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Conserved domains on  [gi|543583787|ref|NP_001269472|]
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BRCA1-associated RING domain protein 1 isoform 2 [Homo sapiens]

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 ...
 652-752 3.23e-45

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


:

Pssm-ID: 349352  Cd Length: 101  Bit Score: 156.75  E-value: 3.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 652 LFDGCYFYLWGTFKHH-PKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYhARPDSDQRFCTQYIIYEDLCNYHPER 730
Cdd:cd17720    1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                         90       100
                 ....*....|....*....|..
gi 543583787 731 VRQGKVWKAPSSWFIDCVMSFE 752
Cdd:cd17720   80 VRQGKVRVVPVSWLLDCISQFK 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
405-514 1.09e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 484
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                         90       100       110
                 ....*....|....*....|....*....|
gi 543583787 485 NGHVDIVKLLLSYGASRNAVNIFGLRPVDY 514
Cdd:COG0666  196 NGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 551-627 8.33e-30

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


:

Pssm-ID: 349366  Cd Length: 80  Bit Score: 112.69  E-value: 8.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 551 LVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGD---AVQSTLKCMLGILNGCWILKFEWVKACLRRKVCE 627
Cdd:cd17734    1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADergVCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 33-99 1.08e-29

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16496:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 86  Bit Score: 112.43  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787  33 AWAHSRAALDRLEKLLRCSRC-------------------NCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMIQLCSKLR 93
Cdd:cd16496    1 KWARTRAALDELENLLRCSRCasilkepvtlggcehvfcrSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLR 80


                 ....*.
gi 543583787  94 NLLHDN 99
Cdd:cd16496   81 NLLNDN 86
 
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 ...
 652-752 3.23e-45

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


Pssm-ID: 349352  Cd Length: 101  Bit Score: 156.75  E-value: 3.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 652 LFDGCYFYLWGTFKHH-PKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYhARPDSDQRFCTQYIIYEDLCNYHPER 730
Cdd:cd17720    1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                         90       100
                 ....*....|....*....|..
gi 543583787 731 VRQGKVWKAPSSWFIDCVMSFE 752
Cdd:cd17720   80 VRQGKVRVVPVSWLLDCISQFK 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
405-514 1.09e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 484
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                         90       100       110
                 ....*....|....*....|....*....|
gi 543583787 485 NGHVDIVKLLLSYGASRNAVNIFGLRPVDY 514
Cdd:COG0666  196 NGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 551-627 8.33e-30

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


Pssm-ID: 349366  Cd Length: 80  Bit Score: 112.69  E-value: 8.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 551 LVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGD---AVQSTLKCMLGILNGCWILKFEWVKACLRRKVCE 627
Cdd:cd17734    1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADergVCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 33-99 1.08e-29

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


Pssm-ID: 438159 [Multi-domain]  Cd Length: 86  Bit Score: 112.43  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787  33 AWAHSRAALDRLEKLLRCSRC-------------------NCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMIQLCSKLR 93
Cdd:cd16496    1 KWARTRAALDELENLLRCSRCasilkepvtlggcehvfcrSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLR 80


                 ....*.
gi 543583787  94 NLLHDN 99
Cdd:cd16496   81 NLLNDN 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
413-505 2.49e-27

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 105.97  E-value: 2.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787  413 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTgyQNDSPLHDAAKNGHVDIVK 492
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 543583787  493 LLLSYGASRNAVN 505
Cdd:pfam12796  79 LLLEKGADINVKD 91
zf-RING_6 pfam14835
zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer ...
 41-86 6.14e-19

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


Pssm-ID: 434253 [Multi-domain]  Cd Length: 65  Bit Score: 81.25  E-value: 6.14e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543583787   41 LDRLEKLLRCSRC-------------------NCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI 86
Cdd:pfam14835   1 LDRLEKLLRCSRCtnilrepvclggcehifcsNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 389-505 2.45e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 389 MSSPSAMKLLPNMAVKRN---HRGETLLHIA--SIKGDIP----------------SVEYLLQNGSDPNVKDHAGWTPLH 447
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNiknSDGENLLHLYleSNKIDLKilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLH 197

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 543583787 448 EACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVN 505
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
BRCT smart00292
breast cancer carboxy-terminal domain;
552-621 4.27e-10

