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Conserved domains on  [gi|725562523|ref|XP_010334664|]
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BRCA1-associated RING domain protein 1 isoform X3 [Saimiri boliviensis boliviensis]

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 ...
 525-625 4.85e-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: 157.91  E-value: 4.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 525 LFDGCYFYFGGTFKHH-PKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYhARPDSDQRFCTQYIIYENLSNYHPER 603
Cdd:cd17720    1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                         90       100
                 ....*....|....*....|..
gi 725562523 604 VRQGKVWMAPSSWFIDCVMSFE 625
Cdd:cd17720   80 VRQGKVRVVPVSWLLDCISQFK 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
278-399 1.08e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 1.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 357
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 725562523 358 NGHMDIVKLLLSCGASRNAVNIFGLRPVDY---TDDEDMKSLLLL 399
Cdd:COG0666  196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLaaeNGNLEIVKLLLE 240
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 424-500 3.06e-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: 116.16  E-value: 3.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 424 LVLIGSGLSSEQQKMLSELAAILKAKKCTEFDSTVTHVVVPGDE---VQSTLKCMLGILNGCWILKFEWVKACLRRKVCE 500
Cdd:cd17734    1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 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 ...
 525-625 4.85e-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: 157.91  E-value: 4.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 525 LFDGCYFYFGGTFKHH-PKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYhARPDSDQRFCTQYIIYENLSNYHPER 603
Cdd:cd17720    1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                         90       100
                 ....*....|....*....|..
gi 725562523 604 VRQGKVWMAPSSWFIDCVMSFE 625
Cdd:cd17720   80 VRQGKVRVVPVSWLLDCISQFK 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
278-399 1.08e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 1.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 357
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 725562523 358 NGHMDIVKLLLSCGASRNAVNIFGLRPVDY---TDDEDMKSLLLL 399
Cdd:COG0666  196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLaaeNGNLEIVKLLLE 240
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 424-500 3.06e-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: 116.16  E-value: 3.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 424 LVLIGSGLSSEQQKMLSELAAILKAKKCTEFDSTVTHVVVPGDE---VQSTLKCMLGILNGCWILKFEWVKACLRRKVCE 500
Cdd:cd17734    1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
286-378 1.04e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 104.04  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523  286 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTgyQNDSPLHDAAKNGHMDIVK 365
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 725562523  366 LLLSCGASRNAVN 378
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 277-388 2.01e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 277 KRNHRGETLLHIASIK--GDIPSVEYLLQNGSDPNVKDHAGWTPLHEA--CNHGHLKVVELLLQHKALVN---------T 343
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINaknrvnyllS 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 725562523 344 TGY-------QNDSPLHDAAKNGHMDIVKLLLSCGASRNAVNIFGLRPVDYT 388
Cdd:PHA03100 181 YGVpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
BRCT smart00292
breast cancer carboxy-terminal domain;
425-494 6.68e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 52.76  E-value: 6.68e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 725562523   425 VLIGSGLSSEQQKMLSELAAILKAKKCTEFDS-TVTHVVVpGDEVQSTLKCMLGILNGCWILKFEWVKACL 494
Cdd:smart00292   9 FYITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIV-GSPEGGKLELLKAIALGIPIVKEEWLLDCL 78
BRCT smart00292
breast cancer carboxy-terminal domain;
523-621 6.56e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 47.37  E-value: 6.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523   523 PKLFDGCYFYFGGTFKHHPKDNLIKLVTAGGGQILSRKPKPDsdvtqtintvayharpdsdqrfcTQYIIYENLSN--YH 600
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVGSPEGgkLE 57

                           90       100
                   ....*....|....*....|.
gi 725562523   601 PERVRQGKVWMAPSSWFIDCV 621
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 315-342 1.09e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 45.27  E-value: 1.09e-06
                           10        20
                   ....*....|....*....|....*...
gi 725562523   315 GWTPLHEACNHGHLKVVELLLQHKALVN 342
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 282-381 9.52e-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: 48.86  E-value: 9.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 282 GETLLHIASIKGDIPSVEYLLQNGSD----PNVKD-HAGWTPLHEACNHGHLKVVELLLQHKALVNT---TG-------- 345
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPElvnePMTSDlYQGETALHIAVVNQNLNLVRELIARGADVVSpraTGtffrpgpk 130

