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Conserved domains on  [gi|2123772412|ref|NP_001026417|]
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BRCA1-associated RING domain protein 1 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRCT_Bard1_rpt2 cd17720
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ...
 669-769 3.34e-46

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


:

Pssm-ID: 349352  Cd Length: 101  Bit Score: 159.84  E-value: 3.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 669 LFDGCYFYFLGSFNSHQ-KSDLVELVKAGGGQILVRQPKPDSDVTQTINTVAYhAESTSDQRFCTQYVIYDASSKFKPEK 747
Cdd:cd17720     1 LFDGCHFYFHGTFKPPTtKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 2123772412 748 IRQGKVWFAPSSWIVDCIMSFQ 769
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 28-113 3.65e-46

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: 159.04  E-value: 3.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412  28 PWAHTRAALERLERALSCSRCAGVLREPVSLGGCEHVFCLSCMGDHVGKGCPVCHVPAWVQDMQINRQLDDMVQLCGKLR 107
Cdd:cd16496     1 KWARTRAALDELENLLRCSRCASILKEPVTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLR 80


                  ....*.
gi 2123772412 108 HLLDAG 113
Cdd:cd16496    81 NLLNDN 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
420-544 2.10e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 2.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 420 IARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHD 499
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2123772412 500 AAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYAESEKMKSVLML 544
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 570-644 1.53e-31

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


:

Pssm-ID: 349366  Cd Length: 80  Bit Score: 117.70  E-value: 1.53e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123772412 570 ILGSGLSSKQQKLLNKLATVLKARRCTEFNSTVTHVVVPDVP---MPSTVKCMMAVLSGCWVLKFEWVQACLQSTVRE 644
Cdd:cd17734     3 LLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
 
Name Accession Description Interval E-value
BRCT_Bard1_rpt2 cd17720
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ...
 669-769 3.34e-46

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


Pssm-ID: 349352  Cd Length: 101  Bit Score: 159.84  E-value: 3.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 669 LFDGCYFYFLGSFNSHQ-KSDLVELVKAGGGQILVRQPKPDSDVTQTINTVAYhAESTSDQRFCTQYVIYDASSKFKPEK 747
Cdd:cd17720     1 LFDGCHFYFHGTFKPPTtKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 2123772412 748 IRQGKVWFAPSSWIVDCIMSFQ 769
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 28-113 3.65e-46

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: 159.04  E-value: 3.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412  28 PWAHTRAALERLERALSCSRCAGVLREPVSLGGCEHVFCLSCMGDHVGKGCPVCHVPAWVQDMQINRQLDDMVQLCGKLR 107
Cdd:cd16496     1 KWARTRAALDELENLLRCSRCASILKEPVTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLR 80


                  ....*.
gi 2123772412 108 HLLDAG 113
Cdd:cd16496    81 NLLNDN 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
420-544 2.10e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 2.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 420 IARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHD 499
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2123772412 500 AAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYAESEKMKSVLML 544
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 570-644 1.53e-31

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


Pssm-ID: 349366  Cd Length: 80  Bit Score: 117.70  E-value: 1.53e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123772412 570 ILGSGLSSKQQKLLNKLATVLKARRCTEFNSTVTHVVVPDVP---MPSTVKCMMAVLSGCWVLKFEWVQACLQSTVRE 644
Cdd:cd17734     3 LLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
431-518 1.85e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 103.66  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 431 LHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHkALVNSTGYQNdSPLHDAAKNGHVSIVE 510
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78


                  ....*...
gi 2123772412 511 LLLLHGAS 518
Cdd:pfam12796  79 LLLEKGAD 86
zf-RING_6 pfam14835
zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer ...
 36-100 5.47e-25

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: 98.58  E-value: 5.47e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123772412  36 LERLERALSCSRCAGVLREPVSLGGCEHVFCLSCMGDHVGKGCPVCHVPAWVQDMQINRQLDDMV 100
Cdd:pfam14835   1 LDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI 65
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 423-516 1.63e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 423 RNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAK 502
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                          90
                  ....*....|....
gi 2123772412 503 NGHVSIVELLLLHG 516
Cdd:PHA02874  200 YGDYACIKLLIDHG 213
BRCT smart00292
breast cancer carboxy-terminal domain;
667-765 2.06e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 54.69  E-value: 2.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412  667 PKLFDGCYFYFLGSFNSHQKSDLVELVKAGGGQILVRQPKPDsdvtqtintvayhaestsdqrfcTQYVIY--DASSKFK 744
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVgsPEGGKLE 57

                           90       100
                   ....*....|....*....|.
gi 2123772412  745 PEKIRQGKVWFAPSSWIVDCI 765
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 428-518 1.07e-07

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: 55.40  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 428 ETLLHIASIKGDLAAVEELLK-NGADPNVKDNAGWTPLHEACNHGHQEVVELLLQH-KALVN----STGYQNDSPLHDAA 501
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNepmtSDLYQGETALHIAV 97

                          90
                  ....*....|....*..
gi 2123772412 502 KNGHVSIVELLLLHGAS 518
Cdd:cd22192    98 VNQNLNLVRELIARGAD 114
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 666-774 1.03e-06

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


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 46.97  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 666 LPKLFDGCYFYfLGSFNSHQKSDLVELVKAGGGQIlvrqpkpdsdvtqtintvayhaesTSDQRFCTQYVIYDASSKFKP 745
Cdd:pfam16589   1 LPNLFEPLRFY-INAIPSPSRSKLKRLIEANGGTV------------------------VDNINPAVYIVIAPYNKTDKL 55

                          90       100
                  ....*....|....*....|....*....
gi 2123772412 746 EKIRqgKVWFAPSSWIVDCIMSFQLLPVK 774
Cdd:pfam16589  56 AENT--KLGVVSPQWIFDCVKKGKLLPLE 82
BRCT smart00292
breast cancer carboxy-terminal domain;
571-638 2.71e-06

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 45.83  E-value: 2.71e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2123772412  571 LGSGLSSKQQKLLNKLATVLKARRCTEFNS-TVTHVVVPDvPMPSTVKCMMAVLSGCWVLKFEWVQACL 638
Cdd:smart00292  11 ITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIVGS-PEGGKLELLKAIALGIPIVKEEWLLDCL 78
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 460-487 3.56e-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: 44.12  E-value: 3.56e-06
                           10        20
                   ....*....|....*....|....*...
gi 2123772412  460 GWTPLHEACNHGHQEVVELLLQHKALVN 487
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 422-518 4.09e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.92  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 422 RRNYKGETLLHIASiKGDLAAVEELL--------KNGADPNVKDNA------GWTPLHEACNHGHQEVVELLLQHKALVN 487
Cdd:TIGR00870  77 CRGAVGDTLLHAIS-LEYVDAVEAILlhllaafrKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVP 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2123772412 488 ---------STGYQN-----DSPLHDAAKNGHVSIVELLLLHGAS 518
Cdd:TIGR00870 156 aracgdffvKSQGVDsfyhgESPLNAAACLGSPSIVALLSEDPAD 200
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
43-116 7.16e-04

