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Conserved domains on  [gi|568905654|ref|XP_006495695|]
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BRCA1-associated RING domain protein 1 isoform X2 [Mus musculus]

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 ...
 28-112 1.63e-43

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: 148.64  E-value: 1.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  28 WAHSRAALARLEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSGCPVCYTPAWILDLKINRQLDSMIQLSSKLQN 107
Cdd:cd16496    2 WARTRAALDELENLLRCSRCASILKEPVTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLRN 81


                 ....*
gi 568905654 108 LLHDN 112
Cdd:cd16496   82 LLNDN 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
403-510 8.90e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 8.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 403 LSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQN 482
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                         90       100
                 ....*....|....*....|....*...
gi 568905654 483 DSPLHDAVKSGHIDIVKVLLSHGASRNA 510
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNA 214
 
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 ...
 28-112 1.63e-43

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: 148.64  E-value: 1.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  28 WAHSRAALARLEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSGCPVCYTPAWILDLKINRQLDSMIQLSSKLQN 107
Cdd:cd16496    2 WARTRAALDELENLLRCSRCASILKEPVTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLRN 81


                 ....*
gi 568905654 108 LLHDN 112
Cdd:cd16496   82 LLNDN 86
zf-RING_6 pfam14835
zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer ...
 35-99 5.83e-35

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: 125.16  E-value: 5.83e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568905654   35 LARLEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSGCPVCYTPAWILDLKINRQLDSMI 99
Cdd:pfam14835   1 LDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
403-510 8.90e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 8.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 403 LSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQN 482
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                         90       100
                 ....*....|....*....|....*...
gi 568905654 483 DSPLHDAVKSGHIDIVKVLLSHGASRNA 510
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNA 214
Ank_2 pfam12796
Ankyrin repeats (3 copies);
420-507 3.24e-27

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 104.81  E-value: 3.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  420 LHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTpgYQNDSPLHDAVKSGHIDIVK 499
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK--DNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 568905654  500 VLLSHGAS 507
Cdd:pfam12796  79 LLLEKGAD 86
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 382-505 4.54e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.39  E-value: 4.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 382 PPPLLNNSTHRQMmsspstvkLSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGH 461
Cdd:PHA02874  98 PIPCIEKDMIKTI--------LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568905654 462 LKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIVKVLLSHG 505
Cdd:PHA02874 170 FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 449-476 3.12e-07

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: 46.43  E-value: 3.12e-07
                           10        20
                   ....*....|....*....|....*...
gi 568905654   449 GWTPLHEACSHGHLKVVELLLQHNALVN 476
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 416-507 1.04e-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: 51.17  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 416 GETLLHIASIKGDIPSVEYLLQNG----NDPNVKD-HAGWTPLHEACSHGHLKVVELLLQHNALVNTPG----------- 479
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAApelvNEPMTSDlYQGETALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpgpk 130

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568905654 480 ---YQNDSPLHDAVKSGHIDIVKVLLSHGAS 507
Cdd:cd22192  131 nliYYGEHPLSFAACVGNEEIVRLLIEHGAD 161
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 33-100 2.45e-06

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: 49.62  E-value: 2.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654   33 AALARLEKLLRCSRCANILKEPVcLGGCEHIFCSGCISDC--VGSGCPVCYTPAWILDLKINRQLDSMIQ 100
Cdd:TIGR00599  18 PSLYPLDTSLRCHICKDFFDVPV-LTSCSHTFCSLCIRRClsNQPKCPLCRAEDQESKLRSNWLVSEIVE 86
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 44-80 1.43e-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: 39.41  E-value: 1.43e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568905654    44 CSRCANILKEPVCLGGCEHIFCSGCISDCVGSG---CPVC 80
Cdd:smart00184   1 CPICLEEYLKDPVILPCGHTFCRSCIRKWLESGnntCPIC 40
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
34-111 4.30e-04

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


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 42.77  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  34 ALARLEKLLRCSRCANILKEPvCLGGCEHIFCSGCISDCVGS--GCPVCYTPAWILDLKINRQLDSMIQLSSKLQNLLHD 111
Cdd:COG5432   18 SLKGLDSMLRCRICDCRISIP-CETTCGHTFCSLCIRRHLGTqpFCPVCREDPCESRLRGSSGSREINESHARNRDLLRK 96
 
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 ...
 28-112 1.63e-43

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: 148.64  E-value: 1.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  28 WAHSRAALARLEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSGCPVCYTPAWILDLKINRQLDSMIQLSSKLQN 107
Cdd:cd16496    2 WARTRAALDELENLLRCSRCASILKEPVTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLRN 81


                 ....*
gi 568905654 108 LLHDN 112
Cdd:cd16496   82 LLNDN 86
zf-RING_6 pfam14835
zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer ...
 35-99 5.83e-35