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 56.61  E-value: 4.27e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543583787   552 VLIGSGLSSEQQKMLSELAVILKAKKYTEFDS-TVTHVVVpGDAVQSTLKCMLGILNGCWILKFEWVKACL 621
Cdd:smart00292   9 FYITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIV-GSPEGGKLELLKAIALGIPIVKEEWLLDCL 78
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 442-469 1.31e-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: 1.31e-06
                           10        20
                   ....*....|....*....|....*...
gi 543583787   442 GWTPLHEACNHGHLKVVELLLQHKALVN 469
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 410-500 3.71e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 410 ETLLHIASIKGDIPSVEYLLQNGS-DPNVKDHAGWTPLHEACNHGHLKVVELLLQH-KALVN--TTG--YQNDSPLHDAA 483
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNepMTSdlYQGETALHIAV 97

                         90
                 ....*....|....*..
gi 543583787 484 KNGHVDIVKLLLSYGAS 500
Cdd:cd22192   98 VNQNLNLVRELIARGAD 114
BRCT smart00292
breast cancer carboxy-terminal domain;
650-748 2.57e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 43.13  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787   650 PKLFDGCYFYLWGTFKHHPKDNLIKLVTAGGGQILSRKPKPDsdvtqtintvayharpdsdqrfcTQYIIYEDL--CNYH 727
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVGSPegGKLE 57

                           90       100
                   ....*....|....*....|.
gi 543583787   728 PERVRQGKVWKAPSSWFIDCV 748
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 649-757 1.60e-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: 40.81  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787  649 LPKLFDGCYFYLwGTFKHHPKDNLIKLVTAGGGQIlsrkpkpdsdvTQTINTvayharpdsdqrfCTQYIIYEDLCNYHP 728
Cdd:pfam16589   1 LPNLFEPLRFYI-NAIPSPSRSKLKRLIEANGGTV-----------VDNINP-------------AVYIVIAPYNKTDKL 55

                          90       100
                  ....*....|....*....|....*....
gi 543583787  729 ERVRQGKVWKApsSWFIDCVMSFELLPLD 757
Cdd:pfam16589  56 AENTKLGVVSP--QWIFDCVKKGKLLPLE 82
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 556-621 1.64e-04

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


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 40.74  E-value: 1.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543583787  556 SGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGDavqsTLKCMLGILNGCWILKFEWVKACL 621
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 ...
 652-752 3.23e-45

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


Pssm-ID: 349352  Cd Length: 101  Bit Score: 156.75  E-value: 3.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 652 LFDGCYFYLWGTFKHH-PKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYhARPDSDQRFCTQYIIYEDLCNYHPER 730
Cdd:cd17720    1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                         90       100
                 ....*....|....*....|..
gi 543583787 731 VRQGKVWKAPSSWFIDCVMSFE 752
Cdd:cd17720   80 VRQGKVRVVPVSWLLDCISQFK 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
405-514 1.09e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 484
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                         90       100       110
                 ....*....|....*....|....*....|
gi 543583787 485 NGHVDIVKLLLSYGASRNAVNIFGLRPVDY 514
Cdd:COG0666  196 NGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
405-524 2.89e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.69  E-value: 2.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 484
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 543583787 485 NGHVDIVKLLLSYGASRNAVNIFGLRP----VDYTDDESMKSLL 524
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPlhlaAENGHLEIVKLLL 206
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 551-627 8.33e-30

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


Pssm-ID: 349366  Cd Length: 80  Bit Score: 112.69  E-value: 8.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 551 LVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGD---AVQSTLKCMLGILNGCWILKFEWVKACLRRKVCE 627
Cdd:cd17734    1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADergVCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 33-99 1.08e-29

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


Pssm-ID: 438159 [Multi-domain]  Cd Length: 86  Bit Score: 112.43  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787  33 AWAHSRAALDRLEKLLRCSRC-------------------NCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMIQLCSKLR 93
Cdd:cd16496    1 KWARTRAALDELENLLRCSRCasilkepvtlggcehvfcrSCVGDRLGNGCPVCDTPAWARDLQINRQLDSMVQLCRKLR 80


                 ....*.
gi 543583787  94 NLLHDN 99
Cdd:cd16496   81 NLLNDN 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
405-514 1.81e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 1.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 484
Cdd:COG0666  149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                         90       100       110
                 ....*....|....*....|....*....|
gi 543583787 485 NGHVDIVKLLLSYGASRNAVNIFGLRPVDY 514
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
413-505 2.49e-27

