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Conserved domains on  [gi|1958803882|ref|XP_038940104|]
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BRCA1-associated RING domain protein 1 isoform X5 [Rattus norvegicus]

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 ...
 497-597 7.19e-39

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: 138.27  E-value: 7.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 497 LFDGCYFFLGGNFKHH-PKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYhAKPDSDQRFCTQYIVYEDLFNCHPER 575
Cdd:cd17720     1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 1958803882 576 VRQGKVWMAPSTWLISCVMAFE 597
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 396-472 7.45e-29

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: 109.61  E-value: 7.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 396 LVLIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVPDEE---AQSTLKCMLGILNGCWVLKFDWVKACLDSQERE 472
Cdd:cd17734     1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-370 2.76e-21

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.64  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 267 LSSGIPARKRNHRGETLLHIAsikheaCSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRN 346
Cdd:COG0666   140 LEAGADVNAQDNDGNTPLHLA------AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          90       100
                  ....*....|....*....|....
gi 1958803882 347 AVNIFGERPVDYTDAENIRSLLLL 370
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKL 237
 
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 ...
 497-597 7.19e-39

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: 138.27  E-value: 7.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 497 LFDGCYFFLGGNFKHH-PKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYhAKPDSDQRFCTQYIVYEDLFNCHPER 575
Cdd:cd17720     1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 1958803882 576 VRQGKVWMAPSTWLISCVMAFE 597
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 396-472 7.45e-29

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: 109.61  E-value: 7.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 396 LVLIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVPDEE---AQSTLKCMLGILNGCWVLKFDWVKACLDSQERE 472
Cdd:cd17734     1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-370 2.76e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.64  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 267 LSSGIPARKRNHRGETLLHIAsikheaCSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRN 346
Cdd:COG0666   140 LEAGADVNAQDNDGNTPLHLA------AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          90       100
                  ....*....|....*....|....
gi 1958803882 347 AVNIFGERPVDYTDAENIRSLLLL 370
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
262-349 6.12e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 262 PSTVK--LSSGIPARKRNHRGETLLHIAsikheaCSHGHLKIVELLLQHNALVNTTgyHNDSPLHDAAKNGHIDIVKVLL 339
Cdd:pfam12796  10 LELVKllLENGADANLQDKNGRTALHLA------AKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1958803882 340 SHGASRNAVN 349
Cdd:pfam12796  82 EKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 259-369 5.37e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 5.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 259 MSKPSTVK--LSSGIPARKRNHRGETLLHIASIkheaCSHGHLKIVELLLQHNALVN---------TTGYHND------- 320
Cdd:PHA03100  118 SNSYSIVEylLDNGANVNIKNSDGENLLHLYLE----SNKIDLKILKLLIDKGVDINaknrvnyllSYGVPINikdvygf 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958803882 321 SPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDY---TDAENIRSLLL 369
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIailNNNKEIFKLLL 245
BRCT smart00292
breast cancer carboxy-terminal domain;
407-466 3.51e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 48.14  E-value: 3.51e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958803882  407 QQKLLSKLETVLKAKKCAEFDN----TVTHVIVPDEEaQSTLKCMLGILNGCWVLKFDWVKACL 466
Cdd:smart00292  16 DKEERDELKELIEALGGKVTSSlsskTTTHVIVGSPE-GGKLELLKAIALGIPIVKEEWLLDCL 78
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 318-347 1.52e-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: 44.89  E-value: 1.52e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958803882  318 HNDSPLHDAAKNGHIDIVKVLLSHGASRNA 347
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
BRCT smart00292
breast cancer carboxy-terminal domain;
495-593 3.54e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 42.36  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882  495 PKLFDGCYFFLGGNFKHHPKEDLLKLIAAAGGRILSRKPKPDsdvtqtintvayhakpdsdqrfcTQYIVYEDLFN--CH 572
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVGSPEGgkLE 57

                           90       100
                   ....*....|....*....|.
gi 1958803882  573 PERVRQGKVWMAPSTWLISCV 593
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 280-356 2.20e-04

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: 44.23  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 280 GETLLHIASIKheacshGHLKIVELLLQHNALVNT---TG-----------YHNDSPLHDAAKNGHIDIVKVLLSHGASR 345
Cdd:cd22192    89 GETALHIAVVN------QNLNLVRELIARGADVVSpraTGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADI 162