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 42.81  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412  43 LSCSRCAGVLREPVSLGGCEHVFCLSCMGDHV---GKGCPVCH-----VPAWVQDMQINRQLDDMVQLCGKLrhlldAGT 114
Cdd:COG5222   275 LKCPLCHCLLRNPMKTPCCGHTFCDECIGTALldsDFKCPNCSrkdvlLDGLTPDIDKKLEVEKALKKQRKK-----VGT 349


                  ..
gi 2123772412 115 SD 116
Cdd:COG5222   350 SD 351
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 573-638 2.05e-03

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


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 37.66  E-value: 2.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123772412 573 SGLSSKQQKLLNKLATVLKARRCTEFNSTVTHVVVPdvpmPSTVKCMMAVLSGCWVLKFEWVQACL 638
Cdd:pfam00533  14 TGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVE----ARTKKYLKAKELGIPIVTEEWLLDCI 75
 
Name Accession Description Interval E-value
BRCT_Bard1_rpt2 cd17720
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ...
 669-769 3.34e-46

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


Pssm-ID: 349352  Cd Length: 101  Bit Score: 159.84  E-value: 3.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 669 LFDGCYFYFLGSFNSHQ-KSDLVELVKAGGGQILVRQPKPDSDVTQTINTVAYhAESTSDQRFCTQYVIYDASSKFKPEK 747
Cdd:cd17720     1 LFDGCHFYFHGTFKPPTtKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 2123772412 748 IRQGKVWFAPSSWIVDCIMSFQ 769
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 28-113 3.65e-46

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: 159.04  E-value: 3.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412  28 PWAHTRAALERLERALSCSRCAGVLREPVSLGGCEHVFCLSCMGDHVGKGCPVCHVPAWVQDMQINRQLDDMVQLCGKLR 107
Cdd:cd16496     1 KWARTRAALDELENLLRCSRCASILKEPVTLGGCEHVFCRSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLR 80


                  ....*.
gi 2123772412 108 HLLDAG 113
Cdd:cd16496    81 NLLNDN 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
420-544 2.10e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 2.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 420 IARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHD 499
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2123772412 500 AAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYAESEKMKSVLML 544
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
416-533 2.36e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 2.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 416 GSNPIARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDS 495
Cdd:COG0666    76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2123772412 496 PLHDAAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYA 533
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 570-644 1.53e-31

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


Pssm-ID: 349366  Cd Length: 80  Bit Score: 117.70  E-value: 1.53e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123772412 570 ILGSGLSSKQQKLLNKLATVLKARRCTEFNSTVTHVVVPDVP---MPSTVKCMMAVLSGCWVLKFEWVQACLQSTVRE 644
Cdd:cd17734     3 LLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
420-533 1.97e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 1.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 420 IARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHD 499
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2123772412 500 AAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYA 533
Cdd:COG0666   226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
Ank_2 pfam12796
Ankyrin repeats (3 copies);
431-518 1.85e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 103.66  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 431 LHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHkALVNSTGYQNdSPLHDAAKNGHVSIVE 510
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78


                  ....*...
gi 2123772412 511 LLLLHGAS 518
Cdd:pfam12796  79 LLLEKGAD 86
zf-RING_6 pfam14835
zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer ...
 36-100 5.47e-25

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: 98.58  E-value: 5.47e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123772412  36 LERLERALSCSRCAGVLREPVSLGGCEHVFCLSCMGDHVGKGCPVCHVPAWVQDMQINRQLDDMV 100
Cdd:pfam14835   1 LDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
418-533 9.82e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 9.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 418 NPIARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPL 497
Cdd:COG0666    45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2123772412 498 HDAAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYA 533
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
416-528 7.54e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 7.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 416 GSNPIARrNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDS 495
Cdd:COG0666   176 GADVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2123772412 496 PLHDAAKNGHVSIVELLLLHGASRDAVNIFGLR 528
Cdd:COG0666   255 ALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 423-516 1.63e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 423 RNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAK 502
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                          90
                  ....*....|....
gi 2123772412 503 NGHVSIVELLLLHG 516
Cdd:PHA02874  200 YGDYACIKLLIDHG 213
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 424-551 2.67e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 2.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 424 NYKGETLLHIA--SIKGDLAAVEELLKNGADPNVK----------------DNAGWTPLHEACNHGHQEVVELLLQHKAL 485
Cdd:PHA03100  138 NSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2123772412 486 VNSTGYQNDSPLHDAAKNGHVSIVELLLLHGASRDAVN----IFGLRPVDYAESEKM--KSVLMLPVKNESF 551
Cdd:PHA03100  218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIetllYFKDKDLNTITKIKMlkKSIMYMFLLDPGF 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
427-489 8.38e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 8.38e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2123772412 427 GETLLHIASIKGDLAAVEELLKNgADPNVKDNaGWTPLHEACNHGHQEVVELLLQHKALVNST 489
Cdd:pfam12796  30 GRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
429-480 1.26e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.06  E-value: 1.26e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2123772412 429 TLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLL 480
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 570-637 1.61e-12

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


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 63.15  E-value: 1.61e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123772412 570 ILGSGLSSKQQKLLNKLATVLKARRCTEFNSTVTHVVVPDVpmPSTVKCMMAVLSGCWVLKFEWVQAC 637
Cdd:cd00027     3 ICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSP--SGEKYYLAALAWGIPIVSPEWLLDC 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
460-513 1.65e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.68  E-value: 1.65e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2123772412 460 GWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHVSIVELLL 513
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 420-531 7.36e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 7.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 420 IARRNYKGE---TLLHI---ASIKGDLAAVEELLKNGADPNVKDNAGWTPLH-EACNHGHQEVVELLLQHKALVNSTGYQ 492
Cdd:PHA03095   37 GADVNFRGEygkTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKV 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2123772412 493 NDSPLHD--AAKNGHVSIVELLLLHGASRDAVNIFGLRPVD 531
Cdd:PHA03095  117 GRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 446-535 1.97e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.21  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 446 LLKNGADPNVKD-NAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHVSIVELLLLHGASRDAVNI 524
Cdd:PHA02878  153 LLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232