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: 125.16  E-value: 5.83e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568905654   35 LARLEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSGCPVCYTPAWILDLKINRQLDSMI 99
Cdd:pfam14835   1 LDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
403-510 8.90e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 8.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 403 LSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQN 482
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                         90       100
                 ....*....|....*....|....*...
gi 568905654 483 DSPLHDAVKSGHIDIVKVLLSHGASRNA 510
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNA 214
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
403-511 1.35e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 1.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 403 LSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQN 482
Cdd:COG0666   74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG 153

                         90       100
                 ....*....|....*....|....*....
gi 568905654 483 DSPLHDAVKSGHIDIVKVLLSHGASRNAV 511
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNAR 182
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-510 2.83e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 2.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 412 RNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVK 491
Cdd:COG0666  149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                         90
                 ....*....|....*....
gi 568905654 492 SGHIDIVKVLLSHGASRNA 510
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNA 247
Ank_2 pfam12796
Ankyrin repeats (3 copies);
420-507 3.24e-27

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 104.81  E-value: 3.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  420 LHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTpgYQNDSPLHDAVKSGHIDIVK 499
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK--DNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 568905654  500 VLLSHGAS 507
Cdd:pfam12796  79 LLLEKGAD 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
411-510 1.43e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.94  E-value: 1.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 411 KRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAV 490
Cdd:COG0666   49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                         90       100
                 ....*....|....*....|
gi 568905654 491 KSGHIDIVKVLLSHGASRNA 510
Cdd:COG0666  129 YNGNLEIVKLLLEAGADVNA 148
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-510 3.57e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 3.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 412 RNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVK 491
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                         90
                 ....*....|....*....
gi 568905654 492 SGHIDIVKVLLSHGASRNA 510
Cdd:COG0666  262 AGAALIVKLLLLALLLLAA 280
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 382-505 4.54e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.39  E-value: 4.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 382 PPPLLNNSTHRQMmsspstvkLSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGH 461
Cdd:PHA02874  98 PIPCIEKDMIKTI--------LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568905654 462 LKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIVKVLLSHG 505
Cdd:PHA02874 170 FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
Ank_2 pfam12796
Ankyrin repeats (3 copies);
397-477 5.79e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 5.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  397 SPSTVK--LSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNgNDPNVKDHaGWTPLHEACSHGHLKVVELLLQHNAL 474
Cdd:pfam12796   9 NLELVKllLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGAD 86


                  ...
gi 568905654  475 VNT 477
Cdd:pfam12796  87 INV 89
Ank_4 pfam13637
Ankyrin repeats (many copies);
418-469 4.37e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 69.23  E-value: 4.37e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568905654  418 TLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLL 469
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 383-511 9.05e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.24  E-value: 9.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 383 PPLLNNSTHRqmMSSPSTVK--LSSGMPARKRNHRGETLLHIA--SIKGDIP----------------SVEYLLQNGNDP 442
Cdd:PHA03100 108 TPLLYAISKK--SNSYSIVEylLDNGANVNIKNSDGENLLHLYleSNKIDLKilkllidkgvdinaknRVNYLLSYGVPI 185

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568905654 443 NVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIVKVLLSHGASRNAV 511
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 411-510 1.95e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.22  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 411 KRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAV 490
Cdd:PHA02878 163 KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242

                         90       100
                 ....*....|....*....|.
gi 568905654 491 KS-GHIDIVKVLLSHGASRNA 510
Cdd:PHA02878 243 GYcKDYDILKLLLEHGVDVNA 263
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 418-510 2.85e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 2.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 418 TLLHIAS-----IKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSH--GHLKVVELLLQHNALVNTPGYQNDSPLHDAV 490
Cdd:PHA03100  70 TPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149

                         90       100
                 ....*....|....*....|..
gi 568905654 491 KSGHID--IVKVLLSHGASRNA 510
Cdd:PHA03100 150 ESNKIDlkILKLLIDKGVDINA 171
Ank_4 pfam13637
Ankyrin repeats (many copies);
449-502 1.33e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 1.33e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568905654  449 GWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIVKVLL 502
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 419-504 1.99e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.46  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 419 LLHIASiKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIV 498
Cdd:PTZ00322  86 LCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                 ....*.
gi 568905654 499 KVLLSH 504
Cdd:PTZ00322 165 QLLSRH 170
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 401-506 7.16e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 7.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 401 VKLSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHlKVVELLLqHNALVNTPGY 480
Cdd:PHA02874 175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDI 252

                         90       100
                 ....*....|....*....|....*..
gi 568905654 481 QNDSPLHDAVK-SGHIDIVKVLLSHGA 506
Cdd:PHA02874 253 DGSTPLHHAINpPCDIDIIDILLYHKA 279
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 415-511 1.37e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 415 RGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGH 494
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                         90
                 ....*....|....*..
gi 568905654 495 IDIVKVLLSHGASRNAV 511
Cdd:PHA02875 181 IAICKMLLDSGANIDYF 197
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
418-511 1.65e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 418 TLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDI 497
Cdd:COG0666   23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                         90
                 ....*....|....
gi 568905654 498 VKVLLSHGASRNAV 511
Cdd:COG0666  103 VKLLLEAGADVNAR 116
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 417-509 3.55e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 417 ETLLHIASIKGDIPSVEYLLQNG---NDPNVKDhaGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSG 493
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGkfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                         90
                 ....*....|....*.
gi 568905654 494 HIDIVKVLLSHGASRN 509
Cdd:PHA02875 147 DIKGIELLIDHKACLD 162
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 381-511 1.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 381 TPPPLLNNSTHRQMMSSPSTVKLSSGMPARKRNhrgeTLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHG 460
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKF----SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568905654 461 HLKVVELLLQHNALVNTPGYQND-SPLHDAVKSGHIDIVKVLLSHGASRNAV 511
Cdd:PHA02875 180 DIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 401-486 2.49e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 401 VKLSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQH--------- 471
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelga 179