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 105.97  E-value: 2.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787  413 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTgyQNDSPLHDAAKNGHVDIVK 492
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 543583787  493 LLLSYGASRNAVN 505
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
394-511 1.30e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 1.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 394 AMKLLPNMAVKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGY 473
Cdd:COG0666   39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 543583787 474 QNDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIFGLRP 511
Cdd:COG0666  119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
405-510 7.50e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.78  E-value: 7.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 484
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                         90       100
                 ....*....|....*....|....*.
gi 543583787 485 NGHVDIVKLLLSYGASRNAVNIFGLR 510
Cdd:COG0666  262 AGAALIVKLLLLALLLLAAALLDLLT 287
zf-RING_6 pfam14835
zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer ...
 41-86 6.14e-19

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


Pssm-ID: 434253 [Multi-domain]  Cd Length: 65  Bit Score: 81.25  E-value: 6.14e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543583787   41 LDRLEKLLRCSRC-------------------NCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI 86
Cdd:pfam14835   1 LDRLEKLLRCSRCtnilrepvclggcehifcsNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 389-505 2.45e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 389 MSSPSAMKLLPNMAVKRN---HRGETLLHIA--SIKGDIP----------------SVEYLLQNGSDPNVKDHAGWTPLH 447
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNiknSDGENLLHLYleSNKIDLKilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLH 197

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 543583787 448 EACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVN 505
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 405-498 7.74e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.23  E-value: 7.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 484
Cdd:PHA02874 120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                         90
                 ....*....|....
gi 543583787 485 NGHVDIVKLLLSYG 498
Cdd:PHA02874 200 YGDYACIKLLIDHG 213
Ank_2 pfam12796
Ankyrin repeats (3 copies);
405-471 1.02e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.02e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543583787  405 RNHRGETLLHIASIKGDIPSVEYLLQNGsDPNVKDHaGWTPLHEACNHGHLKVVELLLQHKALVNTT 471
Cdd:pfam12796  26 QDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
411-462 1.36e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 65.76  E-value: 1.36e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 543583787  411 TLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLL 462
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
442-495 3.50e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 64.60  E-value: 3.50e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 543583787  442 GWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLL 495
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 412-497 2.20e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 70.31  E-value: 2.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 412 LLHIASiKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIV 491
Cdd:PTZ00322  86 LCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                 ....*.
gi 543583787 492 KLLLSY 497
Cdd:PTZ00322 165 QLLSRH 170
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 551-620 7.17e-12

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


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 61.22  E-value: 7.17e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 551 LVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGDAvqSTLKCMLGILNGCWILKFEWVKAC 620
Cdd:cd00027    1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPS--GEKYYLAALAWGIPIVSPEWLLDC 68
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 403-526 1.15e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 403 VKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDA 482
Cdd:PHA02878 162 MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 543583787 483 AKN-GHVDIVKLLLSYGASRNAVN-IFGLRPVDYTDDESMKSLLLL 526
Cdd:PHA02878 242 VGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSERKLKLLL 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
394-525 1.31e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.13  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 394 AMKLLPNMAVKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGY 473
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 543583787 474 QNDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIFGLRPVD---YTDDESMKSLLL 525
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHlaaYNGNLEIVKLLL 140
PHA03095 PHA03095
ankyrin-like protein; Provisional
 385-513 2.09e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 385 YRRVMSSPSA----MKLLPNMAVKRNHRGE---TLLHI---ASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLH-EACNHG 453
Cdd:PHA03095  16 YDYLLNASNVtveeVRRLLAAGADVNFRGEygkTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNAT 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543583787 454 HLKVVELLLQHKALVNTTGYQNDSPLHD--AAKNGHVDIVKLLLSYGASRNAVNIFGLRPVD 513
Cdd:PHA03095  96 TLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 417-515 5.36e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 5.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 417 SIKGDIpsVEYLLQNGSDPNVKD-HAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLL 495
Cdd:PHA02878 144 IIEAEI--TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL 221

                         90       100
                 ....*....|....*....|
gi 543583787 496 SYGASRNAVNIFGLRPVDYT 515
Cdd:PHA02878 222 ENGASTDARDKCGNTPLHIS 241
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 553-634 6.95e-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: 6.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 553 LIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGDA---VQSTLKCMLGILNGCWILKFEWVKACLRRKVCEQE 629
Cdd:cd17735    3 MVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAelvCERTLKYFLGIAGRKWVVSYQWITQSIKEGKILPE 82