                          90
                  ....*....|.
gi 2123772412 525 FGLRPVDYAES 535
Cdd:PHA02878  233 CGNTPLHISVG 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
418-533 3.90e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.59  E-value: 3.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 418 NPIARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPL 497
Cdd:COG0666    12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2123772412 498 HDAAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYA 533
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 426-560 4.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 426 KGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKN-G 504
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2123772412 505 HVSIVELLLLHGASRDAVN-IFGLRPVDYAESEKMKSVLMLPVKNESFSFSQPSESP 560
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSyILGLTALHSSIKSERKLKLLLEYGADINSLNSYKLTP 303
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 443-533 4.72e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 443 VEELLKNGADPNVKDNAGWTPLHEACNHGH-----QEVVELLLQHKALVNSTGYQNDSPLHDAA--KNGHVSIVELLLLH 515
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDN 130

                          90
                  ....*....|....*...
gi 2123772412 516 GASRDAVNIFGLRPVDYA 533
Cdd:PHA03100  131 GANVNIKNSDGENLLHLY 148
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 430-515 5.37e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.07  E-value: 5.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 430 LLHIASiKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHVSIV 509
Cdd:PTZ00322   86 LCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                  ....*.
gi 2123772412 510 ELLLLH 515
Cdd:PTZ00322  165 QLLSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
464-533 1.18e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.18e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 464 LHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHVSIVELLLLHGASRDAVNifGLRPVDYA 533
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYA 68
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 429-525 2.26e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 429 TLLHIAS-----IKGDLAAVEELLKNGADPNVKDNAGWTPLHEA-CNH-GHQEVVELLLQHKALVNSTGYQNDSPLHDAA 501
Cdd:PHA03100   70 TPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAiSKKsNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149

                          90       100
                  ....*....|....*....|....*....
gi 2123772412 502 KNGHV--SIVELLLLHGASRDA---VNIF 525
Cdd:PHA03100  150 ESNKIdlKILKLLIDKGVDINAknrVNYL 178
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 418-537 4.39e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 418 NPIARRNYKG-ETLLHIASIKGDLAAVEELLKNGADPN-VKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDS 495
Cdd:PHA02875   58 GAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFS 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2123772412 496 PLHDAAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYAESEK 537
Cdd:PHA02875  138 PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 423-549 5.98e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.29  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 423 RNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHgHQEVVELLLQHKAlVNSTGYQNDSPLHDAAK 502
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNAS-INDQDIDGSTPLHHAIN 263

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2123772412 503 NG-HVSIVELLLLHGASRDAVNIFGLRPVDYAesekMKSVLMLPVKNE 549
Cdd:PHA02874  264 PPcDIDIIDILLYHKADISIKDNKGENPIDTA----FKYINKDPVIKD 307
Ank_5 pfam13857
Ankyrin repeats (many copies);
416-467 8.39e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 55.05  E-value: 8.39e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2123772412 416 GSNPIARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEA 467
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 401-482 1.10e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 401 DQVGIpqspSVFKSPGSNPIARrNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLL 480
Cdd:PTZ00322   94 DAVGA----RILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                  ..
gi 2123772412 481 QH 482
Cdd:PTZ00322  169 RH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 430-512 1.35e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 430 LLHIASIkGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHVSIV 509
Cdd:PLN03192  529 LLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF 607


                  ...
gi 2123772412 510 ELL 512
Cdd:PLN03192  608 RIL 610
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 570-653 1.40e-09

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 55.82  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 570 ILGSGLSSKQQKLLNKLATVLKARRCTEFNSTVTHVVV-PDVPM--PSTVKCMMAVLSGCWVLKFEWVQACLQSTVREQE 646
Cdd:cd17735     3 MVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMkTDAELvcERTLKYFLGIAGRKWVVSYQWITQSIKEGKILPE 82


                  ....*..
gi 2123772412 647 EKYEIQG 653
Cdd:cd17735    83 HDFEVRG 89
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 426-529 2.01e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 426 KGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGH 505
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                          90       100
                  ....*....|....*....|....
gi 2123772412 506 VSIVELLLLHGASrdaVNIFGLRP 529
Cdd:PHA02875  181 IAICKMLLDSGAN---IDYFGKNG 201
BRCT smart00292
breast cancer carboxy-terminal domain;
667-765 2.06e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 54.69  E-value: 2.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412  667 PKLFDGCYFYFLGSFNSHQKSDLVELVKAGGGQILVRQPKPDsdvtqtintvayhaestsdqrfcTQYVIY--DASSKFK 744
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVgsPEGGKLE 57

                           90       100
                   ....*....|....*....|.
gi 2123772412  745 PEKIRQGKVWFAPSSWIVDCI 765
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 423-523 1.21e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 423 RNYKGETLLHIASIKG-DLAAVEELLKNGADPNVKDNAGWTPLHEACN-HGHQEVVELLLQHKALVNSTGYQNDSPLHDA 500
Cdd:PHA02876  303 KNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYA 382

                          90       100
                  ....*....|....*....|...
gi 2123772412 501 AKNGHVSIVELLLLHGASRDAVN 523
Cdd:PHA02876  383 AVRNNVVIINTLLDYGADIEALS 405
Ank_5 pfam13857
Ankyrin repeats (many copies);
479-533 5.12e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 5.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2123772412 479 LLQHK-ALVNSTGYQNDSPLHDAAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYA 533
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 446-537 5.70e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 5.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 446 LLKNGADPNVKDNAGWTPLHeACNHG---HQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHVSI--VELLLLHGASRD 520
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVY 181

                          90
                  ....*....|....*...
gi 2123772412 521 AVNIFGLRPVDY-AESEK 537
Cdd:PHA03095  182 AVDDRFRSLLHHhLQSFK 199
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 431-533 9.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 9.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 431 LHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHvSIVE 510
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIE 239

                          90       100
                  ....*....|....*....|...
gi 2123772412 511 lLLLHGASRDAVNIFGLRPVDYA 533
Cdd:PHA02874  240 -LLINNASINDQDIDGSTPLHHA 261
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 428-518 1.07e-07

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: 55.40  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 428 ETLLHIASIKGDLAAVEELLK-NGADPNVKDNAGWTPLHEACNHGHQEVVELLLQH-KALVN----STGYQNDSPLHDAA 501
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNepmtSDLYQGETALHIAV 97

                          90
                  ....*....|....*..
gi 2123772412 502 KNGHVSIVELLLLHGAS 518
Cdd:cd22192    98 VNQNLNLVRELIARGAD 114
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 419-498 1.42e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 419 PIARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQH----KALVNSTGYQND 494
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNgpsiKTIIETLLYFKD 263


                  ....
gi 2123772412 495 SPLH 498
Cdd:PHA03100  264 KDLN 267
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 426-548 2.02e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 426 KGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNStgYQNDSPLHDAAKNGH 505
Cdd:PLN03192  557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLLCTAAKRND 634

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2123772412 506 VSIVELLLLHGASRDAVNIFGLRPVDYAESEKMKSVLMLPVKN 548
Cdd:PLN03192  635 LTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMN 677
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
 35-101 2.26e-07

RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting it may be a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated with uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438258 [Multi-domain]  Cd Length: 77  Bit Score: 48.74  E-value: 2.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412  35 ALERLERALSCSRCAGVLREPVSLGgCEHVFCLSCM---GDHVGKGCPVCHVPAWVQDMQINRQLDDMVQ 101
Cdd:cd16596     2 RLTMMWEEVTCPICLDPFVEPVSIE-CGHSFCQECIsqvGKGGGSVCPVCRQRFLLKNLRPNRQLANMVN 70
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
 39-96 6.31e-07

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: 47.08  E-value: 6.31e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123772412  39 LERALSCSRCAGVLREPVSLGgCEHVFCLSCMGDHVGKG-------CPVCHVPAWVQDMQINRQL 96
Cdd:cd16598     1 LEEEVTCSICLDYLRDPVTID-CGHNFCRSCITDYCPISggherpvCPLCRKPFKKENIRPNWQL 64
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 425-523 7.28e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 425 YKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQN-DSPLHDAAKN 503
Cdd:PHA02875   33 YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATIL 112

                          90       100
                  ....*....|....*....|
gi 2123772412 504 GHVSIVELLLLHGASRDAVN 523
Cdd:PHA02875  113 KKLDIMKLLIARGADPDIPN 132
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 460-489 8.76e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.74  E-value: 8.76e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2123772412 460 GWTPLHEACNH-GHQEVVELLLQHKALVNST 489
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 429-533 1.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.89  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 429 TLLHIASIKGDLaaVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHVSI 508
Cdd:PHA02874   95 SILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI 172

                          90       100
                  ....*....|....*....|....*
gi 2123772412 509 VELLLLHGASRDAVNIFGLRPVDYA 533
Cdd:PHA02874  173 IKLLLEKGAYANVKDNNGESPLHNA 197
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 666-774 1.03e-06

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


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 46.97  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 666 LPKLFDGCYFYfLGSFNSHQKSDLVELVKAGGGQIlvrqpkpdsdvtqtintvayhaesTSDQRFCTQYVIYDASSKFKP 745
Cdd:pfam16589   1 LPNLFEPLRFY-INAIPSPSRSKLKRLIEANGGTV------------------------VDNINPAVYIVIAPYNKTDKL 55

                          90       100
                  ....*....|....*....|....*....
gi 2123772412 746 EKIRqgKVWFAPSSWIVDCIMSFQLLPVK 774
Cdd:pfam16589  56 AENT--KLGVVSPQWIFDCVKKGKLLPLE 82
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
 38-81 1.24e-06

RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) by binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438270 [Multi-domain]  Cd Length: 52  Bit Score: 45.95  E-value: 1.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2123772412  38 RLERALSCSRCAGVLREPVSLgGCEHVFCLSCMGDHVGKG----CPVC 81
Cdd:cd16608     2 SLKDELLCSICLSIYQDPVSL-GCEHYFCRQCITEHWSRSehrdCPEC 48
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 413-526 1.34e-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: 51.94  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 413 KSPGSNPIARRNYkGETLLHIASIKGDLAAVEELLKngADPNVKDNA-------GWTPLHEACNHGHQEVVELLLQHKAL 485
Cdd:cd22192    38 KCPSCDLFQRGAL-GETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALHIAVVNQNLNLVRELIARGAD 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2123772412 486 VNS---TG-----------YQNDSPLHDAAKNGHVSIVELLLLHGASRDAVNIFG 526
Cdd:cd22192   115 VVSpraTGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 429-517 1.62e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 429 TLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQND-SPLHDAAKNGHVS 507
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKID 216

                          90
                  ....*....|
gi 2123772412 508 IVELLLLHGA 517
Cdd:PHA02875  217 IVRLFIKRGA 226
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 429-521 2.21e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 429 TLLHIASIKGD-LAAVEELLKNGADPNVKDNAGWTPLHEAC-NHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAknGHV 506
Cdd:PHA02876  410 TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYH 487

                          90
                  ....*....|....*.
gi 2123772412 507 SIVELLLLHGAS-RDA 521
Cdd:PHA02876  488 GIVNILLHYGAElRDS 503
BRCT smart00292
breast cancer carboxy-terminal domain;
571-638 2.71e-06

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 45.83  E-value: 2.71e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2123772412  571 LGSGLSSKQQKLLNKLATVLKARRCTEFNS-TVTHVVVPDvPMPSTVKCMMAVLSGCWVLKFEWVQACL 638
Cdd:smart00292  11 ITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIVGS-PEGGKLELLKAIALGIPIVKEEWLLDCL 78
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 576-640 2.95e-06

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


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 45.66  E-value: 2.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123772412 576 SSKQQKLLNKLATVLKARRCTEFNSTVTHVVVPDvpmPS-TVKCMMAVLSGCWVLKFEWVQACLQS 640
Cdd:cd17736    10 SEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGS---PRrTLNVLLGIARGCWILSPDWVLESLEA 72
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 418-498 3.47e-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: 50.40  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 418 NPIARRNYKGETLLHIASIKGDLAAVEELLKNGAD---PNV--------KDNA---GWTPLHEACNHGHQEVVELLLQHK 483
Cdd:cd22192    80 EPMTSDLYQGETALHIAVVNQNLNLVRELIARGADvvsPRAtgtffrpgPKNLiyyGEHPLSFAACVGNEEIVRLLIEHG 159

                          90
                  ....*....|....*
gi 2123772412 484 ALVNSTGYQNDSPLH 498
Cdd:cd22192   160 ADIRAQDSLGNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 460-487 3.56e-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: 44.12  E-value: 3.56e-06
                           10        20
                   ....*....|....*....|....*...
gi 2123772412  460 GWTPLHEACNHGHQEVVELLLQHKALVN 487
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 438-542 3.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 3.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 438 GDLAAVEELLKNGAD-PNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHVSIVELLLLHG 516
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                          90       100
                  ....*....|....*....|....*.
gi 2123772412 517 ASRDAVnifglrPVDYAESEKMKSVL 542
Cdd:PHA02874   92 VDTSIL------PIPCIEKDMIKTIL 111
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 416-530 4.10e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 4.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 416 GSNpIARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEA-CNHGHQEVVELLLQHKALVNSTGYQND 494
Cdd:PHA02876  365 GAN-VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLS 443