                         90
                 ....*....|....*....
gi 568905654 472 ----NALVNTPGYQNDSPL 486
Cdd:PTZ00322 180 nakpDSFTGKPPSLEDSPI 198
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 419-501 3.11e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 419 LLHIASIkGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIV 498
Cdd:PLN03192 529 LLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF 607


                 ...
gi 568905654 499 KVL 501
Cdd:PLN03192 608 RIL 610
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 418-509 6.04e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 6.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 418 TLLHIASIKGDIpsVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDI 497
Cdd:PHA02874  95 SILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI 172

                         90
                 ....*....|..
gi 568905654 498 VKVLLSHGASRN 509
Cdd:PHA02874 173 IKLLLEKGAYAN 184
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 428-506 7.17e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 7.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 428 DIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQN-DSPLHDAVKSGHIDIVKVLLSHGA 506
Cdd:PHA02875  47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGA 126
PHA03095 PHA03095
ankyrin-like protein; Provisional
 413-511 1.55e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 413 NHRGE---TLLHI---ASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLH-EACSHGHLKVVELLLQHNALVNTPGYQNDSP 485
Cdd:PHA03095  41 NFRGEygkTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTP 120

                         90       100
                 ....*....|....*....|....*...
gi 568905654 486 LHD--AVKSGHIDIVKVLLSHGASRNAV 511
Cdd:PHA03095 121 LHVylSGFNINPKVIRLLLRKGADVNAL 148
RING-HC_AtBARD1-like cd23146
RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 ...
 38-83 2.08e-07

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: 47.47  E-value: 2.08e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568905654  38 LEKLLRCSRCANILKEPVCLGgCEHIFCSGCISDC--VGSGCPVCYTP 83
Cdd:cd23146    1 MELELKCPICLKLLNRPVLLP-CDHIFCSSCITDStkVGSDCPVCKLP 47
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 403-511 2.23e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 403 LSSGMPARKRNHRGETLLHIASIKG-DIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLK-VVELLLQHNALVNTPGY 480
Cdd:PHA02876 294 LERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDY 373

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568905654 481 QNDSPLHDAVKSGHIDIVKVLLSHGASRNAV 511
Cdd:PHA02876 374 CDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 449-476 3.12e-07

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: 46.43  E-value: 3.12e-07
                           10        20
                   ....*....|....*....|....*...
gi 568905654   449 GWTPLHEACSHGHLKVVELLLQHNALVN 476
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
 41-84 5.62e-07

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: 46.24  E-value: 5.62e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568905654  41 LLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSG---CPVCYTPA 84
Cdd:cd16544    2 ELTCPVCQEVLKDPVELPPCRHIFCKACILLALRSSgarCPLCRGPV 48
PHA03095 PHA03095
ankyrin-like protein; Provisional
 429-507 6.43e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 429 IPSVEYLLQNGNDPNVKDHAGWTPLHeACSHG---HLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDI--VKVLLS 503
Cdd:PHA03095  97 LDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLID 175


                 ....
gi 568905654 504 HGAS 507
Cdd:PHA03095 176 AGAD 179
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 427-505 6.55e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 6.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 427 GDIPSVEYLLQN-GNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIVKVLLSHG 505
Cdd:PHA02874  12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
 34-100 7.86e-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: 46.82  E-value: 7.86e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  34 ALARLEKLLRCSRCANILKEPVCLGgCEHIFCSGCISDC---VGSGCPVCYTPAWILDLKINRQLDSMIQ 100
Cdd:cd16596    2 RLTMMWEEVTCPICLDPFVEPVSIE-CGHSFCQECISQVgkgGGSVCPVCRQRFLLKNLRPNRQLANMVN 70
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 416-507 1.04e-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: 51.17  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 416 GETLLHIASIKGDIPSVEYLLQNG----NDPNVKD-HAGWTPLHEACSHGHLKVVELLLQHNALVNTPG----------- 479
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAApelvNEPMTSDlYQGETALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpgpk 130

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568905654 480 ---YQNDSPLHDAVKSGHIDIVKVLLSHGAS 507
Cdd:cd22192  131 nliYYGEHPLSFAACVGNEEIVRLLIEHGAD 161
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 449-476 1.09e-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: 44.97  E-value: 1.09e-06
                          10        20
                  ....*....|....*....|....*....
gi 568905654  449 GWTPLHEACSH-GHLKVVELLLQHNALVN 476
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 417-509 1.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 417 ETLLHIASIKGDIPS-----VEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVK 491
Cdd:PHA02876 141 ESIEYMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD 220