                          90
                  ....*....|.
gi 1958803882 346 NAVNIFGERPV 356
Cdd:cd22192   163 RAQDSLGNTVL 173
PHA02946 PHA02946
ankyin-like protein; Provisional
 300-448 6.57e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.27  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 300 KIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDY---TDAENIRSLLLLPEKTDS 376
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsgTDDEVIERINLLVQYGAK 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958803882 377 FSTSqcsvqvnTGQRKSGPLVligsGLSSQQQKLLSKLETV-LKAKKCAEF-DNTVTHVIVPDEEAQSTLKCML 448
Cdd:PHA02946  133 INNS-------VDEEGCGPLL----ACTDPSERVFKKIMSIgFEARIVDKFgKNHIHRHLMSDNPKASTISWMM 195
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 494-581 7.78e-03

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: 35.80  E-value: 7.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 494 LPKLFDGCYFFLGGnFKHHPKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYHAKPDSDQRFCTQYIvyedlFNChp 573
Cdd:pfam16589   1 LPNLFEPLRFYINA-IPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWI-----FDC-- 72


                  ....*...
gi 1958803882 574 erVRQGKV 581
Cdd:pfam16589  73 --VKKGKL 78
 
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 ...
 497-597 7.19e-39

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: 138.27  E-value: 7.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 497 LFDGCYFFLGGNFKHH-PKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYhAKPDSDQRFCTQYIVYEDLFNCHPER 575
Cdd:cd17720     1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 1958803882 576 VRQGKVWMAPSTWLISCVMAFE 597
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 396-472 7.45e-29

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: 109.61  E-value: 7.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 396 LVLIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVPDEE---AQSTLKCMLGILNGCWVLKFDWVKACLDSQERE 472
Cdd:cd17734     1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-370 2.76e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.64  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 267 LSSGIPARKRNHRGETLLHIAsikheaCSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRN 346
Cdd:COG0666   140 LEAGADVNAQDNDGNTPLHLA------AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          90       100
                  ....*....|....*....|....
gi 1958803882 347 AVNIFGERPVDYTDAENIRSLLLL 370
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-368 6.63e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 6.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 267 LSSGIPARKRNHRGETLLHIAsikheaCSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRN 346
Cdd:COG0666   107 LEAGADVNARDKDGETPLHLA------AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                          90       100
                  ....*....|....*....|....*.
gi 1958803882 347 AVNIFGERP----VDYTDAENIRSLL 368
Cdd:COG0666   181 ARDNDGETPlhlaAENGHLEIVKLLL 206
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-368 1.91e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.00  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 267 LSSGIPARKRNHRGETLLHIAsikheaCSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRN 346
Cdd:COG0666    74 LAAGADINAKDDGGNTLLHAA------ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147

                          90       100
                  ....*....|....*....|....*.
gi 1958803882 347 AVNIFGERP----VDYTDAENIRSLL 368
Cdd:COG0666   148 AQDNDGNTPlhlaAANGNLEIVKLLL 173
Ank_2 pfam12796
Ankyrin repeats (3 copies);
262-349 6.12e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 262 PSTVK--LSSGIPARKRNHRGETLLHIAsikheaCSHGHLKIVELLLQHNALVNTTgyHNDSPLHDAAKNGHIDIVKVLL 339
Cdd:pfam12796  10 LELVKllLENGADANLQDKNGRTALHLA------AKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1958803882 340 SHGASRNAVN 349
Cdd:pfam12796  82 EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
276-370 5.01e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.06  E-value: 5.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 276 RNHRGETLLHIAsikheaCSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERP 355
Cdd:COG0666   182 RDNDGETPLHLA------AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255

                          90
                  ....*....|....*
gi 1958803882 356 VDYTDAENIRSLLLL 370
Cdd:COG0666   256 LLLAAAAGAALIVKL 270
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 398-481 1.20e-11

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: 61.21  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 398 LIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIV-PDEE--AQSTLKCMLGILNGCWVLKFDWVKACLDSQEREQE 474
Cdd:cd17735     3 MVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMkTDAElvCERTLKYFLGIAGRKWVVSYQWITQSIKEGKILPE 82


                  ....*..
gi 1958803882 475 EKYEVPG 481
Cdd:cd17735    83 HDFEVRG 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
291-349 3.36e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 3.36e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958803882 291 HEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVN 349
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN 60
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 396-465 4.00e-11