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 725562523 346 ---YQNDSPLHDAAKNGHMDIVKLLLSCGASRNAVNIFG 381
Cdd:cd22192  131 nliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 522-630 2.89e-04

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


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 40.04  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523  522 LPKLFDGCYFYFgGTFKHHPKDNLIKLVTAGGGQIlsrkpkpdsdvTQTINTVAYHarpdsdqRFCTQYIIYENLSNYHP 601
Cdd:pfam16589   1 LPNLFEPLRFYI-NAIPSPSRSKLKRLIEANGGTV-----------VDNINPAVYI-------VIAPYNKTDKLAENTKL 61

                          90       100
                  ....*....|....*....|....*....
gi 725562523  602 ERVRqgkvwmapSSWFIDCVMSFELLPLD 630
Cdd:pfam16589  62 GVVS--------PQWIFDCVKKGKLLPLE 82
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 429-494 2.29e-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: 37.27  E-value: 2.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 725562523  429 SGLSSEQQKMLSELAAILKAKKCTEFDSTVTHVVVPGDevqsTLKCMLGILNGCWILKFEWVKACL 494
Cdd:pfam00533  14 TGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEAR----TKKYLKAKELGIPIVTEEWLLDCI 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 ...
 525-625 4.85e-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: 157.91  E-value: 4.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 525 LFDGCYFYFGGTFKHH-PKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYhARPDSDQRFCTQYIIYENLSNYHPER 603
Cdd:cd17720    1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                         90       100
                 ....*....|....*....|..
gi 725562523 604 VRQGKVWMAPSSWFIDCVMSFE 625
Cdd:cd17720   80 VRQGKVRVVPVSWLLDCISQFK 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
278-399 1.08e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 1.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 357
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 725562523 358 NGHMDIVKLLLSCGASRNAVNIFGLRPVDY---TDDEDMKSLLLL 399
Cdd:COG0666  196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLaaeNGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
278-398 4.96e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 4.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 357
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 725562523 358 NGHMDIVKLLLSCGASRNAVNIFGLRPVDY---TDDEDMKSLLL 398
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLaaeNGHLEIVKLLL 206
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 424-500 3.06e-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: 116.16  E-value: 3.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 424 LVLIGSGLSSEQQKMLSELAAILKAKKCTEFDSTVTHVVVPGDE---VQSTLKCMLGILNGCWILKFEWVKACLRRKVCE 500
Cdd:cd17734    1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
278-399 3.80e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 3.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 357
Cdd:COG0666  149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 725562523 358 NGHMDIVKLLLSCGASRNAVNIFGLRPVDYTDDEDMKSLLLL 399
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
Ank_2 pfam12796
Ankyrin repeats (3 copies);
286-378 1.04e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 104.04  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523  286 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTgyQNDSPLHDAAKNGHMDIVK 365
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 725562523  366 LLLSCGASRNAVN 378
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-398 5.18e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 5.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 267 AMKLLPNMAGKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGY 346
Cdd:COG0666   39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 725562523 347 QNDSPLHDAAKNGHMDIVKLLLSCGASRNAVNIFGLRPVDY---TDDEDMKSLLL 398
Cdd:COG0666  119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLEIVKLLL 173
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
278-383 1.48e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 357
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                         90       100
                 ....*....|....*....|....*.
gi 725562523 358 NGHMDIVKLLLSCGASRNAVNIFGLR 383
Cdd:COG0666  262 AGAALIVKLLLLALLLLAAALLDLLT 287
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 277-388 2.01e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 277 KRNHRGETLLHIASIK--GDIPSVEYLLQNGSDPNVKDHAGWTPLHEA--CNHGHLKVVELLLQHKALVN---------T 343
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINaknrvnyllS 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 725562523 344 TGY-------QNDSPLHDAAKNGHMDIVKLLLSCGASRNAVNIFGLRPVDYT 388
Cdd:PHA03100 181 YGVpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 264-378 5.29e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.40  E-value: 5.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 264 SPSAMKLLPNMAGK---RNHRGETLLHIA--SIKGDIP----------------SVEYLLQNGSDPNVKDHAGWTPLHEA 322
Cdd:PHA03100 120 SYSIVEYLLDNGANvniKNSDGENLLHLYleSNKIDLKilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYA 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 725562523 323 CNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHMDIVKLLLSCGASRNAVN 378
Cdd:PHA03100 200 VYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
275-344 2.73e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 2.73e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523  275 AGKRNHRGETLLHIASIKGDIPSVEYLLQNGsDPNVKDHaGWTPLHEACNHGHLKVVELLLQHKALVNTT 344
Cdd:pfam12796  23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
284-335 1.13e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 65.76  E-value: 1.13e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 725562523  284 TLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLL 335
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 278-371 1.87e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.69  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 357
Cdd:PHA02874 120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                         90
                 ....*....|....
gi 725562523 358 NGHMDIVKLLLSCG 371
Cdd:PHA02874 200 YGDYACIKLLIDHG 213
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 285-370 8.73e-13