                         90
                 ....*....|....*...
gi 568905654 492 SGHIDIVKVLLSHGASRN 509
Cdd:PHA02876 221 SKNIDTIKAIIDNRSNIN 238
Ank_5 pfam13857
Ankyrin repeats (many copies);
412-456 1.66e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 1.66e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568905654  412 RNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEA 456
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 423-511 2.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 423 ASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNAL--VNTPGYQndSPLHDAVKSGHIDIVKV 500
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIpdVKYPDIE--SELHDAVEEGDVKAVEE 86

                         90
                 ....*....|.
gi 568905654 501 LLSHGASRNAV 511
Cdd:PHA02875  87 LLDLGKFADDV 97
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 33-100 2.45e-06

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: 49.62  E-value: 2.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654   33 AALARLEKLLRCSRCANILKEPVcLGGCEHIFCSGCISDC--VGSGCPVCYTPAWILDLKINRQLDSMIQ 100
Cdd:TIGR00599  18 PSLYPLDTSLRCHICKDFFDVPV-LTSCSHTFCSLCIRRClsNQPKCPLCRAEDQESKLRSNWLVSEIVE 86
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 449-477 2.74e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 43.79  E-value: 2.74e-06
                          10        20
                  ....*....|....*....|....*....
gi 568905654  449 GWTPLHEACSHGHLKVVELLLQHNALVNT 477
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 481-510 4.56e-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: 43.35  E-value: 4.56e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 568905654   481 QNDSPLHDAVKSGHIDIVKVLLSHGASRNA 510
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 418-506 6.79e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 6.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 418 TLLHIAsIKGDIP--SVEYLLQNGNDPNVKDHAGWTPLHEACSHG-HLKVVELLLQHNALVNTPGYQNDSPLHDAVksGH 494
Cdd:PHA02876 410 TALHFA-LCGTNPymSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EY 486

                         90
                 ....*....|..
gi 568905654 495 IDIVKVLLSHGA 506
Cdd:PHA02876 487 HGIVNILLHYGA 498
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
 38-95 9.68e-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: 43.23  E-value: 9.68e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568905654  38 LEKLLRCSRCANILKEPVCLGgCEHIFCSGCISD-CVGSG------CPVCYTPAWILDLKINRQL 95
Cdd:cd16598    1 LEEEVTCSICLDYLRDPVTID-CGHNFCRSCITDyCPISGgherpvCPLCRKPFKKENIRPNWQL 64
RING-HC_RING1-like cd16531
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and ...
 42-83 1.09e-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: 43.03  E-value: 1.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568905654  42 LRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSG---CPVCYTP 83
Cdd:cd16531    2 LMCPICLGIIKNTMTVKECLHRFCAECIEKALRLGnkeCPTCRKH 46
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 403-505 1.66e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 403 LSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVElLLQHNALVNTPGYQN 482
Cdd:PLN03192 545 LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASISDPHAAG 623

                         90       100
                 ....*....|....*....|...
gi 568905654 483 DSpLHDAVKSGHIDIVKVLLSHG 505
Cdd:PLN03192 624 DL-LCTAAKRNDLTAMKELLKQG 645
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
 38-89 1.71e-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: 42.29  E-value: 1.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568905654  38 LEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVG--SGCPVCYTPAWILDL 89
Cdd:cd16529    1 LDDLLRCPICFEYFNTAMMITQCSHNYCSLCIRRFLSykTQCPTCRAAVTESDL 54
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 42-80 1.76e-05

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: 41.70  E-value: 1.76e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568905654  42 LRCSRCANILKEPVCLGgCEHIFCSGCISDCVGSG---CPVC 80
Cdd:cd16449    1 LECPICLERLKDPVLLP-CGHVFCRECIRRLLESGsikCPIC 41
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
 34-83 1.93e-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: 43.44  E-value: 1.93e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568905654  34 ALARLEKLLRCSRCANILKEPVCLgGCEHIFCSGCISDCVGSG-----CPVCYTP 83
Cdd:cd16498    9 VISAMQKNLECPICLELLKEPVST-KCDHQFCRFCILKLLQKKkkpapCPLCKKS 62
Ank_5 pfam13857
Ankyrin repeats (many copies);
435-487 1.94e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568905654  435 LLQNGN-DPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLH 487
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 417-507 2.18e-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: 46.93  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 417 ETLLHIASIKGDIPSVEYLL-QNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQhNA--LVNTPG----YQNDSPLHDA 489
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AApeLVNEPMtsdlYQGETALHIA 96

                         90
                 ....*....|....*...
gi 568905654 490 VKSGHIDIVKVLLSHGAS 507
Cdd:cd22192   97 VVNQNLNLVRELIARGAD 114
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
 37-80 4.01e-05

