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Conserved domains on  [gi|1370506663|ref|XP_024302003|]
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SMC5-SMC6 complex localization factor protein 1 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 5-85 9.85e-48

BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; SLF1, also termed Smc5/6 localization factor 1, or ankyrin repeat domain-containing protein 32 (ANKRD32), or BRCT domain-containing protein 1 (BRCTD1), plays a role in the DNA damage response (DDR) pathway by regulating post replication repair of UV-damaged DNA and genomic stability maintenance. It is a component of the SLF1-SLF2 complex that acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand break (DSB) sites on chromatin during DNA repair in response to stalled replication forks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


:

Pssm-ID: 349381  Cd Length: 81  Bit Score: 164.22  E-value: 9.85e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663    5 TPKHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLD 84
Cdd:cd17750      1 VQKHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLD 80


                   .
gi 1370506663   85 E 85
Cdd:cd17750     81 E 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
746-866 1.04e-21

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  746 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 825
Cdd:COG0666     76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DG 153

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1370506663  826 VTPLHDALSNGHVEIGKLLLQHGGPVllQQRNAKGELPLDY 866
Cdd:COG0666    154 NTPLHLAAANGNLEIVKLLLEAGADV--NARDNDGETPLHL 192
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 127-198 3.02e-09

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.


The actual alignment was detected with superfamily member cd17728:

Pssm-ID: 469589  Cd Length: 80  Bit Score: 54.58  E-value: 3.02e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506663  127 WKVVLLVRTDKRsDSLIRVLEAGKANVILPKS----SPSGITHVIASNARIKAEKEKDNFKAPFYP---IQYLGDFLLE 198
Cdd:cd17728      2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSPpyslKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
 
Name Accession Description Interval E-value
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 5-85 9.85e-48

BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; SLF1, also termed Smc5/6 localization factor 1, or ankyrin repeat domain-containing protein 32 (ANKRD32), or BRCT domain-containing protein 1 (BRCTD1), plays a role in the DNA damage response (DDR) pathway by regulating post replication repair of UV-damaged DNA and genomic stability maintenance. It is a component of the SLF1-SLF2 complex that acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand break (DSB) sites on chromatin during DNA repair in response to stalled replication forks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349381  Cd Length: 81  Bit Score: 164.22  E-value: 9.85e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663    5 TPKHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLD 84
Cdd:cd17750      1 VQKHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLD 80


                   .
gi 1370506663   85 E 85
Cdd:cd17750     81 E 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
746-866 1.04e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  746 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 825
Cdd:COG0666     76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DG 153

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1370506663  826 VTPLHDALSNGHVEIGKLLLQHGGPVllQQRNAKGELPLDY 866
Cdd:COG0666    154 NTPLHLAAANGNLEIVKLLLEAGADV--NARDNDGETPLHL 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
761-848 1.40e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.40e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  761 LHRACINNQVEKLILLLSlPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 840
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                   ....*...
gi 1370506663  841 GKLLLQHG 848
Cdd:pfam12796   77 VKLLLEKG 84
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 127-198 3.02e-09

eighth (C-terminal) 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 eighth BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.


Pssm-ID: 349360  Cd Length: 80  Bit Score: 54.58  E-value: 3.02e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506663  127 WKVVLLVRTDKRsDSLIRVLEAGKANVILPKS----SPSGITHVIASNARIKAEKEKDNFKAPFYP---IQYLGDFLLE 198
Cdd:cd17728      2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSPpyslKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 734-849 5.24e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 5.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  734 LSCSKENCPSVVKK-----MNFHKTNLKGETALHRA----CINNQVEKLIL--------------LLSLpGIDINVKDNA 790
Cdd:PHA03100   113 AISKKSNSYSIVEYlldngANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVY 191

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506663  791 GWTPLHEACNYGNTVCVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQHGG 849
Cdd:PHA03100   192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 12-88 5.01e-06

Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of regulator of Ty1 transposition protein 107 (RTT107). It is involved in binding phosphorylated histone H2A.