                 ....*
gi 543583787 630 EKYEI 634
Cdd:cd17735   83 HDFEV 87
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 552-622 7.86e-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: 58.37  E-value: 7.86e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543583787 552 VLIGSGLSSEQQKMLSElaVILKAKKY---TEFDSTVTHVVVPGDAvqSTLKCMLGILNGCWILKFEWVKACLR 622
Cdd:cd17736    2 TLVMTSVHSEEQELLES--VVKKLGGFrveDSVTEKTTHVVVGSPR--RTLNVLLGIARGCWILSPDWVLESLE 71
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 411-516 1.38e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 411 TLLHIAS-----IKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEA-CNH-GHLKVVELLLQHKALVNTTGYQNDSPLHDAA 483
Cdd:PHA03100  70 TPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAiSKKsNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 543583787 484 KNGHVD--IVKLLLSYGASRNA---VNIFgLR---PVDYTD 516
Cdd:PHA03100 150 ESNKIDlkILKLLIDKGVDINAknrVNYL-LSygvPINIKD 189
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 404-514 1.56e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 404 KRNHRGETLLHIASIK--GDIPSVEYLLQNGSDPNVKDHAGWTPLHEA--CNHGHLKVVELLLQHKALVNttgyqndspl 479
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDIN---------- 170

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 543583787 480 hdaAKNGhvdiVKLLLSYGASRNAVNIFGLRPVDY 514
Cdd:PHA03100 171 ---AKNR----VNYLLSYGVPINIKDVYGFTPLHY 198
BRCT smart00292
breast cancer carboxy-terminal domain;
552-621 4.27e-10

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 56.61  E-value: 4.27e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543583787   552 VLIGSGLSSEQQKMLSELAVILKAKKYTEFDS-TVTHVVVpGDAVQSTLKCMLGILNGCWILKFEWVKACL 621
Cdd:smart00292   9 FYITGSFDKEERDELKELIEALGGKVTSSLSSkTTTHVIV-GSPEGGKLELLKAIALGIPIVKEEWLLDCL 78
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 413-512 4.30e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 4.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 413 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACnhGHLK---VVELLLQHKALVNTTGY-QNDSPLHDAAKNGhv 488
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdydILKLLLEHGVDVNAKSYiLGLTALHSSIKSE-- 280

                         90       100
                 ....*....|....*....|....
gi 543583787 489 DIVKLLLSYGASRNAVNIFGLRPV 512
Cdd:PHA02878 281 RKLKLLLEYGADINSLNSYKLTPL 304
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 408-511 1.19e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 408 RGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGH 487
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                         90       100
                 ....*....|....*....|....
gi 543583787 488 VDIVKLLLSYGASrnaVNIFGLRP 511
Cdd:PHA02875 181 IAICKMLLDSGAN---IDYFGKNG 201
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 393-524 5.17e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 5.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 393 SAMKLLPNMAVKR---NHRGETLLHIASIKGDIpsVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVN 469
Cdd:PHA02874  74 TAIKIGAHDIIKLlidNGVDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 543583787 470 TTGYQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIFGLRP----VDYTDDESMKSLL 524
Cdd:PHA02874 152 IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPlhnaAEYGDYACIKLLI 210
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 391-505 6.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 6.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 391 SPSAMKLLPNMAVK------RNHRGETLLHIASIKG-DIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLK-VVELLL 462
Cdd:PHA02876 283 APSLSRLVPKLLERgadvnaKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLL 362

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 543583787 463 QHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVN 505
Cdd:PHA02876 363 ELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
Ank_5 pfam13857
Ankyrin repeats (many copies);
461-514 2.27e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 2.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 543583787  461 LLQHK-ALVNTTGYQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIFGLRPVDY 514
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 405-513 4.42e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHlKVVELLLQHKAlVNTTGYQNDSPLHDAAK 484
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNAS-INDQDIDGSTPLHHAIN 263

                         90       100       110
                 ....*....|....*....|....*....|
gi 543583787 485 NG-HVDIVKLLLSYGASRNAVNIFGLRPVD 513
Cdd:PHA02874 264 PPcDIDIIDILLYHKADISIKDNKGENPID 293
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 411-504 4.49e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 411 TLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQND-SPLHDAAKNGHVD 489
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKID 216