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2123772412 495 SPLHDAAKNG-HVSIVELLLLHGASRDAVNIFGLRPV 530
Cdd:PHA02876  444 TPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 426-458 5.98e-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: 43.43  E-value: 5.98e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2123772412 426 KGETLLHIASIK-GDLAAVEELLKNGADPNVKDN 458
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
446-498 6.20e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 6.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2123772412 446 LLKNG-ADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLH 498
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
417-457 6.60e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 6.60e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2123772412 417 SNPIARRNYKGETLLHIASIKGDLAAVEELLKNGADPNVKD 457
Cdd:pfam12796  51 EHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 573-640 1.28e-05

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


Pssm-ID: 349370 [Multi-domain]  Cd Length: 75  Bit Score: 43.71  E-value: 1.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123772412 573 SGLSSKQQKLLNKLATVLKARRCT--EFNSTVTHVVVPDvpmPS-TVKCMMAVLSGCWVLKFEWVQACLQS 640
Cdd:cd17738     7 SGFSEDEKKELISIIEKLGGKVLDsdEFDPKCTHLICGK---PSrSEKFLAACAAGKWILHPSYIEASAKA 74
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 434-522 1.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 434 ASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHVSIVELLL 513
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88


                  ....*....
gi 2123772412 514 LHGASRDAV 522
Cdd:PHA02875   89 DLGKFADDV 97
Ank_4 pfam13637
Ankyrin repeats (many copies);
493-533 1.62e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2123772412 493 NDSPLHDAAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYA 533
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
 40-85 1.65e-05

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: 42.74  E-value: 1.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2123772412  40 ERALSCSRCAGVLREPVSLGgCEHVFCLSCMGDH------VGKGCPVCHVPA 85
Cdd:cd16609     1 EEELTCSICLGLYQDPVTLP-CQHSFCRACIEDHwrqkdeGSFSCPECRAPF 51
RING-HC_PCGF cd16525
RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and ...
 43-82 2.06e-05

RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and 6), and similar proteins; This subfamily includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which is involved in the maintenance of gene repression and which target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger.


Pssm-ID: 438188 [Multi-domain]  Cd Length: 42  Bit Score: 42.21  E-value: 2.06e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2123772412  43 LSCSRCAGVLREPVSLGGCEHVFCLSCMGDHV--GKGCPVCH 82
Cdd:cd16525     1 LTCSLCKGYLIDATTITECLHSFCKSCIVRHLetSKNCPVCD 42
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
 35-117 2.36e-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: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412  35 ALERLERALSCSRCAGVLREPVSLgGCEHVFCLSCMGDHVGKG-----CPVCHVPAWVQDMQINRQLDDMVQlcgKLRHL 109
Cdd:cd16498     9 VISAMQKNLECPICLELLKEPVST-KCDHQFCRFCILKLLQKKkkpapCPLCKKSVTKRSLQESTRFKQLVE---AVKKL 84


                  ....*...
gi 2123772412 110 LDAGTSDS 117
Cdd:cd16498    85 IDAFELDT 92
PHA03095 PHA03095
ankyrin-like protein; Provisional
 421-545 2.44e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 421 ARRNYKGE---TLLHI----ASIKGDLaaVEELLKNGADPNVKDNAGWTPLH-----EACNhghQEVVELLLQHKALVNS 488
Cdd:PHA03095  108 ADVNAKDKvgrTPLHVylsgFNINPKV--IRLLLRKGADVNALDLYGMTPLAvllksRNAN---VELLRLLIDAGADVYA 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 489 TGYQNDSPLHDAAKNGHVS--IVELLLLHGASRDAVNIFGLRPVDY-AESEKMKSVLMLP 545
Cdd:PHA03095  183 VDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSmATGSSCKRSLVLP 242
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 452-544 3.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 452 DPNVKDNAgwTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAKNGHVS-----IVELLLLHGASRDAVNIFG 526
Cdd:PHA03100   29 DYSYKKPV--LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNG 106

                          90
                  ....*....|....*...
gi 2123772412 527 LRPVDYAESEKMKSVLML 544
Cdd:PHA03100  107 ITPLLYAISKKSNSYSIV 124
PHA03095 PHA03095
ankyrin-like protein; Provisional
 416-533 5.09e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 416 GSNPIARRNYkGETLLHI--ASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACN--HGHQEVVELLLQHKALVNSTGY 491
Cdd:PHA03095  142 GADVNALDLY-GMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDM 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2123772412 492 QNDSPLHDAAKNGHV--SIVELLLLHGASRDAVNIFGLRPVDYA 533
Cdd:PHA03095  221 LGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYA 264
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 429-533 5.12e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 429 TLLHIASIKGDLAA-VEELLKNGADPNVKDNAGWTPLHEACNHGHQ-EVVELLLQHKALVNSTGYQNDSPLHDAAK-NGH 505
Cdd:PHA02876  275 TPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTlDRN 354

                          90       100
                  ....*....|....*....|....*...
gi 2123772412 506 VSIVELLLLHGASRDAVNIFGLRPVDYA 533
Cdd:PHA02876  355 KDIVITLLELGANVNARDYCDKTPIHYA 382
RING-HC_AtBARD1-like cd23146
RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 ...
 39-91 5.66e-05

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: 41.30  E-value: 5.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2123772412  39 LERALSCSRCAGVLREPVSLGgCEHVFCLSCMGD--HVGKGCPVCHVPAWVQDMQ 91
Cdd:cd23146     1 MELELKCPICLKLLNRPVLLP-CDHIFCSSCITDstKVGSDCPVCKLPYHSQDLR 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 426-455 6.00e-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: 40.70  E-value: 6.00e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2123772412 426 KGETLLHIASIKGDLAAVEELLKNGADPNV 455
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 494-523 6.89e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 6.89e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2123772412 494 DSPLHDAA-KNGHVSIVELLLLHGASRDAVN 523
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02946 PHA02946
ankyin-like protein; Provisional
 436-517 7.38e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 436 IKG-DLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLH--DAAKNGHVSIVELL 512
Cdd:PHA02946   47 IKGlDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLL 126