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 71.47  E-value: 8.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 285 LLHIASiKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHMDIV 364
Cdd:PTZ00322  86 LCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                 ....*.
gi 725562523 365 KLLLSC 370
Cdd:PTZ00322 165 QLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
315-368 9.11e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.06  E-value: 9.11e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 725562523  315 GWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHMDIVKLLL 368
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 424-493 1.70e-12

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


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 62.76  E-value: 1.70e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 424 LVLIGSGLSSEQQKMLSELAAILKAKKCTEFDSTVTHVVVPGDEvqSTLKCMLGILNGCWILKFEWVKAC 493
Cdd:cd00027    1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPS--GEKYYLAALAWGIPIVSPEWLLDC 68
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-398 1.26e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.75  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 267 AMKLLPNMAGKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGY 346
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 725562523 347 QNDSPLHDAAKNGHMDIVKLLLSCGASRNAVNIFGLRPVD---YTDDEDMKSLLL 398
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHlaaYNGNLEIVKLLL 140
PHA03095 PHA03095
ankyrin-like protein; Provisional
 255-386 1.27e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 255 SSRYRRVTSSPSA----MKLLPNMAGKRNHRGE---TLLHI---ASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLH-EAC 323
Cdd:PHA03095  13 AALYDYLLNASNVtveeVRRLLAAGADVNFRGEygkTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLY 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 725562523 324 NHGHLKVVELLLQHKALVNTTGYQNDSPLHD--AAKNGHMDIVKLLLSCGASRNAVNIFGLRPVD 386
Cdd:PHA03095  93 NATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 277-398 1.61e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 277 KRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAA 356
Cdd:PHA02878 163 KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 725562523 357 KN-GHMDIVKLLLSCGASRNAVN-IFGLRPVDYT-DDEDMKSLLL 398
Cdd:PHA02878 243 GYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSiKSERKLKLLL 287
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 425-495 2.70e-11

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


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 59.53  E-value: 2.70e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 725562523 425 VLIGSGLSSEQQKMLSELAAILK-AKKCTEFDSTVTHVVVPGDEvqSTLKCMLGILNGCWILKFEWVKACLR 495
Cdd:cd17736    2 TLVMTSVHSEEQELLESVVKKLGgFRVEDSVTEKTTHVVVGSPR--RTLNVLLGIARGCWILSPDWVLESLE 71
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 426-507 6.30e-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: 59.28  E-value: 6.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 426 LIGSGLSSEQQKMLSELAAILKAKKCTEFDSTVTHVVVPGDE---VQSTLKCMLGILNGCWILKFEWVKACLRRKVCEQE 502
Cdd:cd17735    3 MVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAelvCERTLKYFLGIAGRKWVVSYQWITQSIKEGKILPE 82