                         90
                 ....*....|....*
gi 543583787 490 IVKLLLSYGASRNAV 504
Cdd:PHA02875 217 IVRLFIKRGADCNIM 231
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 421-499 5.07e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 5.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 421 DIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQN-DSPLHDAAKNGHVDIVKLLLSYGA 499
Cdd:PHA02875  47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGA 126
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 410-524 5.16e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 5.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 410 ETLLHIASIKGDIPSVEYLLQNGSDPN-VKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHV 488
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 543583787 489 DIVKLLLSYGASRNAVNIFGLRP----VDYTDDESMKSLL 524
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPliiaMAKGDIAICKMLL 188
Ank_2 pfam12796
Ankyrin repeats (3 copies);
397-439 3.19e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 3.19e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 543583787  397 LLPNMAVKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKD 439
Cdd:pfam12796  49 LLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
405-449 4.51e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 543583787  405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEA 449
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 405-464 7.97e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 7.97e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQH 464
Cdd:PTZ00322 111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA03095 PHA03095
ankyrin-like protein; Provisional
 422-514 8.14e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 8.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 422 IPSVEYLLQNGSDPNVKDHAGWTPLHeACNHG---HLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDI--VKLLLS 496
Cdd:PHA03095  97 LDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLID 175

                         90
                 ....*....|....*...
gi 543583787 497 YGASRNAVNIFGLRPVDY 514
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHH 193
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 412-502 1.02e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 412 LLHIASIkGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIV 491
Cdd:PLN03192 529 LLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF 607

                         90
                 ....*....|.
gi 543583787 492 KLLLSYGASRN 502
Cdd:PLN03192 608 RILYHFASISD 618
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 424-523 1.03e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 424 SVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHV-----DIVKLLLSYG 498
Cdd:PHA03100  17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYG 96

                         90       100
                 ....*....|....*....|....*
gi 543583787 499 ASRNAVNIFGLRPVDYTDDESMKSL 523
Cdd:PHA03100  97 ANVNAPDNNGITPLLYAISKKSNSY 121
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 442-469 1.31e-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: 1.31e-06
                           10        20
                   ....*....|....*....|....*...
gi 543583787   442 GWTPLHEACNHGHLKVVELLLQHKALVN 469
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 442-469 1.43e-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: 1.43e-06
                          10        20
                  ....*....|....*....|....*....
gi 543583787  442 GWTPLHEACNH-GHLKVVELLLQHKALVN 469
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 410-525 1.80e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 410 ETLLHIASIKGDIPS-----VEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAK 484
Cdd:PHA02876 141 ESIEYMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD 220

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 543583787 485 NGHVDIVKLLLSYGASRNAVNIFGLRPVDYTDDESmkSLLL 525
Cdd:PHA02876 221 SKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLET--SLLL 259
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 413-514 2.53e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 413 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHvDIVK 492
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIE 239

                         90       100
                 ....*....|....*....|..
gi 543583787 493 LLLSyGASRNAVNIFGLRPVDY 514
Cdd:PHA02874 240 LLIN-NASINDQDIDGSTPLHH 260
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 476-505 3.66e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 3.66e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 543583787  476 DSPLHDAA-KNGHVDIVKLLLSYGASRNAVN 505
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 410-500 3.71e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 410 ETLLHIASIKGDIPSVEYLLQNGS-DPNVKDHAGWTPLHEACNHGHLKVVELLLQH-KALVN--TTG--YQNDSPLHDAA 483
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNepMTSdlYQGETALHIAV 97

                         90
                 ....*....|....*..
gi 543583787 484 KNGHVDIVKLLLSYGAS 500
Cdd:cd22192   98 VNQNLNLVRELIARGAD 114
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 474-503 4.12e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 4.12e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 543583787   474 QNDSPLHDAAKNGHVDIVKLLLSYGASRNA 503
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 420-524 5.29e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 420 GDIPSVEYLLQN-GSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLLSYG 498
Cdd:PHA02874  12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                         90       100
                 ....*....|....*....|....*.
gi 543583787 499 ASRNAVnifglrPVDYTDDESMKSLL 524
Cdd:PHA02874  92 VDTSIL------PIPCIEKDMIKTIL 111
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 408-563 8.79e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 8.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 408 RGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVN------------------ 469
Cdd:PLN03192 557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDphaagdllctaakrndlt 636

