd16639     4 CSDCRNILRRPF-QAQCGHRYCSYCLKKILSSGpqkCAAC 42
RING-HC_RNFT1-like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
 45-81 7.63e-03

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 438194 [Multi-domain]  Cd Length: 41  Bit Score: 34.97  E-value: 7.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2102106746  45 CSRCTNILREPVCLGgCEHIFCSNCVSDCIG--SGCPVC 81
Cdd:cd16532     3 CPICQDEFKDPVVLR-CKHIFCEDCVSEWFEreRTCPLC 40
PHA02795 PHA02795
ankyrin-like protein; Provisional
 425-513 9.11e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 39.21  E-value: 9.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102106746 425 GETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHG--------HLKVVELLLQHKALVNTTgyqNDSPLH 496
Cdd:PHA02795  221 GRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLREPLSIDCI---KLAILN 297

                          90
                  ....*....|....*..
gi 2102106746 497 DAVKNGhvDIVKLLLAY 513
Cdd:PHA02795  298 NTIENH--DVIKLCIKY 312
RING-HC_RAD16-like cd16567
RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, ...
 45-84 9.21e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, Schizosaccharomyces pombe rhp16, and similar proteins; Budding yeast RAD16, also known as ATP-dependent helicase RAD16, is encoded by a yeast excision repair gene homologous to the recombinational repair gene RAD54 and to the SNF2 gene involved in transcriptional activation. It is a component of the global genome repair (GGR) complex that promotes global genome nucleotide excision repair (GG-NER) by removing DNA damage from non-transcribing DNA. RAD16 is involved in differential repair of DNA after UV damage, and repairs preferentially the MAT-alpha locus compared with the HML-alpha locus. Fission yeast rhp16, also known as ATP-dependent helicase rhp16, is a RAD16 homolog. It is involved in GGR via nucleotide excision repair (NER), in conjunction with rhp7, after UV irradiation. Both RAD16 and rhp16 contain a C3HC4-type RING-HC finger, as well as a DEAD-like helicase domain and a helicase superfamily C-terminal domain.


Pssm-ID: 438229 [Multi-domain]  Cd Length: 48  Bit Score: 35.01  E-value: 9.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2102106746  45 CSRCTNILREPVcLGGCEHIFCSNCVSDCIGSG------CPVCYTP 84
Cdd:cd16567     3 CGICHEEAEDPV-VARCHHVFCRACVKEYIESApggkvtCPTCHKP 47
RING-HC_RNF180 cd16554
RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; ...
 43-86 9.36e-03

RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; RNF180, also known as Rines, is a membrane-bound E3 ubiquitin-protein ligase well conserved among vertebrates. It is a critical regulator of the monoaminergic system, as well as emotional and social behavior. It interacts with brain monoamine oxidase A (MAO-A) and targets it for ubiquitination and degradation. It also functions as a novel tumor suppressor in gastric carcinogenesis. The hypermethylated CpG site count of the RNF180 DNA promoter can be used to predict survival of gastric cancer. RNF180 contains a novel conserved dual specificity protein phosphatase Rines conserved (DSPRC) domain, a basic coiled-coil domain, a C3HC4-type RING-HC finger, and a C-terminal hydrophobic region that is predicted to be a transmembrane domain.


Pssm-ID: 438216 [Multi-domain]  Cd Length: 59  Bit Score: 35.37  E-value: 9.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2102106746  43 LRCSRCTNILREPVCLGGCEHIFCSNCV-----SDCIGSGCPVCYTPAW 86
Cdd:cd16554     3 LTCPVCLDLYYDPYMCYPCGHIFCEPCLrqlakSSPKNTPCPLCRTTIR 51
 
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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