                 ....*
gi 725562523 503 EKYEI 507
Cdd:cd17735   83 HDFEV 87
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 281-384 1.20e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 281 RGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGH 360
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                         90       100
                 ....*....|....*....|....
gi 725562523 361 MDIVKLLLSCGASrnaVNIFGLRP 384
Cdd:PHA02875 181 IAICKMLLDSGAN---IDYFGKNG 201
BRCT smart00292
breast cancer carboxy-terminal domain;
425-494 6.68e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 52.76  E-value: 6.68e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 725562523   425 VLIGSGLSSEQQKMLSELAAILKAKKCTEFDS-TVTHVVVpGDEVQSTLKCMLGILNGCWILKFEWVKACL 494
Cdd:smart00292   9 FYITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIV-GSPEGGKLELLKAIALGIPIVKEEWLLDCL 78
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 286-385 6.90e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 286 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACnhGHLK---VVELLLQHKALVNTTGY-QNDSPLHDAAKNGhm 361
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdydILKLLLEHGVDVNAKSYiLGLTALHSSIKSE-- 280

                         90       100
                 ....*....|....*....|....
gi 725562523 362 DIVKLLLSCGASRNAVNIFGLRPV 385
Cdd:PHA02878 281 RKLKLLLEYGADINSLNSYKLTPL 304
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 284-388 1.37e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 284 TLLHIASIKGDIpsVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHMDI 363
Cdd:PHA02874  95 SILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI 172

                         90       100
                 ....*....|....*....|....*
gi 725562523 364 VKLLLSCGASRNAVNIFGLRPVDYT 388
Cdd:PHA02874 173 IKLLLEKGAYANVKDNNGESPLHNA 197
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 284-377 9.48e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 9.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 284 TLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQND-SPLHDAAKNGHMD 362
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKID 216

                         90
                 ....*....|....*
gi 725562523 363 IVKLLLSCGASRNAV 377
Cdd:PHA02875 217 IVRLFIKRGADCNIM 231
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 278-386 1.58e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHlKVVELLLQHKAlVNTTGYQNDSPLHDAAK 357
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNAS-INDQDIDGSTPLHHAIN 263

                         90       100       110
                 ....*....|....*....|....*....|
gi 725562523 358 NG-HMDIVKLLLSCGASRNAVNIFGLRPVD 386
Cdd:PHA02874 264 PPcDIDIIDILLYHKADISIKDNKGENPID 293
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 262-378 1.75e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.30  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 262 TSSPSAMKLLPNM------AGKRNHRGETLLHIASIKG-DIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLK-VVEL 333
Cdd:PHA02876 281 SQAPSLSRLVPKLlergadVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVIT 360

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 725562523 334 LLQHKALVNTTGYQNDSPLHDAAKNGHMDIVKLLLSCGASRNAVN 378
Cdd:PHA02876 361 LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 285-375 2.79e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 285 LLHIASIkGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHMDIV 364
Cdd:PLN03192 529 LLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF 607

                         90
                 ....*....|.
gi 725562523 365 KLLLSCGASRN 375
Cdd:PLN03192 608 RILYHFASISD 618
Ank_5 pfam13857
Ankyrin repeats (many copies);
278-322 3.74e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 3.74e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 725562523  278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEA 322
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
270-312 4.63e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 4.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 725562523  270 LLPNMAGKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKD 312
Cdd:pfam12796  49 LLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 243-397 5.60e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 5.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 243 SLSPGTPPSTLnSSRYRRVTsspsAMKLLPNMAGKRNHRG---ETLLHIASIKGDIPSVEYLLQNGSDPN-VKDHAGWTP 318
Cdd:PHA02875  31 EIYDGISPIKL-AMKFRDSE----AIKLLMKHGAIPDVKYpdiESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 319 LHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHMDIVKLLLSCGASRNAVNIFGLRP----VDYTDDEDMK 394
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPliiaMAKGDIAICK 185


                 ...
gi 725562523 395 SLL 397
Cdd:PHA02875 186 MLL 188
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 278-337 6.15e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 6.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQH 337
Cdd:PTZ00322 111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
BRCT smart00292
breast cancer carboxy-terminal domain;
523-621 6.56e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 47.37  E-value: 6.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523   523 PKLFDGCYFYFGGTFKHHPKDNLIKLVTAGGGQILSRKPKPDsdvtqtintvayharpdsdqrfcTQYIIYENLSN--YH 600
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVGSPEGgkLE 57