                  ....*
gi 2123772412 513 LLHGA 517
Cdd:PHA02946  127 VQYGA 131
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 43-81 9.73e-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: 40.16  E-value: 9.73e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2123772412  43 LSCSRCAGVLREPVSLGgCEHVFCLSCMGDHVGKG---CPVC 81
Cdd:cd16449     1 LECPICLERLKDPVLLP-CGHVFCRECIRRLLESGsikCPIC 41
RING-HC_AtBRCA1-like cd23147
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 ...
 39-91 1.33e-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: 40.14  E-value: 1.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2123772412  39 LERALSCSRCAGVLREPVSLGgCEHVFCLSCMGDHV--GKGCPVCHVPAWVQDMQ 91
Cdd:cd23147     1 LGKELKCPICLSLFKSAANLS-CNHCFCAGCIGESLklSAICPVCKIPATRRDTR 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 416-502 1.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 416 GSNPIARRNYkGETLLHIASIK-GDLAAVEELLKNGADPNVKDNA-GWTPLHEACNHghQEVVELLLQHKALVNSTGYQN 493
Cdd:PHA02878  224 GASTDARDKC-GNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKS--ERKLKLLLEYGADINSLNSYK 300


                  ....*....
gi 2123772412 494 DSPLHDAAK 502
Cdd:PHA02878  301 LTPLSSAVK 309
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 417-494 1.73e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 1.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123772412 417 SNPiarrnYKGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQND 494
Cdd:PLN03192  617 SDP-----HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 428-544 2.17e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 428 ETLLHIASIK-----GDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQHKALVNSTGYQNDSPLHDAAK 502
Cdd:PHA02876  141 ESIEYMKLIKeriqqDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2123772412 503 NGHVSIVELLLlhgASRDAVNIFGLRPVDYAESEKMKSVLML 544
Cdd:PHA02876  221 SKNIDTIKAII---DNRSNINKNDLSLLKAIRNEDLETSLLL 259
RING-HC_RNF39 cd16592
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ...
 39-84 2.59e-04

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


Pssm-ID: 438254 [Multi-domain]  Cd Length: 58  Bit Score: 39.74  E-value: 2.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2123772412  39 LERALSCSRCAGVLREPVSLGgCEHVFCLSCMGDHVGKG-----------CPVCHVP 84
Cdd:cd16592     1 LQEETTCPICLGYFKDPVILD-CEHSFCRACIARHWGQEamegngaegvfCPQCGEP 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 426-455 3.18e-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: 38.34  E-value: 3.18e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2123772412  426 KGETLLHIASIKGDLAAVEELLKNGADPNV 455
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 492-518 3.31e-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: 38.34  E-value: 3.31e-04
                           10        20
                   ....*....|....*....|....*..
gi 2123772412  492 QNDSPLHDAAKNGHVSIVELLLLHGAS 518
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 422-518 4.09e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.92  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 422 RRNYKGETLLHIASiKGDLAAVEELL--------KNGADPNVKDNA------GWTPLHEACNHGHQEVVELLLQHKALVN 487
Cdd:TIGR00870  77 CRGAVGDTLLHAIS-LEYVDAVEAILlhllaafrKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVP 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2123772412 488 ---------STGYQN-----DSPLHDAAKNGHVSIVELLLLHGAS 518
Cdd:TIGR00870 156 aracgdffvKSQGVDsfyhgESPLNAAACLGSPSIVALLSEDPAD 200
RING-HC_RNF166 cd16549
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; ...
 42-84 6.13e-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: 38.25  E-value: 6.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2123772412  42 ALSCSRCAGVLREPVSLGGCEHVFCLSCMGDHV---GKGCPVCHVP 84
Cdd:cd16549     1 QFSCPICLEVYHKPVVITSCGHTFCGECLQPCLqvaSPLCPLCRMP 46
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
 45-84 6.78e-04

RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also known as probable E3 NEDD8-protein ligase or RING finger protein 35 (RNF35), is highly expressed in the gastrointestinal tract including the stomach, small intestine, and large intestine. It enhances neddylation of inhibitor of nuclear factor kappaB kinase subunit gamma (IKKgamma), inhibits the activity of nuclear factor-kappaB (NF-kappaB)-mediated transcription, and thus prevents inflammation-associated carcinogenesis in the gastrointestinal tract. TRIM40 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438245 [Multi-domain]  Cd Length: 63  Bit Score: 38.66  E-value: 6.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2123772412  45 CSRCAGVLREPVSLGgCEHVFCLSCMGDHVGKG-------CPVCHVP 84
Cdd:cd16583     8 CPICQEPLKEAVSTD-CGHLFCRMCLTQHAKKAsasgvfsCPVCRKP 53
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
43-116 7.16e-04

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 42.81  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412  43 LSCSRCAGVLREPVSLGGCEHVFCLSCMGDHV---GKGCPVCH-----VPAWVQDMQINRQLDDMVQLCGKLrhlldAGT 114
Cdd:COG5222   275 LKCPLCHCLLRNPMKTPCCGHTFCDECIGTALldsDFKCPNCSrkdvlLDGLTPDIDKKLEVEKALKKQRKK-----VGT 349


                  ..
gi 2123772412 115 SD 116
Cdd:COG5222   350 SD 351
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 390-518 7.50e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.15  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 390 SPSTPSTFKACDQVGIPQSPSVFKsPGSNP----IARRNYKGETLLHIASIKGDLAAVEELLKN-GADPNVKDNAgwtpL 464
Cdd:TIGR00870  12 SPLSDEEKAFLPAAERGDLASVYR-DLEEPkklnINCPDRLGRSALFVAAIENENLELTELLLNlSCRGAVGDTL----L 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123772412 465 HEACNhGHQEVVELLLQHKA----------LVN----STGYQNDSPLHDAAKNGHVSIVELLLLHGAS 518
Cdd:TIGR00870  87 HAISL-EYVDAVEAILLHLLaafrksgpleLANdqytSEFTPGITALHLAAHRQNYEIVKLLLERGAS 153
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
 43-94 8.05e-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: 38.12  E-value: 8.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2123772412  43 LSCSRCAGVLREPVSLGGCEHVFCLSCMGDHVGKG---CPVCHVPawVQDMQINR 94
Cdd:cd16503     3 LTCSICQDLLHDCVSLQPCMHNFCAACYSDWMERSnteCPTCRAT--VQRVNKNH 55
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 460-487 8.85e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 8.85e-04
                          10        20
                  ....*....|....*....|....*...
gi 2123772412 460 GWTPLHEACNHGHQEVVELLLQHKALVN 487
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
 43-85 1.17e-03