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: 41.33  E-value: 4.01e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568905654  37 RLEKLLRCSRCANILKEPVCLGgCEHIFCSGCISDCVGSG----CPVC 80
Cdd:cd16608    2 SLKDELLCSICLSIYQDPVSLG-CEHYFCRQCITEHWSRSehrdCPEC 48
RING-HC_ScRAD18-like cd23148
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ...
 39-83 4.68e-05

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: 40.98  E-value: 4.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568905654  39 EKLLRCSRCANILKEPVcLGGCEHIFCSGCISDC--VGSGCPVCYTP 83
Cdd:cd23148    1 DHALRCHICKDLLKAPM-RTPCNHTFCSFCIRTHlnNDARCPLCKAE 46
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 431-510 6.76e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.43  E-value: 6.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 431 SVEYLLQNG--NDPNVKDHAgwTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHI-----DIVKVLLS 503
Cdd:PHA03100  17 NIKYIIMEDdlNDYSYKKPV--LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94


                 ....*..
gi 568905654 504 HGASRNA 510
Cdd:PHA03100  95 YGANVNA 101
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 415-444 7.55e-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: 39.93  E-value: 7.55e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 568905654  415 RGETLLHIASIKGDIPSVEYLLQNGNDPNV 444
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 403-504 8.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 8.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 403 LSSGMPARKRNHRGETLLHIASIK-GDIPSVEYLLQNGNDPNVKDHA-GWTPLHEACSHGhlKVVELLLQHNALVNTPGY 480
Cdd:PHA02878 221 LENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSE--RKLKLLLEYGADINSLNS 298

                         90       100
                 ....*....|....*....|....*
gi 568905654 481 QNDSPLHDAVKSGH-IDIVKVLLSH 504
Cdd:PHA02878 299 YKLTPLSSAVKQYLcINIGRILISN 323
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
 44-80 9.53e-05

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: 9.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568905654   44 CSRCANILKEPVCLGGCEHIFCSGCISDCVGSG---CPVC 80
Cdd:pfam00097   1 CPICLEEPKDPVTLLPCGHLFCSKCIRSWLESGnvtCPLC 40
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
 42-83 1.03e-04

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: 40.04  E-value: 1.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568905654  42 LRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSG---CPVCYTP 83
Cdd:cd16503    3 LTCSICQDLLHDCVSLQPCMHNFCAACYSDWMERSnteCPTCRAT 47
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 483-511 1.05e-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. 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: 39.58  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 568905654  483 DSPLHDAV-KSGHIDIVKVLLSHGASRNAV 511
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
mRING-HC-C3HC3D_TRAF7 cd16644
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 42-79 1.05e-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: 1.05e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568905654  42 LRCSRCANILKEPVcLGGCEHIFCSGCISDCVGSGCPV 79
Cdd:cd16644    6 LYCPLCQRVFKDPV-ITSCGHTFCRRCALTAPGEKCPV 42
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 415-447 1.21e-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. 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: 39.19  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568905654  415 RGETLLHIASIK-GDIPSVEYLLQNGNDPNVKDH 447
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 44-80 1.43e-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: 39.41  E-value: 1.43e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568905654    44 CSRCANILKEPVCLGGCEHIFCSGCISDCVGSG---CPVC 80
Cdd:smart00184   1 CPICLEEYLKDPVILPCGHTFCRSCIRKWLESGnntCPIC 40
Ank_2 pfam12796
Ankyrin repeats (3 copies);
416-446 1.93e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 1.93e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568905654  416 GETLLHIASIKGDIPSVEYLLQNGNDPNVKD 446
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
RING-HC_RNF166 cd16549
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; ...
 44-83 2.13e-04

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: 39.02  E-value: 2.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568905654  44 CSRCANILKEPVCLGGCEHIFCSGCISDCVGSG---CPVCYTP 83
Cdd:cd16549    4 CPICLEVYHKPVVITSCGHTFCGECLQPCLQVAsplCPLCRMP 46
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
 38-95 2.70e-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: 2.70e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568905654  38 LEKLLRCSRCANILKEPVCLGgCEHIFCSGCIS----DCVGSGCPVCYTPAWILDLKINRQL 95
Cdd:cd16599    1 FKEELLCPICYEPFREAVTLR-CGHNFCKGCVSrsweRQPRAPCPVCKEASSSDDLRTNHTL 61
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 403-511 3.50e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 403 LSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEA-CSHGHLKVVELLLQHNALVNTPGYQ 481
Cdd:PHA02876 362 LELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKD 441

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568905654 482 NDSPLHDAVKSG-HIDIVKVLLSHGASRNAV 511
Cdd:PHA02876 442 LSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
 42-80 3.52e-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: 38.23  E-value: 3.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568905654  42 LRCSRCANILKEPVCLGgCEHIFCSGCIS----DCVGS-GCPVC 80
Cdd:cd16601    2 ASCSLCKEYLKDPVIIE-CGHNFCRACITrfweELDGDfPCPQC 44
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
34-111 4.30e-04