                           90       100
                   ....*....|....*....|.
gi 725562523   601 PERVRQGKVWMAPSSWFIDCV 621
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
Ank_5 pfam13857
Ankyrin repeats (many copies);
334-387 7.58e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 7.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 725562523  334 LLQHK-ALVNTTGYQNDSPLHDAAKNGHMDIVKLLLSCGASRNAVNIFGLRPVDY 387
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 254-399 9.21e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 9.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 254 NSSRYRRVTSSPSAMKLLPnmagKRNHRGETLLhiasikgdipsVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVEL 333
Cdd:PHA02876 132 NDIHYDKINESIEYMKLIK----ERIQQDELLI-----------AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNL 196

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 725562523 334 LLQHKALVNTTGYQNDSPLHDAAKNGHMDIVKLLLScgaSRNAVNIFGLRPVDYTDDEDMKSLLLL 399
Cdd:PHA02876 197 LLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID---NRSNINKNDLSLLKAIRNEDLETSLLL 259
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 315-342 1.09e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 45.27  E-value: 1.09e-06
                           10        20
                   ....*....|....*....|....*...
gi 725562523   315 GWTPLHEACNHGHLKVVELLLQHKALVN 342
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 315-342 1.19e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.36  E-value: 1.19e-06
                          10        20
                  ....*....|....*....|....*....
gi 725562523  315 GWTPLHEACNH-GHLKVVELLLQHKALVN 342
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 295-387 1.58e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 295 IPSVEYLLQNGSDPNVKDHAGWTPLHeACNHG---HLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGH--MDIVKLLLS 369
Cdd:PHA03095  97 LDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLID 175

                         90
                 ....*....|....*...
gi 725562523 370 CGASRNAVNIFGLRPVDY 387
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHH 193
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 286-387 2.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 286 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHmDIVK 365
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIE 239

                         90       100
                 ....*....|....*....|..
gi 725562523 366 LLLScGASRNAVNIFGLRPVDY 387
Cdd:PHA02874 240 LLIN-NASINDQDIDGSTPLHH 260
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 281-436 3.38e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 3.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 281 RGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVN------------------ 342
Cdd:PLN03192 557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDphaagdllctaakrndlt 636

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 343 ------TTGYQNDSPLHD-------AAKNGHMDIVKLLLSCGASRNAVNIfglrpvdytdDEDMKSLLL--LPEKNESSS 407
Cdd:PLN03192 637 amkellKQGLNVDSEDHQgatalqvAMAEDHVDMVRLLIMNGADVDKANT----------DDDFSPTELreLLQKRELGH 706

                        170       180       190
                 ....*....|....*....|....*....|....
gi 725562523 408 T-----SHCSVVNTGQRKDGPLVLIGSGLSSEQQ 436
Cdd:PLN03192 707 SitivdSVPADEPDLGRDGGSRPGRLQGTSSDNQ 740
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 349-378 5.95e-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: 43.05  E-value: 5.95e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 725562523  349 DSPLHDAA-KNGHMDIVKLLLSCGASRNAVN 378
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 293-397 8.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 8.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 293 GDIPSVEYLLQN-GSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHMDIVKLLLSCG 371
Cdd:PHA02874  12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                         90       100
                 ....*....|....*....|....*.
gi 725562523 372 ASRNAVnifglrPVDYTDDEDMKSLL 397
Cdd:PHA02874  92 VDTSIL------PIPCIEKDMIKTIL 111
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 278-385 9.13e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 9.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEA-CNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAA 356
Cdd:PHA02876 371 RDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYAC 450

                         90       100       110
                 ....*....|....*....|....*....|
gi 725562523 357 KNG-HMDIVKLLLSCGASRNAVNIFGLRPV 385
Cdd:PHA02876 451 KKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 282-381 9.52e-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: 48.86  E-value: 9.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 282 GETLLHIASIKGDIPSVEYLLQNGSD----PNVKD-HAGWTPLHEACNHGHLKVVELLLQHKALVNT---TG-------- 345
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPElvnePMTSDlYQGETALHIAVVNQNLNLVRELIARGADVVSpraTGtffrpgpk 130