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: 37.38  E-value: 1.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2123772412  43 LSCSRCAGVLREPVSLGGCEHVFCLSCMGDHVGKG---CPVCHVPA 85
Cdd:cd16544     3 LTCPVCQEVLKDPVELPPCRHIFCKACILLALRSSgarCPLCRGPV 48
PHA03095 PHA03095
ankyrin-like protein; Provisional
 408-513 1.27e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 408 SPSVFKS---PGSNPIARrNYKGETLLHIASIKGDLAA--VEELLKNGADPNVKDNAGWTPLHEACNHGHQEVVELLLQH 482
Cdd:PHA03095  201 RARIVRElirAGCDPAAT-DMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL 279

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2123772412 483 KALVNSTGYQNDSPLHDAAKNGHVSIVELLL 513
Cdd:PHA03095  280 GADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
RING-HC_TRIM72_C-IV cd16612
RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar ...
 43-93 1.39e-03

RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar proteins; TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of the peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis by targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 belongs to the C-IV subclass of 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: 438274 [Multi-domain]  Cd Length: 60  Bit Score: 37.41  E-value: 1.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2123772412  43 LSCSRCAGVLREPVSlGGCEHVFCLSCMG------DHVGKGCPVCHVPAWVQDMQIN 93
Cdd:cd16612     5 LSCPLCLKLFQSPVT-TECGHTFCQDCLSrvpkeeDGGSTSCPTCQAPTKPEQLSIN 60
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
 38-94 1.63e-03

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: 37.28  E-value: 1.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2123772412  38 RLERALSCSRCAGVLREPVSLgGCEHVFCLSCMGDHVGKG-----CPVCHVPAWVQDMQINR 94
Cdd:cd16594     1 SLQEELTCPICLDYFTDPVTL-DCGHSFCRACIARCWEEPetsasCPQCRETCPQRNLRPNR 61
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
 43-81 1.69e-03

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: 36.69  E-value: 1.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2123772412  43 LSCSRCAGVLREPVSLGgCEHVFCLSCM--------GDHVgkgCPVC 81
Cdd:cd16601     2 ASCSLCKEYLKDPVIIE-CGHNFCRACItrfweeldGDFP---CPQC 44
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
 43-84 1.85e-03

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: 37.00  E-value: 1.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2123772412  43 LSCSRCAGVLREPVSLGGCEHVFCLSCMGDHVGKG---CPVCHVP 84
Cdd:cd16620     4 LKCPICKDLMKDAVLTPCCGNSFCDECIRTALLEEdftCPTCKEP 48
RING-HC_TRIM47-like_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
 43-85 1.92e-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: 37.02  E-value: 1.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2123772412  43 LSCSRCAGVLREPVSLGgCEHVFCLSCMGDHVGKG------CPVCHVPA 85
Cdd:cd16604     1 LSCPICLDLLKDPVTLP-CGHSFCMGCLGALWGAGrggrasCPLCRQTF 48
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 573-638 2.05e-03

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


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 37.66  E-value: 2.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123772412 573 SGLSSKQQKLLNKLATVLKARRCTEFNSTVTHVVVPdvpmPSTVKCMMAVLSGCWVLKFEWVQACL 638
Cdd:pfam00533  14 TGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVE----ARTKKYLKAKELGIPIVTEEWLLDCI 75
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
 39-81 2.35e-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: 37.29  E-value: 2.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2123772412  39 LERALSCSRCAGVLREPVSLgGCEHVFCLSCMG---DHVGKG---CPVC 81
Cdd:cd16597     2 LEEELTCSICLELFKDPVTL-PCGHNFCGVCIEktwDSQHGSeysCPQC 49
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 425-493 2.41e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.40  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123772412 425 YKGETLLHIASIKGDLAAVEELLKNGADPNVKDNA-------------GWTPLHEACNHGHQEVVELLLQHKALVNSTGY 491
Cdd:cd21882    71 YQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEA 150


                  ..
gi 2123772412 492 QN 493
Cdd:cd21882   151 QD 152
RING-HC_PCGF5 cd16737
RING finger found in polycomb group RING finger protein 5 (PCGF5) and similar proteins; PCGF5, ...
 36-81 2.51e-03

RING finger found in polycomb group RING finger protein 5 (PCGF5) and similar proteins; PCGF5, also known as RING finger protein 159 (RNF159), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) and serves as the core component of a Polycomb repressive complex 1 (PRC1). Like other PCGF homologs, PCGF5 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. PCGF5 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438395 [Multi-domain]  Cd Length: 95  Bit Score: 37.81  E-value: 2.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2123772412  36 LERLERALSCSRCAGVLREPVSLGGCEHVFCLSCMGDHV--GKGCPVC 81
Cdd:cd16737     4 VRDFNPYITCRICKGYLIKPTTVTECLHTFCKSCIVQHFedSNDCPEC 51
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 475-550 2.85e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 2.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123772412 475 VVELLLQHKALVNSTGYQNDSPLHDAAKNGHVSIVELLLLHGASRDAVNIFGLRPVDYAESEKMKSVLMLPVKNES 550
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
mRING-HC-C3HC3D_Nrdp1 cd16634
Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation ...
 43-70 2.94e-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: 36.25  E-value: 2.94e-03
                          10        20
                  ....*....|....*....|....*...
gi 2123772412  43 LSCSRCAGVLREPVSLGGCEHVFCLSCM 70
Cdd:cd16634     2 LICPICSGVLEEPLQAPHCEHAFCNACI 29
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 577-637 3.03e-03

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


Pssm-ID: 349359 [Multi-domain]  Cd Length: 75  Bit Score: 37.19  E-value: 3.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123772412 577 SKQQKLLNKLATVLKARRCTEFNSTVTHVVVPDVPMPSTVKCMMAVLSGCWVLKFEWVQAC 637
Cdd:cd17727    13 SKRQGELNKIAASLGAEYRWTYDESCTHFIYQGKANDTNREYKSAKEQGKFIVSPHWLYAC 73
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
 44-101 3.04e-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: 37.04  E-value: 3.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123772412  44 SCSRCAGVLREPVSLGgCEHVFCLSCMGDHVGK--------GCPVCHVPAWVQDMQINRQLDDMVQ 101
Cdd:cd16591     8 TCPICLELLTEPLSLD-CGHSFCQACITANHKEsvnqegesSCPVCRTSYQPENLRPNRHLANIVE 72
RING-HC_TRIM10_C-IV cd16593
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ...
 45-86 3.59e-03

RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins; TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438255 [Multi-domain]  Cd Length: 61  Bit Score: 36.42  E-value: 3.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2123772412  45 CSRCAGVLREPVSLgGCEHVFCLSC---------MGDHVGKGCPVCHVPAW 86
Cdd:cd16593     8 CPICQGTLREPVTI-DCGHNFCRACltryceipgPDLEEPPTCPLCKEPFR 57
RING-HC_RFPL4B cd16623
RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; ...
 38-81 4.07e-03

RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; RFPL4B, also called RING finger protein 211 (RNF211), is an uncharacterized RING finger protein containing a typical C3HC4-type RING-HC finger.