Pssm-ID: 465266  Cd Length: 91  Bit Score: 45.59  E-value: 5.01e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506663   12 MTGFKMEEK--EALVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLDETTY 88
Cdd:pfam16770   13 LTGCERWIDkeDLDKKKLRLLGIKIV--QDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 758-851 1.26e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  758 ETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEvdLLTQV------DGVTPLHD 831
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHI 95

                           90       100
                   ....*....|....*....|
gi 1370506663  832 ALSNGHVEIGKLLLQHGGPV 851
Cdd:cd22192     96 AVVNQNLNLVRELIARGADV 115
BRCT smart00292
breast cancer carboxy-terminal domain;
6-74 5.02e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 39.67  E-value: 5.02e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370506663     6 PKHIIQMTG-FKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERL-CKSEKFLAACAAGKWILTKDYII 74
Cdd:smart00292    5 KGKTFYITGsFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPeGGKLELLKAIALGIPIVKEEWLL 75
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 791-819 5.07e-03

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: 35.26  E-value: 5.07e-03
                            10        20
                    ....*....|....*....|....*....
gi 1370506663   791 GWTPLHEACNYGNTVCVQEILQRCPEVDL 819
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 5-85 9.85e-48

BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; SLF1, also termed Smc5/6 localization factor 1, or ankyrin repeat domain-containing protein 32 (ANKRD32), or BRCT domain-containing protein 1 (BRCTD1), plays a role in the DNA damage response (DDR) pathway by regulating post replication repair of UV-damaged DNA and genomic stability maintenance. It is a component of the SLF1-SLF2 complex that acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand break (DSB) sites on chromatin during DNA repair in response to stalled replication forks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349381  Cd Length: 81  Bit Score: 164.22  E-value: 9.85e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663    5 TPKHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLD 84
Cdd:cd17750      1 VQKHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLD 80


                   .
gi 1370506663   85 E 85
Cdd:cd17750     81 E 81
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 7-80 2.63e-28

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: 108.42  E-value: 2.63e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370506663    7 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYK-NCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSG 80
Cdd:cd17738      1 KPVFLLSGFSEDEKKELISIIEKLGGKVLDSDEFDpKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
746-866 1.04e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  746 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 825
Cdd:COG0666     76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DG 153

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1370506663  826 VTPLHDALSNGHVEIGKLLLQHGGPVllQQRNAKGELPLDY 866
Cdd:COG0666    154 NTPLHLAAANGNLEIVKLLLEAGADV--NARDNDGETPLHL 192
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
746-884 8.83e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 8.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  746 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 825
Cdd:COG0666    142 AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DG 219

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506663  826 VTPLHDALSNGHVEIGKLLLQHGGPVLLQQRNAKGELPLDYVVSPQIKEELFAITKIED 884
Cdd:COG0666    220 KTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
761-848 1.40e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.40e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  761 LHRACINNQVEKLILLLSlPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 840
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                   ....*...
gi 1370506663  841 GKLLLQHG 848
Cdd:pfam12796   77 VKLLLEKG 84
BRCT_BRC1_like_rpt5 cd17743
fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 12-80 4.30e-12

fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins; Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. The family also includes Cryptococcus neoformans DNA ligase 4 (LIG4, also known as DNA ligase IV or polydeoxyribonucleotide synthase [ATP] 4), which is involved in dsDNA break repair, and plays a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining. Members in this family contain six BRCT domains. This family corresponds to the fifth one.


Pssm-ID: 349374  Cd Length: 70  Bit Score: 62.26  E-value: 4.30e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506663   12 MTGFKMEEKEaLVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSG 80
Cdd:cd17743      5 FTGYKLWTEK-EIKKLKKLGISIV--EDPDECTHLVAPKIVRTEKFLCALAYAPVIVTTDWLEACLKAG 70
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 9-76 5.15e-11

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


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 59.30  E-value: 5.15e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370506663    9 IIQMTGFKMEEKEALVKLLLKLDCTFIKSeKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHS 76
Cdd:cd00027      2 VICFSGLDDEEREELKKLIEALGGKVSES-LSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLDC 68
Ank_2 pfam12796
Ankyrin repeats (3 copies);
736-819 1.26e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  736 CSKENCPSVVKKM-----NFHKTNLKGETALHRACINNQVEKLILLLSlpGIDINVKDNaGWTPLHEACNYGNTVCVQEI 810
Cdd:pfam12796    4 AAKNGNLELVKLLlengaDANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDN-GRTALHYAARSGHLEIVKLL 80


                   ....*....
gi 1370506663  811 LQRCPEVDL 819
Cdd:pfam12796   81 LEKGADINV 89
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 127-198 3.02e-09

eighth (C-terminal) 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 eighth BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.