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: 58.91  E-value: 4.00e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 396 LVLIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVPDEEaqSTLKCMLGILNGCWVLKFDWVKAC 465
Cdd:cd00027     1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPS--GEKYYLAALAWGIPIVSPEWLLDC 68
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 259-369 5.37e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 5.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 259 MSKPSTVK--LSSGIPARKRNHRGETLLHIASIkheaCSHGHLKIVELLLQHNALVN---------TTGYHND------- 320
Cdd:PHA03100  118 SNSYSIVEylLDNGANVNIKNSDGENLLHLYLE----SNKIDLKILKLLIDKGVDINaknrvnyllSYGVPINikdvygf 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958803882 321 SPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDY---TDAENIRSLLL 369
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIailNNNKEIFKLLL 245
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 404-473 6.98e-10

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: 55.67  E-value: 6.98e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 404 SSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVpdEEAQSTLKCMLGILNGCWVLKFDWVkacLDSQEREQ 473
Cdd:cd17736    10 SEEQELLESVVKKLGGFRVEDSVTEKTTHVVV--GSPRRTLNVLLGIARGCWILSPDWV---LESLEAGK 74
Ank_4 pfam13637
Ankyrin repeats (many copies);
291-339 3.34e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 3.34e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958803882 291 HEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLL 339
Cdd:pfam13637   6 HAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
305-358 6.76e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 6.76e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958803882 305 LLQH-NALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDY 358
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
271-355 1.36e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.50  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 271 IPARKRNHRGETLLHIASIKHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNI 350
Cdd:COG0666    39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118


                  ....*
gi 1958803882 351 FGERP 355
Cdd:COG0666   119 DGETP 123
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 267-368 2.34e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.51  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 267 LSSGIPARKRNHRGETLLHIAsIKHeacshGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRN 346
Cdd:PHA02874  111 LDCGIDVNIKDAELKTFLHYA-IKK-----GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100
                  ....*....|....*....|....*.
gi 1958803882 347 AVNIFGERP----VDYTDAENIRSLL 368
Cdd:PHA02874  185 VKDNNGESPlhnaAEYGDYACIKLLI 210
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 267-349 1.03e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 267 LSSGIPARKRNHRGETLLHiasikhEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRN 346
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLH------YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                  ...
gi 1958803882 347 AVN 349
Cdd:PHA03100  253 TII 255
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 275-359 2.97e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 275 KRNHRGETLLHIASikheacSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGER 354
Cdd:PHA02878  163 KDRHKGNTALHYAT------ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236


                  ....*
gi 1958803882 355 PVDYT 359
Cdd:PHA02878  237 PLHIS 241
BRCT smart00292
breast cancer carboxy-terminal domain;
407-466 3.51e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 48.14  E-value: 3.51e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958803882  407 QQKLLSKLETVLKAKKCAEFDN----TVTHVIVPDEEaQSTLKCMLGILNGCWVLKFDWVKACL 466
Cdd:smart00292  16 DKEERDELKELIEALGGKVTSSlsskTTTHVIVGSPE-GGKLELLKAIALGIPIVKEEWLLDCL 78
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 401-469 1.33e-06

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: 46.02  E-value: 1.33e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958803882 401 SGLSSQQQKLLSKLETVLKAKKC--AEFDNTVTHVIVpdEEAQSTLKCMLGILNGCWVLKFDWVKACLDSQ 469
Cdd:cd17738     7 SGFSEDEKKELISIIEKLGGKVLdsDEFDPKCTHLIC--GKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 265-341 1.35e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 1.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958803882 265 VKLSSGIPARKRNHRGETLLHIAsikheaCSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSH 341
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIA------CANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 318-347 1.52e-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: 44.89  E-value: 1.52e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958803882  318 HNDSPLHDAAKNGHIDIVKVLLSHGASRNA 347
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
319-358 2.62e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958803882 319 NDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDY 358
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 318-349 3.77e-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: 43.82  E-value: 3.77e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958803882 318 HNDSPLHDAA-KNGHIDIVKVLLSHGASRNAVN 349
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 261-358 4.74e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 261 KPSTVK--LSSGIPARKRNHRGETLLHIASIKHEACSHGhLKIVELLLQHNALVNTTGYHNDSPLHDAA--KNGHIDIVK 336
Cdd:PHA03100   47 NIDVVKilLDNGADINSSTKNNSTPLHYLSNIKYNLTDV-KEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVE 125

                          90       100
                  ....*....|....*....|..
gi 1958803882 337 VLLSHGASRNAVNIFGERPVDY 358
Cdd:PHA03100  126 YLLDNGANVNIKNSDGENLLHL 147
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 281-367 1.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 281 ETLLHIASIKhEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDYT- 359
Cdd:PHA02876  141 ESIEYMKLIK-ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAv 219