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 470 ------TTGYQNDSPLHD-------AAKNGHVDIVKLLLSYGASRNAVNIFglrpvdytDDESMKSLLLLPEKNESSSA- 535
Cdd:PLN03192 637 amkellKQGLNVDSEDHQgatalqvAMAEDHVDMVRLLIMNGADVDKANTD--------DDFSPTELRELLQKRELGHSi 708

                        170       180       190
                 ....*....|....*....|....*....|..
gi 543583787 536 ----SHCSVMNTGQRRDGPLVLIGSGLSSEQQ 563
Cdd:PLN03192 709 tivdSVPADEPDLGRDGGSRPGRLQGTSSDNQ 740
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 409-508 9.21e-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: 49.24  E-value: 9.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 409 GETLLHIASIKGDIPSVEYLLQNGSD----PNVKD-HAGWTPLHEACNHGHLKVVELLLQHKALVNT---TG-------- 472
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPElvnePMTSDlYQGETALHIAVVNQNLNLVRELIARGADVVSpraTGtffrpgpk 130

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 543583787 473 ---YQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIFG 508
Cdd:cd22192  131 nliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
475-514 1.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 543583787  475 NDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIFGLRPVDY 514
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 405-512 1.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEA-CNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAA 483
Cdd:PHA02876 371 RDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYAC 450

                         90       100       110
                 ....*....|....*....|....*....|
gi 543583787 484 KNG-HVDIVKLLLSYGASRNAVNIFGLRPV 512
Cdd:PHA02876 451 KKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 442-470 1.88e-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: 1.88e-05
                          10        20
                  ....*....|....*....|....*....
gi 543583787  442 GWTPLHEACNHGHLKVVELLLQHKALVNT 470
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 409-527 2.30e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 409 GETLLHI----ASIKGDIpsVEYLLQNGSDPNVKDHAGWTPLH-----EACNhghLKVVELLLQHKALVNTTGYQNDSPL 479
Cdd:PHA03095 117 GRTPLHVylsgFNINPKV--IRLLLRKGADVNALDLYGMTPLAvllksRNAN---VELLRLLIDAGADVYAVDDRFRSLL 191

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 543583787 480 HDAAKNGHVD--IVKLLLSYGASRNAVNIFGLRPVDY-TDDESMKSLLLLP 527
Cdd:PHA03095 192 HHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSmATGSSCKRSLVLP 242
BRCT smart00292
breast cancer carboxy-terminal domain;
650-748 2.57e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 43.13  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787   650 PKLFDGCYFYLWGTFKHHPKDNLIKLVTAGGGQILSRKPKPDsdvtqtintvayharpdsdqrfcTQYIIYEDL--CNYH 727
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVGSPegGKLE 57

                           90       100
                   ....*....|....*....|.
gi 543583787   728 PERVRQGKVWKAPSSWFIDCV 748
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
Ank_5 pfam13857
Ankyrin repeats (many copies);
428-480 3.56e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 543583787  428 LLQNGS-DPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLH 480
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 416-504 5.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 5.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 416 ASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLL 495
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88


                 ....*....
gi 543583787 496 SYGASRNAV 504
Cdd:PHA02875  89 DLGKFADDV 97
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 408-440 5.77e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 5.77e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 543583787  408 RGETLLHIASIK-GDIPSVEYLLQNGSDPNVKDH 440
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
 418-521 7.43e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 7.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 418 IKG-DIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLH--DAAKNGHVDIVKLL 494
Cdd:PHA02946  47 IKGlDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLL 126

                         90       100
                 ....*....|....*....|....*...
gi 543583787 495 LSYGAS-RNAVNIFGLRPVDYTDDESMK 521
Cdd:PHA02946 127 VQYGAKiNNSVDEEGCGPLLACTDPSER 154
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 649-757 1.60e-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: 40.81  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787  649 LPKLFDGCYFYLwGTFKHHPKDNLIKLVTAGGGQIlsrkpkpdsdvTQTINTvayharpdsdqrfCTQYIIYEDLCNYHP 728
Cdd:pfam16589   1 LPNLFEPLRFYI-NAIPSPSRSKLKRLIEANGGTV-----------VDNINP-------------AVYIVIAPYNKTDKL 55