Pssm-ID: 349360  Cd Length: 80  Bit Score: 54.58  E-value: 3.02e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506663  127 WKVVLLVRTDKRsDSLIRVLEAGKANVILPKS----SPSGITHVIASNARIKAEKEKDNFKAPFYP---IQYLGDFLLE 198
Cdd:cd17728      2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSPpyslKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 734-849 5.24e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 5.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  734 LSCSKENCPSVVKK-----MNFHKTNLKGETALHRA----CINNQVEKLIL--------------LLSLpGIDINVKDNA 790
Cdd:PHA03100   113 AISKKSNSYSIVEYlldngANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVY 191

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506663  791 GWTPLHEACNYGNTVCVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQHGG 849
Cdd:PHA03100   192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
BRCT_PAXIP1_rpt5 cd17712
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 13-83 6.65e-07

fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the fifth BRCT domain.


Pssm-ID: 349344  Cd Length: 75  Bit Score: 47.62  E-value: 6.65e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370506663   13 TGFKMEEKEALVKLLLKLDCTFIKSEKykNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWL 83
Cdd:cd17712      7 TGFDPVQVRKLTKKVTILGGEVVESPQ--ECTHLVAPKVSRTVKFLTAISVCKHIVTPEWLEESFKQGKFL 75
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 8-83 1.88e-06

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


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 46.43  E-value: 1.88e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506663    8 HIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWL 83
Cdd:cd17736      1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 17-83 3.20e-06

first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also termed nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The family corresponds to the first BRCT domain.


Pssm-ID: 349375 [Multi-domain]  Cd Length: 72  Bit Score: 45.69  E-value: 3.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370506663   17 MEEKEALVKLLLKLDCTFIKSekYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWL 83
Cdd:cd17744      8 VSDKEEGEKIIKKLGGSVVDS--VEDCTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKANKFL 72
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 12-88 5.01e-06

Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of regulator of Ty1 transposition protein 107 (RTT107). It is involved in binding phosphorylated histone H2A.


Pssm-ID: 465266  Cd Length: 91  Bit Score: 45.59  E-value: 5.01e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506663   12 MTGFKMEEK--EALVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLDETTY 88
Cdd:pfam16770   13 LTGCERWIDkeDLDKKKLRLLGIKIV--QDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 753-845 5.65e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 5.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  753 TNLKGETALHRA-----CINNQVEKLILllslPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDGVT 827
Cdd:PHA03095   218 TDMLGNTPLHSMatgssCKRSLVLPLLI----AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNT 292

                           90
                   ....*....|....*...
gi 1370506663  828 PLHDALSNGHVEIGKLLL 845
Cdd:PHA03095   293 PLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
746-868 1.38e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.03  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  746 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 825
Cdd:COG0666      9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GG 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1370506663  826 VTPLHDALSNGHVEIGKLLLQHGGPVLlqQRNAKGELPLDYVV 868
Cdd:COG0666     88 NTLLHAAARNGDLEIVKLLLEAGADVN--ARDKDGETPLHLAA 128
Ank_5 pfam13857
Ankyrin repeats (many copies);
748-798 1.42e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370506663  748 MNFHKTNLKGETALHRACINNQVEKLILLLsLPGIDINVKDNAGWTPLHEA 798
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 753-818 2.06e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 2.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506663  753 TNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVD 818
Cdd:PHA03100   188 KDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
759-808 2.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.25e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1370506663  759 TALHRACINNQVEkLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQ 808
Cdd:pfam13637    3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
Ank_5 pfam13857
Ankyrin repeats (many copies);
810-867 2.58e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370506663  810 ILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQHGGPVLLqqRNAKGELPLDYV 867
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL--KDEEGLTALDLA 56
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 18-73 3.25e-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: 42.97  E-value: 3.25e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506663   18 EEKEALVKLLLKLDCTFIKsEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYI 73
Cdd:cd17741     13 EEKKKLKQIIAKLGGKVVN-EWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYL 67
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 9-80 3.59e-05

second 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 second BRCT domain.