                  ....*...
gi 1958803882 360 DAENIRSL 367
Cdd:PHA02876  220 DSKNIDTI 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 279-313 2.00e-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. 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: 41.51  E-value: 2.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958803882 279 RGETLLHIAsikheACSHGHLKIVELLLQHNALVN 313
Cdd:pfam00023   1 DGNTPLHLA-----AGRRGNLEIVKLLLSKGADVN 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 302-414 2.67e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 302 VELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDYTDAENIRSL--LLLPEKTDSFST 379
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVvqLLSRHSQCHFEL 177

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958803882 380 SQCSV-QVNTGQRKS---GPLVLIGSGLSSQQQKLLSKL 414
Cdd:PTZ00322  178 GANAKpDSFTGKPPSledSPISSHHPDFSAVPQPMMGSL 216
BRCT smart00292
breast cancer carboxy-terminal domain;
495-593 3.54e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 42.36  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882  495 PKLFDGCYFFLGGNFKHHPKEDLLKLIAAAGGRILSRKPKPDsdvtqtintvayhakpdsdqrfcTQYIVYEDLFN--CH 572
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVGSPEGgkLE 57

                           90       100
                   ....*....|....*....|.
gi 1958803882  573 PERVRQGKVWMAPSTWLISCV 593
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-354 9.59e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.56  E-value: 9.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 267 LSSGIPARKRNHRGETLLHIAsikheaCSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRN 346
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLA------AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                  ....*...
gi 1958803882 347 AVNIFGER 354
Cdd:COG0666   280 AALLDLLT 287
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 291-347 1.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.49  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958803882 291 HEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKN-GHIDIVKVLLSHGASRNA 347
Cdd:PHA02878  206 HHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNA 263
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 280-356 2.20e-04

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: 44.23  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 280 GETLLHIASIKheacshGHLKIVELLLQHNALVNT---TG-----------YHNDSPLHDAAKNGHIDIVKVLLSHGASR 345
Cdd:cd22192    89 GETALHIAVVN------QNLNLVRELIARGADVVSpraTGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADI 162

                          90
                  ....*....|.
gi 1958803882 346 NAVNIFGERPV 356
Cdd:cd22192   163 RAQDSLGNTVL 173
Ank_2 pfam12796
Ankyrin repeats (3 copies);
323-355 2.67e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 2.67e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958803882 323 LHDAAKNGHIDIVKVLLSHGASRNAVNIFGERP 355
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 292-393 3.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 292 EACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVnifgerPVDYTDAENIRSLLllp 371
Cdd:PHA02874   41 DAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL------PIPCIEKDMIKTIL--- 111

                          90       100
                  ....*....|....*....|..
gi 1958803882 372 ektdsfstsQCSVQVNTGQRKS 393
Cdd:PHA02874  112 ---------DCGIDVNIKDAEL 124
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 279-313 5.73e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 5.73e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958803882  279 RGETLLHIAsikheaCSHGHLKIVELLLQHNALVN 313
Cdd:smart00248   1 DGRTPLHLA------AENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 279-314 6.72e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 6.72e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958803882 279 RGETLLHIAsikheaCSHGHLKIVELLLQHNALVNT 314
Cdd:pfam13606   1 DGNTPLHLA------ARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 276-356 6.96e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 276 RNHRGETLLHIASikheacshGHLK---IVELLLQHNALVNTTGY-HNDSPLHDAAKNGhiDIVKVLLSHGASRNAVNIF 351
Cdd:PHA02878  230 RDKCGNTPLHISV--------GYCKdydILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSY 299


                  ....*
gi 1958803882 352 GERPV 356
Cdd:PHA02878  300 KLTPL 304
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 300-356 7.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 7.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958803882 300 KIVELLLQHNALVNTTGYHND-SPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPV 356
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPL 205
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 318-347 9.57e-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: 36.85  E-value: 9.57e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958803882 318 HNDSPLHDAAKNGHIDIVKVLLSHGASRNA 347
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 280-369 1.13e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 280 GETLLHIASIkheacsHGHLKIVELLLQhNA--LVN--TTG--YHNDSPLHDAAKNGHIDIVKVLLSHGA---------- 343
Cdd:cd22192    51 GETALHVAAL------YDNLEAAVVLME-AApeLVNepMTSdlYQGETALHIAVVNQNLNLVRELIARGAdvvspratgt 123