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


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 42.77  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  34 ALARLEKLLRCSRCANILKEPvCLGGCEHIFCSGCISDCVGS--GCPVCYTPAWILDLKINRQLDSMIQLSSKLQNLLHD 111
Cdd:COG5432   18 SLKGLDSMLRCRICDCRISIP-CETTCGHTFCSLCIRRHLGTqpFCPVCREDPCESRLRGSSGSREINESHARNRDLLRK 96
RING-HC_TRIM41-like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
 44-80 4.34e-04

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: 38.37  E-value: 4.34e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568905654  44 CSRCANILKEPVCLGgCEHIFCSGCISDCVGSGCPVC 80
Cdd:cd16602    6 CAICLDYFKDPVSIG-CGHNFCRVCVTQLWGFTCPQC 41
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
 42-83 5.95e-04

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: 37.77  E-value: 5.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568905654  42 LRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSG---CPVCYTP 83
Cdd:cd16620    4 LKCPICKDLMKDAVLTPCCGNSFCDECIRTALLEEdftCPTCKEP 48
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 415-444 6.10e-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: 6.10e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568905654   415 RGETLLHIASIKGDIPSVEYLLQNGNDPNV 444
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
RING-HC_PRT1-like cd23132
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and ...
 44-83 6.22e-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: 6.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568905654  44 CSRCANILKEPVCLGgCEHIFCSGCISDCVG----SGCPVCYTP 83
Cdd:cd23132    5 CCICLDLLYKPVVLE-CGHVFCFWCVHRCMNgydeSHCPLCRRP 47
Ank_5 pfam13857
Ankyrin repeats (many copies);
468-510 6.35e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 6.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568905654  468 LLQH-NALVNTPGYQNDSPLHDAVKSGHIDIVKVLLSHGASRNA 510
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL 44
RING-HC_AtBRCA1-like cd23147
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 ...
 38-84 7.25e-04

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: 37.83  E-value: 7.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568905654  38 LEKLLRCSRCANILKEPVCLGgCEHIFCSGCI--SDCVGSGCPVCYTPA 84
Cdd:cd23147    1 LGKELKCPICLSLFKSAANLS-CNHCFCAGCIgeSLKLSAICPVCKIPA 48
PHA03095 PHA03095
ankyrin-like protein; Provisional
 397-511 7.81e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 7.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 397 SPSTVKL--SSGMPARKRNHRGETLLHI--ASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLK--VVELLLQ 470
Cdd:PHA03095 166 NVELLRLliDAGADVYAVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLI 245

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568905654 471 HNALVNTPGYQNDSPLHDAVKSGHIDIVKVLLSHGASRNAV 511
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
 37-93 7.86e-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: 37.67  E-value: 7.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568905654  37 RLEKLLRCSRCANILKEPVCLGgCEHIFCSGCISDCVGSG-----CPVCYTPAWILDLKINR 93
Cdd:cd16594    1 SLQEELTCPICLDYFTDPVTLD-CGHSFCRACIARCWEEPetsasCPQCRETCPQRNLRPNR 61
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
 39-84 1.24e-03

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: 36.97  E-value: 1.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568905654  39 EKLLRCSRCANILKEPVCLGgCEHIFCSGCISDC------VGSGCPVCYTPA 84
Cdd:cd16609    1 EEELTCSICLGLYQDPVTLP-CQHSFCRACIEDHwrqkdeGSFSCPECRAPF 51
mRING-HC-C3HC3D_Nrdp1 cd16634
Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation ...
 42-79 1.35e-03

Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation protein-1 (Nrdp1) and similar proteins; Nrdp1 (referred to as FLRF in mice), also known as RING finger protein 41 (RNF41), is an E3 ubiquitin-protein ligase that plays a critical role in the regulation of cell growth and apoptosis, inflammation and production of reactive oxygen species (ROS), as well as in doxorubicin (DOX)-induced cardiac injury. It promotes the degradation of the epidermal growth factor receptor (EGFR/ErbB) family member, ErbB3, which is independent of growth factor stimulation. It also promotes M2 macrophage polarization by ubiquitinating and activating transcription factor CCAAT/enhancer-binding protein beta (C/EBPbeta) via Lys-63-linked ubiquitination. Moreover, Nrdp1 interacts with and modulates the activity of Parkin, a causative protein for early onset recessive juvenile parkinsonism (AR-JP). It also interacts with ubiquitin-specific protease 8 (USP8), which is involved in trafficking of various transmembrane proteins. Furthermore, Nrdp1 inhibits basal lysosomal degradation and enhances ectodomain shedding of JAK2-associated cytokine receptors. Its phosphorylation by the kinase Par-1b (also known as MARK2) is required for epithelial cell polarity. Nrdp1 contains an N-terminal modified C3HC3D-type RING-HC finger required for enhancing ErbB3 degradation, a B-box, a coiled-coil domain responsible for Nrdp1 oligomerization, and a C-terminal ErbB3-binding domain.