                          90       100
                  ....*....|....*....|....*....
gi 543583787  729 ERVRQGKVWKApsSWFIDCVMSFELLPLD 757
Cdd:pfam16589  56 AENTKLGVVSP--QWIFDCVKKGKLLPLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
479-511 1.62e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.25  E-value: 1.62e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 543583787  479 LHDAAKNGHVDIVKLLLSYGASRNAVNIFGLRP 511
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 556-621 1.64e-04

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


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 40.74  E-value: 1.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543583787  556 SGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGDavqsTLKCMLGILNGCWILKFEWVKACL 621
Cdd:pfam00533  14 TGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEAR----TKKYLKAKELGIPIVTEEWLLDCI 75
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 408-437 1.68e-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: 1.68e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 543583787  408 RGETLLHIASIKGDIPSVEYLLQNGSDPNV 437
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 556-622 2.62e-04

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: 39.86  E-value: 2.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543583787 556 SGLSSEQQKMLSELAVILKAK--KYTEFDSTVTHVVVpGDAVQSTlKCMLGILNGCWILKFEWVKACLR 622
Cdd:cd17738    7 SGFSEDEKKELISIIEKLGGKvlDSDEFDPKCTHLIC-GKPSRSE-KFLAACAAGKWILHPSYIEASAK 73
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 550-622 3.52e-04

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: 39.51  E-value: 3.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543583787 550 PLVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGdaVQSTLKCMLGILNGCWILKFEWVKACLR 622
Cdd:cd17741    2 PLVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMSK--IKVTVKVICALISGKPIVTPEYLDALLE 72
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 408-437 7.92e-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: 7.92e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 543583787   408 RGETLLHIASIKGDIPSVEYLLQNGSDPNV 437
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 413-578 1.24e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 413 LHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHL------------------------------------- 455
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKlgmkemirsinkcsvfytlvaikdafnnrnveifkii 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 456 ---------------------------KVVELLLQHKALVN-TTGYQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIF 507
Cdd:PHA02878 121 ltnrykniqtidlvyidkkskddiieaEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543583787 508 GLRPVDYTDDESMKSLLLLPEKNESSSASHCSVMNTgqrrdgPL-VLIGSGLSSEQQKMLSELAVILKAKKY 578
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT------PLhISVGYCKDYDILKLLLEHGVDVNAKSY 266
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 405-496 1.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 405 RNHRGETLLHIASIK-GDIPSVEYLLQNGSDPNVKDHA-GWTPLHEACNHGhlKVVELLLQHKALVNTTGYQNDSPLHDA 482
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307

                         90
                 ....*....|....*
gi 543583787 483 AKNGH-VDIVKLLLS 496
Cdd:PHA02878 308 VKQYLcINIGRILIS 322
PHA03095 PHA03095
ankyrin-like protein; Provisional
 405-462 1.86e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 543583787 405 RNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLL 462
Cdd:PHA03095 253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 566-627 2.68e-03

BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins; CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.


Pssm-ID: 349361 [Multi-domain]  Cd Length: 97  Bit Score: 37.90  E-value: 2.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543583787 566 LSELAVILKAKKYTEFDSTVTHVVVpgdAVQSTLKCMLGI-LNGCWILKFEWVKACLRR--KVCE 627
Cdd:cd17729   36 LWKLAESLGAKVVTDLSPRTTHLVA---AKLGTEKVKQALkMPGIHVVHPDWLWACAERweRVDE 97
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 477-503 3.37e-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: 35.70  E-value: 3.37e-03
                          10        20
                  ....*....|....*....|....*..
gi 543583787  477 SPLHDAAKNGHVDIVKLLLSYGASRNA 503
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 421-512 6.51e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.90  E-value: 6.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543583787 421 DIPSVEYLLQNGSDPNVKDHAGWTPLHEAC--NHGHLKVVELLLQHKALVNTTGYQNDSPLH------------DAAKNG 486
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYIlrHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnilDPETDN 375

                         90       100
                 ....*....|....*....|....*...
gi 543583787 487 HV--DIVKLLLSYGASRNAVNIFGLRPV 512
Cdd:PHA02716 376 DIrlDVIQCLISLGADITAVNCLGYTPL 403
PHA03095 PHA03095
ankyrin-like protein; Provisional
 455-514 9.48e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 9.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543583787 455 LKVVELLLQHKALVNTTGYQNDSPLHDAAKNGH---VDIVKLLLSYGASRNAVNIFGLRPVDY 514
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHL 89
 
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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