Pssm-ID: 349363 [Multi-domain]  Cd Length: 77  Bit Score: 42.91  E-value: 3.59e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506663    9 IIQMTGFKMEEKEALVKLLLKLDCTFIKSEKyKNCTHLIAERLcKSEKFLAACaagKW----ILTKDYIIHSAKSG 80
Cdd:cd17731      7 VICVTGFDSEERKEIQQLVEQNGGSYSPDLS-KNCTHLIAGSP-SGQKYEFAR---KWnsihIVTPEWLYDSIEAG 77
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 754-878 3.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 3.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  754 NLKGETALHRACINNQVEkLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQ-------EILQRCPE---------- 816
Cdd:PHA02874   154 DDNGCYPIHIAIKHNFFD-IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKllidhgnHIMNKCKNgftplhnaii 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  817 -----VDLL--------TQVDGVTPLHDALSNG-HVEIGKLLLQHGGPVLLqqRNAKGELPLD----YVVSPQIKEELFA 878
Cdd:PHA02874   233 hnrsaIELLinnasindQDIDGSTPLHHAINPPcDIDIIDILLYHKADISI--KDNKGENPIDtafkYINKDPVIKDIIA 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 752-851 3.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 3.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  752 KTNLKGETALHRACiNNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQVdGVTPLHD 831
Cdd:PHA02878   163 KDRHKGNTALHYAT-ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKC-GNTPLHI 240

                           90       100
                   ....*....|....*....|.
gi 1370506663  832 ALSN-GHVEIGKLLLQHGGPV 851
Cdd:PHA02878   241 SVGYcKDYDILKLLLEHGVDV 261
Ank_4 pfam13637
Ankyrin repeats (many copies);
791-845 5.95e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 5.95e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370506663  791 GWTPLHEACNYGNTVCVQEILQRCPEVDLlTQVDGVTPLHDALSNGHVEIGKLLL 845
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 734-848 6.48e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 6.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  734 LSCSKENCPSVVKKM-----NFHKTNLKGETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHeACNYGNTV--C 806
Cdd:PHA03095    55 LHYSSEKVKDIVRLLleagaDVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFNInpK 133

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1370506663  807 VQEILQRcPEVDL-LTQVDGVTPLHDALSNGHVEIG--KLLLQHG 848
Cdd:PHA03095   134 VIRLLLR-KGADVnALDLYGMTPLAVLLKSRNANVEllRLLIDAG 177
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 765-868 1.25e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  765 CINNQVEKLILLlslPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLL 844
Cdd:PHA02874   101 CIEKDMIKTILD---CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLL 176

                           90       100
                   ....*....|....*....|....
gi 1370506663  845 LQHGGpvLLQQRNAKGELPLDYVV 868
Cdd:PHA02874   177 LEKGA--YANVKDNNGESPLHNAA 198
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 758-851 1.26e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  758 ETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEvdLLTQV------DGVTPLHD 831
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHI 95

                           90       100
                   ....*....|....*....|
gi 1370506663  832 ALSNGHVEIGKLLLQHGGPV 851
Cdd:cd22192     96 AVVNQNLNLVRELIARGADV 115
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 775-847 2.11e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 2.11e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370506663  775 LLLSlPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKLLLQH 847
Cdd:PTZ00322   100 ILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK-DGKTPLELAEENGFREVVQLLSRH 170
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 13-83 4.61e-04

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: 39.89  E-value: 4.61e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506663   13 TGFKMEEKEALVKLLLKLDCTfIKSEKYKNCTHLIAE----RLCKSE-KFLAACAAGKWILTKDYIIHSAKSGRWL 83
Cdd:cd17734      6 SGLSSEQKKLLEKLAQLLKAK-VVTEFSPEVTHVVVPaderGVCPRTmKYLMGILAGKWIVSFEWVEACLKAKKLV 80
BRCT smart00292
breast cancer carboxy-terminal domain;
6-74 5.02e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 39.67  E-value: 5.02e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370506663     6 PKHIIQMTG-FKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERL-CKSEKFLAACAAGKWILTKDYII 74
Cdd:smart00292    5 KGKTFYITGsFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPeGGKLELLKAIALGIPIVKEEWLL 75
Ank_2 pfam12796
Ankyrin repeats (3 copies);
754-788 6.33e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.71  E-value: 6.33e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1370506663  754 NLKGETALHRACINNQVEKLILLLSLpGIDINVKD 788
Cdd:pfam12796   58 KDNGRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 754-864 7.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 7.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  754 NLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDlLTQVDGVTPLHDAL 833
Cdd:PHA02874   121 DAELKTFLHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAA 198