Pssm-ID: 438296 [Multi-domain]  Cd Length: 43  Bit Score: 36.63  E-value: 1.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568905654  42 LRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSG--CPV 79
Cdd:cd16634    2 LICPICSGVLEEPLQAPHCEHAFCNACITEWLSRQqtCPV 41
RING-HC_RAG1 cd16530
RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar ...
 40-83 1.40e-03

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: 36.65  E-value: 1.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568905654  40 KLLRCSRCANILKEPVCLGgCEHIFCSGCISDCV---GSGCPVCYTP 83
Cdd:cd16530    1 KSVSCQVCEHILADPVQTP-CKHLFCRTCILKCLkvmGSYCPSCRYP 46
zf-C3HC4_4 pfam15227
zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like ...
 44-80 1.42e-03

zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development. This domain is likely to be DNA-binding. This zinc-finger domain together with the RDM domain, pfam11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme.


Pssm-ID: 464570 [Multi-domain]  Cd Length: 42  Bit Score: 36.64  E-value: 1.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568905654   44 CSRCANILKEPVCLGgCEHIFCSGCIS------DCVGSGCPVC 80
Cdd:pfam15227   1 CPICLDYLEKPVSIE-CGHSFCLSCINslqkepDGESLLCPQC 42
PHA02946 PHA02946
ankyin-like protein; Provisional
 425-509 1.43e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 425 IKG-DIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLH--DAVKSGHIDIVKVL 501
Cdd:PHA02946  47 IKGlDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLL 126


                 ....*...
gi 568905654 502 LSHGASRN 509
Cdd:PHA02946 127 VQYGAKIN 134
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
 38-80 1.72e-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: 36.90  E-value: 1.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568905654  38 LEKLLRCSRCANILKEPVCLgGCEHIFCSGCIS----DCVGSG--CPVC 80
Cdd:cd16597    2 LEEELTCSICLELFKDPVTL-PCGHNFCGVCIEktwdSQHGSEysCPQC 49
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
 44-90 1.82e-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: 36.45  E-value: 1.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568905654  44 CSRCaniLKEPVC--LGGCEHIFCSGCI------SDCVGSGCPVCYTPAWILDLK 90
Cdd:cd16536    3 CPIC---LEPPVAprITRCGHIFCWPCIlrylslSEKKWRKCPICFESIHKKDLR 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 412-469 1.83e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 1.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568905654 412 RNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLL 469
Cdd:PHA03095 253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
zf-RING_5 pfam14634
zinc-RING finger domain;
43-80 2.07e-03

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 35.87  E-value: 2.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568905654   43 RCSRCAN--ILKEPVCLGGCEHIFCSGCISDCVGSG-CPVC 80
Cdd:pfam14634   1 HCNKCFKelSKTRPFYLTSCGHIFCEECLTRLLQERqCPIC 41
RING-HC_TRIM58_C-IV cd16606
RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar ...
 43-83 2.31e-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: 36.38  E-value: 2.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568905654  43 RCSRCANILKEPVCLGgCEHIFCSGCIS------DCVGSG---CPVCYTP 83
Cdd:cd16606    4 RCPVCLDFLQEPVSVD-CGHSFCLRCISefceksDSAQGGvyaCPQCRGP 52
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
 44-95 2.40e-03

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


Pssm-ID: 438253 [Multi-domain]  Cd Length: 72  Bit Score: 36.65  E-value: 2.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  44 CSRCANILKEPVCLGgCEHIFCSGCISDCVG--------SGCPVCYTPAWILDLKINRQL 95
Cdd:cd16591    9 CPICLELLTEPLSLD-CGHSFCQACITANHKesvnqegeSSCPVCRTSYQPENLRPNRHL 67
mRING-HC-C3HC3D_TRAF4-like cd23126
Modified RING finger, HC subclass (C3HC3D-type), found in uncharacterized proteins similar to ...
 38-79 2.78e-03

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: 35.78  E-value: 2.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568905654  38 LEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDC--VGSGCPV 79
Cdd:cd23126    1 LDKKYECPVCCQVLRYPVQFEECGHRVCSSCLPELlrVEPRCPI 44
RING-HC_TRIM8_C-V cd16580
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ...
 38-80 2.82e-03

RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar proteins; TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53 impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF- kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V 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 domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.


Pssm-ID: 438242 [Multi-domain]  Cd Length: 67  Bit Score: 36.41  E-value: 2.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568905654  38 LEKLLRCSRCANILKEPVCLGgCEHIFCSGCIS-----DCVGSGCPVC 80
Cdd:cd16580    8 FEEELICPICLHVFVEPVQLP-CKHNFCRGCIGeawakDAGLVRCPEC 54
RING-HC_TRIM47-like_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
 42-84 2.94e-03

RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar proteins; TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), 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, 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. It plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. This subfamily also includes RING finger protein 135 (RNF135). RNF135, also known as RIG-I E3 ubiquitin ligase (REUL) or Riplet, is a widely expressed E3 ubiquitin-protein ligase that consists of an N-terminal C3HC4-type RING-HC finger and C-terminal B30.2/SPRY and PRY motifs, but lacks the B-box and coiled-coil domains that are also typically present in TRIM proteins. RNF135 serves as a specific retinoic acid-inducible gene-I (RIG-I)-interacting protein that ubiquitinates RIG-I and specifically stimulates RIG-I-mediated innate antiviral activity to produce antiviral type-I interferon (IFN) during the early phase of viral infection. It also has been identified as a bio-marker and therapy target of glioblastoma. It associates with the ERK signal transduction pathway and plays a role in glioblastoma cell proliferation, migration and cell cycle.