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 725562523 346 ---YQNDSPLHDAAKNGHMDIVKLLLSCGASRNAVNIFG 381
Cdd:cd22192  131 nliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 429-495 1.09e-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: 1.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 725562523 429 SGLSSEQQKMLSELAAILKAKKCT--EFDSTVTHVVVPgdEVQSTLKCMLGILNGCWILKFEWVKACLR 495
Cdd:cd17738    7 SGFSEDEKKELISIIEKLGGKVLDsdEFDPKCTHLICG--KPSRSEKFLAACAAGKWILHPSYIEASAK 73
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 315-343 1.57e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 1.57e-05
                          10        20
                  ....*....|....*....|....*....
gi 725562523  315 GWTPLHEACNHGHLKVVELLLQHKALVNT 343
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 347-376 1.60e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 1.60e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 725562523   347 QNDSPLHDAAKNGHMDIVKLLLSCGASRNA 376
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 282-387 2.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 282 GETLLHI----ASIKGDIpsVEYLLQNGSDPNVKDHAGWTPLH-----EACNhghLKVVELLLQHKALVNTTGYQNDSPL 352
Cdd:PHA03095 117 GRTPLHVylsgFNINPKV--IRLLLRKGADVNALDLYGMTPLAvllksRNAN---VELLRLLIDAGADVYAVDDRFRSLL 191

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 725562523 353 HDAAKNGHMD--IVKLLLSCGASRNAVNIFGLRPVDY 387
Cdd:PHA03095 192 HHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHS 228
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 283-373 2.92e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.93  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 283 ETLLHIASIKGDIPSVEYLLQNGS-DPNVKDHAGWTPLHEACNHGHLKVVELLLQH-KALVN--TTG--YQNDSPLHDAA 356
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNepMTSdlYQGETALHIAV 97

                         90
                 ....*....|....*..
gi 725562523 357 KNGHMDIVKLLLSCGAS 373
Cdd:cd22192   98 VNQNLNLVRELIARGAD 114
Ank_5 pfam13857
Ankyrin repeats (many copies);
301-353 2.95e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 725562523  301 LLQNGS-DPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLH 353
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 423-495 3.36e-05

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


Pssm-ID: 349372 [Multi-domain]  Cd Length: 74  Bit Score: 42.20  E-value: 3.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 725562523 423 PLVLIGSGLSSEQQKMLSELAAILKAKKCTEFDSTVTHVVVPgdEVQSTLKCMLGILNGCWILKFEWVKACLR 495
Cdd:cd17741    2 PLVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMS--KIKVTVKVICALISGKPIVTPEYLDALLE 72
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 297-388 4.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 4.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 297 SVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGH-----MDIVKLLLSCG 371
Cdd:PHA03100  17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYG 96

                         90
                 ....*....|....*..
gi 725562523 372 ASRNAVNIFGLRPVDYT 388
Cdd:PHA03100  97 ANVNAPDNNGITPLLYA 113
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 281-313 4.81e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 4.81e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 725562523  281 RGETLLHIASIK-GDIPSVEYLLQNGSDPNVKDH 313
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 331-446 7.19e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 7.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 331 VELLLQHKALVNTTGYQNDSPLHDAAKNGHMDIVKLLLSCGASRNAVNIFGLRPVDYTDDEDMKSL--LLLPEKNESSST 408
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVvqLLSRHSQCHFEL 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 725562523 409 SHCSVVNT-----GQRKDGPLVLIGSGLSSEQQKMLSELAAIL 446
Cdd:PTZ00322 178 GANAKPDSftgkpPSLEDSPISSHHPDFSAVPQPMMGSLIVIM 220
Ank_4 pfam13637
Ankyrin repeats (many copies);
348-387 8.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 8.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 725562523  348 NDSPLHDAAKNGHMDIVKLLLSCGASRNAVNIFGLRPVDY 387
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 281-310 1.40e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 1.40e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 725562523  281 RGETLLHIASIKGDIPSVEYLLQNGSDPNV 310
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 289-377 1.55e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 289 ASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHMDIVKLLL 368
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88