Pssm-ID: 438285 [Multi-domain]  Cd Length: 63  Bit Score: 36.33  E-value: 4.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2123772412  38 RLERALSCSRCAGVLREPVSLGgCEHVFCLSCMGDHVGKG------CPVC 81
Cdd:cd16623     4 RLEMEATCPICLDFFSHPISLS-CAHIFCFDCIQKWMTKRedsiltCPLC 52
RING-HC_RING1-like cd16531
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and ...
 43-84 4.25e-03

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: 36.48  E-value: 4.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2123772412  43 LSCSRCAGVLREPVSLGGCEHVFCLSCMGDHV---GKGCPVCHVP 84
Cdd:cd16531     2 LMCPICLGIIKNTMTVKECLHRFCAECIEKALrlgNKECPTCRKH 46
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
 45-81 5.40e-03

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: 35.41  E-value: 5.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2123772412  45 CSRCAGVLREPVSLGGCEHVFCLSC---MGDHVGKGCPVC 81
Cdd:pfam00097   1 CPICLEEPKDPVTLLPCGHLFCSKCirsWLESGNVTCPLC 40
RING-HC_PCGF2 cd16734
RING finger found in polycomb group RING finger protein 2 (PCGF2) and similar proteins; PCGF2, ...
 32-100 5.75e-03

RING finger found in polycomb group RING finger protein 2 (PCGF2) and similar proteins; PCGF2, also known as DNA-binding protein Mel-18, RING finger protein 110 (RNF110), or zinc finger protein 144 (ZNF144), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a canonical Polycomb repressive complex 1 (PRC1), which is composed of a chromodomain-containing protein (CBX2, CBX4, CBX6, CBX7 or CBX8) and a Polyhomeotic protein (PHC1, PHC2, or PHC3). Like other PCGF homologs, PCGF2 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF2 uniquely regulates PRC1 to specify mesoderm cell fate in embryonic stem cells. It is required for PRC1 stability and maintenance of gene repression in embryonic stem cells (ESCs) and essential for ESC differentiation into early cardiac-mesoderm precursors. PCGF2 also plays a significant role in the angiogenic function of endothelial cells (ECs) by regulating endothelial gene expression. Furthermore, PCGF2 is a SUMO-dependent regulator of hormone receptors. It facilitates the deSUMOylation process by inhibiting PCGF4/BMI1-mediated ubiquitin-proteasomal degradation of SUMO1/sentrin-specific protease 1 (SENP1). It is also a novel negative regulator of breast cancer stem cells (CSCs) that inhibits the stem cell population and in vitro and in vivo self-renewal through the inactivation of Wnt-mediated Notch signaling. PCGF2 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438392 [Multi-domain]  Cd Length: 80  Bit Score: 36.50  E-value: 5.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123772412  32 TRAALERLERALSCSRCAGVLREPVSLGGCEHVFCLSCMGDHV--GKGCPVC----HVPAWVQDMQINRQLDDMV 100
Cdd:cd16734     4 TRIKITELNPHLMCALCGGYFIDAATIVECLHSFCKTCIVRYLetNKYCPMCdvqvHKTRPLLSIRSDKTLQDIV 78
RING-HC_PCGF1 cd16733
RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar ...
 39-101 7.06e-03

RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar proteins; PCGF1, also known as nervous system Polycomb-1 (NSPc1) or RING finger protein 68 (RNF68), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like BCOR complex that also contains RING1, RNF2, RYBP, SKP1, as well as the BCL6 co-repressor BCOR and the histone demethylase KDM2B, and is required to maintain the transcriptionally repressive state of some genes, such as Hox genes, BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. PCGF1 promotes cell cycle progression and enhances cell proliferation as well. It is a cell growth regulator that acts as a transcriptional repressor of p21Waf1/Cip1 via the retinoid acid response element (RARE element). Moreover, PCGF1 functions as an epigenetic regulator involved in hematopoietic cell differentiation. It cooperates with the transcription factor runt-related transcription factor 1 (Runx1) in regulating differentiation and self-renewal of hematopoietic cells. Furthermore, PCGF1 represents a physical and functional link between Polycomb function and pluripotency. PCGF1 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438391 [Multi-domain]  Cd Length: 71  Bit Score: 36.09  E-value: 7.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123772412  39 LERALSCSRCAGVLREPVSLGGCEHVFCLSCMGDHV--GKGCPVCHVPAWVQDMQINRQLDDMVQ 101
Cdd:cd16733     6 LNEHIVCYLCAGYFIDATTITECLHTFCKSCIVKYLqtSKYCPMCNIKIHETQPLLNLKLDRVMQ 70
PHA02917 PHA02917
ankyrin-like protein; Provisional
 426-483 8.68e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.60  E-value: 8.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2123772412 426 KGETLLHIASIKGDLAAVEELLKNGADPNVKDNAGWTPLHEACNHGHQ-EVVELLLQHK 483
Cdd:PHA02917  451 RGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNiELLKMLLCHK 509
RING-HC_LONFs_rpt2 cd16514
second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
 43-81 8.76e-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: 34.93  E-value: 8.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2123772412  43 LSCSRCAGVLREPVSLGgCEHVFCLSCMG---DHvGKGCPVC 81
Cdd:cd16514     2 LECSLCLRLLYEPVTTP-CGHTFCRACLErclDH-SPKCPLC 41
RING-HC_RNF219 cd16562
RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; ...
 43-84 9.03e-03

RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; RNF219 may function as a modulator of late-onset Alzheimer's disease (LOAD) associated amyloid beta A4 precursor protein (APP) endocytosis and metabolism. It genetically interacts with apolipoprotein E epsilon4 allele (APOE4). Thus, a genetic variant of RNF219 was found to affect amyloid deposition in human brain and LOAD age-of-onset. Moreover, common genetic variants at the RNF219 locus had been associated with alternations in lipid metabolism, cognitive performance and central nervous system ventricle volume. RNF219 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438224 [Multi-domain]  Cd Length: 45  Bit Score: 34.72  E-value: 9.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2123772412  43 LSCSRCAGVLREPVSlggC--EHVFCLSCMGD--HVGKGCPVCHVP 84
Cdd:cd16562     2 ISCHICLGKVRQPVI---CsnNHVFCSSCMDVwlKNNNQCPACRVP 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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