Pssm-ID: 438266 [Multi-domain]  Cd Length: 49  Bit Score: 35.86  E-value: 2.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568905654  42 LRCSRCANILKEPVCLGgCEHIFCSGCISDCVGSG------CPVCYTPA 84
Cdd:cd16604    1 LSCPICLDLLKDPVTLP-CGHSFCMGCLGALWGAGrggrasCPLCRQTF 48
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
 42-99 3.21e-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: 36.22  E-value: 3.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654  42 LRCSRCANILKEPVCLGgCEHIFCSGCISDC--VGSGCPVCYTPawILDLKINRQLDSMI 99
Cdd:cd16535    2 LQCSICSELFIEAVTLN-CSHSFCSYCITEWmkRKKECPICRKP--ITSKTRSLVLDNCI 58
RING-HC_LONFs_rpt2 cd16514
second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
 42-83 3.59e-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: 35.32  E-value: 3.59e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568905654  42 LRCSRCANILKEPVCLGgCEHIFCSGCISDCV--GSGCPVCYTP 83
Cdd:cd16514    2 LECSLCLRLLYEPVTTP-CGHTFCRACLERCLdhSPKCPLCRTS 44
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
 42-80 3.82e-03

RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 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: 438273 [Multi-domain]  Cd Length: 59  Bit Score: 35.89  E-value: 3.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568905654  42 LRCSRCANILKEPVCLGgCEHIFCSGCISDCVGSG-----CPVC 80
Cdd:cd16611    5 LHCPLCLDFFRDPVMLS-CGHNFCQSCITGFWELQaedttCPEC 47
Ank_4 pfam13637
Ankyrin repeats (many copies);
391-436 3.86e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 3.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568905654  391 HRQMMSSP-STVK--LSSGMPARKRNHRGETLLHIASIKGDIPSVEYLL 436
Cdd:pfam13637   6 HAAAASGHlELLRllLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 414-483 3.93e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.85  E-value: 3.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 414 HRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQND 483
Cdd:PLN03192 620 HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
Ank_4 pfam13637
Ankyrin repeats (many copies);
482-511 4.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 4.39e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 568905654  482 NDSPLHDAVKSGHIDIVKVLLSHGASRNAV 511
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 484-510 4.87e-03

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: 34.54  E-value: 4.87e-03
                          10        20
                  ....*....|....*....|....*..
gi 568905654  484 SPLHDAVKSGHIDIVKVLLSHGASRNA 510
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
 44-80 5.04e-03

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may be associated with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can form a huge ring-shaped oligomeric complex.


Pssm-ID: 438223 [Multi-domain]  Cd Length: 50  Bit Score: 35.33  E-value: 5.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 568905654  44 CSRCANILKEPVCLGgCEHIFCSGCISDCV--GSGCPVC 80
Cdd:cd16561    5 CSICLEDLNDPVKLP-CDHVFCEECIRQWLpgQMSCPLC 42
RING-HC_LNX4 cd16719
RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4); LNX4, also known as PDZ ...
 42-69 5.15e-03

RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4); LNX4, also known as PDZ domain-containing RING finger protein 4 (PDZRN4), or SEMACAP3-like protein (SEMCAP3L), is an E3 ubiquitin-protein ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX4 contains an N-terminal C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 438379 [Multi-domain]  Cd Length: 53  Bit Score: 35.29  E-value: 5.15e-03
                         10        20
                 ....*....|....*....|....*...
gi 568905654  42 LRCSRCANILKEPVCLGgCEHIFCSGCI 69
Cdd:cd16719    5 LKCKLCGKVLEEPLSTP-CGHVFCAGCL 31
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 416-487 5.82e-03

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: 39.23  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905654 416 GETLLHIASIKGDIPSVEYLLQNGND------------PNVKD--HAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQ 481
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                 ....*.
gi 568905654 482 NDSPLH 487
Cdd:cd22192  169 GNTVLH 174
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
43-80 9.76e-03

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 33.95  E-value: 9.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568905654   43 RCSRCANILKEPVCLGGCEHIFCSGCISDCVGSG--CPVC 80
Cdd:pfam13923   1 MCPICMDMLKDPSTTTPCGHVFCQDCILRALRAGneCPLC 40
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
 44-80 9.99e-03

RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, HIP116, RING finger protein 80, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.


Pssm-ID: 438172 [Multi-domain]  Cd Length: 53  Bit Score: 34.59  E-value: 9.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568905654  44 CSRCANILKEPVcLGGCEHIFCSGCISDCVGS---GCPVC 80
Cdd:cd16509    6 CAICLDSLTNPV-ITPCAHVFCRRCICEVIQRekaKCPMC 44
 
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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