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1370506663  834 SNGHVEIGKLLLQHGGPVLLQQRNakGELPL 864
Cdd:PHA02874   199 EYGDYACIKLLIDHGNHIMNKCKN--GFTPL 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 758-869 9.67e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 9.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  758 ETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLlTQVDGVTPLHDALSNGH 837
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI-PNTDKFSPLHLAVMMGD 147

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1370506663  838 VEIGKLLLQHGGPVLLQqrNAKGELPLDYVVS 869
Cdd:PHA02875   148 IKGIELLIDHKACLDIE--DCCGCTPLIIAMA 177
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 13-89 1.98e-03

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: 38.48  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663   13 TGFKMEEKEALVKLLLKLDCTFiKSEKYKNCTHLI----AERLC-KSEKFLAACAAGKWILTKDYIIHSAKSGRWLDETT 87
Cdd:cd17735      6 SGLTPEELMLVQKFARKTGSTL-TSQFTEETTHVImktdAELVCeRTLKYFLGIAGRKWVVSYQWITQSIKEGKILPEHD 84


                   ..
gi 1370506663   88 YE 89
Cdd:cd17735     85 FE 86
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 41-85 2.62e-03

second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the second BRCT domain.


Pssm-ID: 349342 [Multi-domain]  Cd Length: 81  Bit Score: 37.60  E-value: 2.62e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1370506663   41 KNCTHLIAERlCKSEKFLAACAAGKW-ILTKDYIIHSAKSGRWLDE 85
Cdd:cd17710     37 KKCTHLVTGK-ASGAKYECALKHEGIkIVTPDWVTDCIKAKTLLDE 81
Ank_5 pfam13857
Ankyrin repeats (many copies);
776-830 2.99e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.99e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370506663  776 LLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRcPEVDLLTQVDGVTPLH 830
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 738-848 3.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  738 KENCPSVVKKM-----NFHKTNLKGETALHRACINNQVE----KLILLLSLPGIDINVKDNAGWTPLHEACNY--GNTVC 806
Cdd:PHA03100    44 EARNIDVVKILldngaDINSSTKNNSTPLHYLSNIKYNLtdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSI 123

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1370506663  807 VQEILQRCPEVDLLTqVDGVTPLHDALSNGHV--EIGKLLLQHG 848
Cdd:PHA03100   124 VEYLLDNGANVNIKN-SDGENLLHLYLESNKIdlKILKLLIDKG 166
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 770-848 3.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.74  E-value: 3.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506663  770 VEKLILLLSLPGIDiNVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQHG 848
Cdd:PHA02875    48 SEAIKLLMKHGAIP-DVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG 125
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 781-847 4.97e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 4.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370506663  781 GIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQH 847
Cdd:PHA02876   168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIA-LDDLSVLECAVDSKNIDTIKAIIDN 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 791-819 5.07e-03

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: 35.26  E-value: 5.07e-03
                            10        20
                    ....*....|....*....|....*....
gi 1370506663   791 GWTPLHEACNYGNTVCVQEILQRCPEVDL 819
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 751-820 5.21e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 5.21e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370506663  751 HKTNLKGETALHRA-CINNQV--EKLILLlslpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLL 820
Cdd:PHA03095   251 NARNRYGQTPLHYAaVFNNPRacRRLIAL----GADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 759-876 5.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 5.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  759 TALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQVDGvTPLHDAL--SNG 836
Cdd:PHA02876   343 TPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALcgTNP 421

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1370506663  837 HVEIgKLLLQHGGPVllQQRNAKGELPLDYVVSPQIKEEL 876
Cdd:PHA02876   422 YMSV-KTLIDRGANV--NSKNKDLSTPLHYACKKNCKLDV 458
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 756-848 6.19e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 6.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506663  756 KGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDlLTQVDGVTPLHDALSN 835
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIAR-GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD-IEDCCGCTPLIIAMAK 178

                           90
                   ....*....|...
gi 1370506663  836 GHVEIGKLLLQHG 848
Cdd:PHA02875   179 GDIAICKMLLDSG 191
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 824-854 6.40e-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. 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: 35.34  E-value: 6.40e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1370506663  824 DGVTPLHDA-LSNGHVEIGKLLLQHGGPVLLQ 854
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNAR 32
 
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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