                 ....*....
gi 725562523 369 SCGASRNAV 377
Cdd:PHA02875  89 DLGKFADDV 97
Ank_2 pfam12796
Ankyrin repeats (3 copies);
352-384 1.57e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 1.57e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 725562523  352 LHDAAKNGHMDIVKLLLSCGASRNAVNIFGLRP 384
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 522-630 2.89e-04

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


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 40.04  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523  522 LPKLFDGCYFYFgGTFKHHPKDNLIKLVTAGGGQIlsrkpkpdsdvTQTINTVAYHarpdsdqRFCTQYIIYENLSNYHP 601
Cdd:pfam16589   1 LPNLFEPLRFYI-NAIPSPSRSKLKRLIEANGGTV-----------VDNINPAVYI-------VIAPYNKTDKLAENTKL 61

                          90       100
                  ....*....|....*....|....*....
gi 725562523  602 ERVRqgkvwmapSSWFIDCVMSFELLPLD 630
Cdd:pfam16589  62 GVVS--------PQWIFDCVKKGKLLPLE 82
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 281-310 6.61e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 6.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 725562523   281 RGETLLHIASIKGDIPSVEYLLQNGSDPNV 310
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 246-357 9.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 9.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 246 PGTPPSTLNSSRYRRVTSS--PSAMKLLPNMA--GKRNHRGETLLHIASIK-GDIPSVEYLLQNGSDPNVKDHA-GWTPL 319
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYnkPIVHILLENGAstDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTAL 273

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 725562523 320 HEACNHGhlKVVELLLQHKALVNTTGYQNDSPLHDAAK 357
Cdd:PHA02878 274 HSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03095 PHA03095
ankyrin-like protein; Provisional
 278-335 1.47e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 725562523 278 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLL 335
Cdd:PHA03095 253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02946 PHA02946
ankyin-like protein; Provisional
 291-385 2.26e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 291 IKG-DIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLH--DAAKNGHMDIVKLL 367
Cdd:PHA02946  47 IKGlDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLL 126

                         90
                 ....*....|....*....
gi 725562523 368 LSCGAS-RNAVNIFGLRPV 385
Cdd:PHA02946 127 VQYGAKiNNSVDEEGCGPL 145
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 429-494 2.29e-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: 37.27  E-value: 2.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 725562523  429 SGLSSEQQKMLSELAAILKAKKCTEFDSTVTHVVVPGDevqsTLKCMLGILNGCWILKFEWVKACL 494
Cdd:pfam00533  14 TGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEAR----TKKYLKAKELGIPIVTEEWLLDCI 75
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 433-495 4.20e-03

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


Pssm-ID: 349359 [Multi-domain]  Cd Length: 75  Bit Score: 36.42  E-value: 4.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 725562523 433 SEQQKMLSELAAILKAKKCTEFDSTVTHVVVPGDEVQSTLKCMLGILNGCWILKFEWVKACLR 495
Cdd:cd17727   13 SKRQGELNKIAASLGAEYRWTYDESCTHFIYQGKANDTNREYKSAKEQGKFIVSPHWLYACKE 75
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 350-376 4.50e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 4.50e-03
                          10        20
                  ....*....|....*....|....*..
gi 725562523  350 SPLHDAAKNGHMDIVKLLLSCGASRNA 376
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 278-377 6.02e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 278 RNHRGETLLHI--ASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLK--VVELLLQHKALVNTTGYQNDSPLH 353
Cdd:PHA03095 183 VDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262

                         90       100
                 ....*....|....*....|....
gi 725562523 354 DAAKNGHMDIVKLLLSCGASRNAV 377
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAV 286
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 294-385 6.12e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.90  E-value: 6.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 294 DIPSVEYLLQNGSDPNVKDHAGWTPLHEAC--NHGHLKVVELLLQHKALVNTTGYQNDSPLH--------------DAAK 357
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYIlrHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildpETDN 375

                         90       100
                 ....*....|....*....|....*...
gi 725562523 358 NGHMDIVKLLLSCGASRNAVNIFGLRPV 385
Cdd:PHA02716 376 DIRLDVIQCLISLGADITAVNCLGYTPL 403
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 280-349 8.22e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 8.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725562523 280 HRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQND 349
Cdd:PLN03192 620 HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
 
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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