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958803882 344 --SRNAVNI--FGERPVDY---TDAENIRSLLL 369
Cdd:cd22192   124 ffRPGPKNLiyYGEHPLSFaacVGNEEIVRLLI 156
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 236-355 1.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 236 DDSLSLSPGTPPSLLNNSTHRQMMSKPSTVKLSSGIPARKRNhrgeTLLHIASIKheacshGHLKIVELLLQHNALVNTT 315
Cdd:PHA02875   95 DDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF----SPLHLAVMM------GDIKGIELLIDHKACLDIE 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958803882 316 GYHNDSPLHDAAKNGHIDIVKVLLSHGASrnaVNIFGERP 355
Cdd:PHA02875  165 DCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNG 201
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 282-356 1.59e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958803882 282 TLLHIAsikheACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNG-HIDIVKVLLSHGASRNAVNIFGERPV 356
Cdd:PHA02876  410 TALHFA-----LCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 286-343 1.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 1.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958803882 286 IASIKHEACSHGHLKIVELLLQHNALVNTTGYHN-DSPLHDAAKNGHIDIVKVLLSHGA 343
Cdd:PHA02875   68 IESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGA 126
PHA03095 PHA03095
ankyrin-like protein; Provisional
 299-357 1.78e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958803882 299 LKIVELLLQHNALVNTTGYHNDSPLHD--AAKNGHIDIVKVLLSHGASRNAVNIFGERPVD 357
Cdd:PHA03095   97 LDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 291-359 2.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 2.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958803882 291 HEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHI-----DIVKVLLSHGASRNAVNIFGERPVDYT 359
Cdd:PHA03100   40 YLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 279-382 4.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 279 RGETLLHIASIKHEacshghLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERP--- 355
Cdd:PHA02875  101 DGMTPLHLATILKK------LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPlii 174

                          90       100
                  ....*....|....*....|....*...
gi 1958803882 356 -VDYTDAENIRSLLLLPEKTDSFSTSQC 382
Cdd:PHA02875  175 aMAKGDIAICKMLLDSGANIDYFGKNGC 202
Ank_4 pfam13637
Ankyrin repeats (many copies);
267-306 4.90e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 4.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958803882 267 LSSGIPARKRNHRGETLLHIasikheACSHGHLKIVELLL 306
Cdd:pfam13637  21 LEKGADINAVDGNGETALHF------AASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 274-377 5.21e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 274 RKRNHRGETLLHIasikheaCSHG---HLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDI--VKVLLSHGASRNAV 348
Cdd:PHA03095  111 NAKDKVGRTPLHV-------YLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958803882 349 NIFGERPVDY------TDAENIRSLLLL---PEKTDSF 377
Cdd:PHA03095  184 DDRFRSLLHHhlqsfkPRARIVRELIRAgcdPAATDML 221
PHA02946 PHA02946
ankyin-like protein; Provisional
 300-448 6.57e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.27  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 300 KIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDY---TDAENIRSLLLLPEKTDS 376
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsgTDDEVIERINLLVQYGAK 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958803882 377 FSTSqcsvqvnTGQRKSGPLVligsGLSSQQQKLLSKLETV-LKAKKCAEF-DNTVTHVIVPDEEAQSTLKCML 448
Cdd:PHA02946  133 INNS-------VDEEGCGPLL----ACTDPSERVFKKIMSIgFEARIVDKFgKNHIHRHLMSDNPKASTISWMM 195
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 494-581 7.78e-03

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: 35.80  E-value: 7.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 494 LPKLFDGCYFFLGGnFKHHPKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYHAKPDSDQRFCTQYIvyedlFNChp 573
Cdd:pfam16589   1 LPNLFEPLRFYINA-IPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWI-----FDC-- 72


                  ....*...
gi 1958803882 574 erVRQGKV 581
Cdd:pfam16589  73 --VKKGKL 78
PHA03095 PHA03095
ankyrin-like protein; Provisional
 277-368 9.13e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803882 277 NHRGE---TLLHI-ASIKHEACshghLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGH-IDIVKVLLSHGASRNAVNIF 351
Cdd:PHA03095   41 NFRGEygkTPLHLyLHYSSEKV----KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKV 116

                          90       100
                  ....*....|....*....|...
gi 1958803882 352 GERPV------DYTDAENIRSLL 368
Cdd:PHA03095  117 GRTPLhvylsgFNINPKVIRLLL 139
 
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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