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Conserved domains on  [gi|755545204|ref|XP_011242758|]
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SMC5-SMC6 complex localization factor protein 1 isoform X7 [Mus musculus]

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; ...
 13-91 1.39e-46

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: 160.75  E-value: 1.39e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545204  13 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDE 91
Cdd:cd17750    3 KHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLDE 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
705-858 4.96e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 4.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 705 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 784
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545204 785 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 858
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 133-204 2.13e-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: 54.97  E-value: 2.13e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545204 133 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 204
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; ...
 13-91 1.39e-46

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: 160.75  E-value: 1.39e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545204  13 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDE 91
Cdd:cd17750    3 KHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLDE 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
705-858 4.96e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 4.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 705 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 784
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545204 785 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 858
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
717-804 2.18e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 2.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204  717 LHRVCIKNQVEKLIILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 796
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                  ....*...
gi 755545204  797 GKLLLQRG 804
Cdd:pfam12796  77 VKLLLEKG 84
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 133-204 2.13e-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: 54.97  E-value: 2.13e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545204 133 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 204
Cdd:cd17728    2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSppysLKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 704-805 6.36e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 6.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 704 MNFHKTNLKGETALHRV----CIKNQVEKLII--------------LLSLpGIDINVKDNAGWTPLHEACNYGNTECVQE 765
Cdd:PHA03100 132 ANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755545204 766 ILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQRGG 805
Cdd:PHA03100 211 LLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 723-805 2.73e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 723 KNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEvdLLTQV------DGVTPLHDALSNGHVEI 796
Cdd:cd22192   27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHIAVVNQNLNL 104


                 ....*....
gi 755545204 797 GKLLLQRGG 805
Cdd:cd22192  105 VRELIARGA 113
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 18-94 1.27e-05

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: 44.43  E-value: 1.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545204   18 MTGFKMEEK--EALVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDETTY 94
Cdd:pfam16770  13 LTGCERWIDkeDLDKKKLRLLGIKIV--QDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 747-775 6.72e-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: 37.95  E-value: 6.72e-04
                           10        20
                   ....*....|....*....|....*....
gi 755545204   747 GWTPLHEACNYGNTECVQEILQRCPEVDL 775
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
BRCT smart00292
breast cancer carboxy-terminal domain;
21-80 1.01e-03

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 38.90  E-value: 1.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545204    21 FKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERL-CKSEKFLAACAAGKWVLTKDYII 80
Cdd:smart00292  15 FDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPeGGKLELLKAIALGIPIVKEEWLL 75
 
Name Accession Description Interval E-value
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 13-91 1.39e-46

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: 160.75  E-value: 1.39e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545204  13 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDE 91
Cdd:cd17750    3 KHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLDE 81
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 13-86 4.29e-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: 108.04  E-value: 4.29e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755545204  13 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYK-NCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSG 86
Cdd:cd17738    1 KPVFLLSGFSEDEKKELISIIEKLGGKVLDSDEFDpKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
705-858 4.96e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 4.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 705 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 784
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545204 785 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 858
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
707-822 5.29e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 5.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 707 HKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLH 786
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLH 158

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755545204 787 DALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 822
Cdd:COG0666  159 LAAANGNLEIVKLLLEAGAD--VNARDNDGETPLHL 192
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
705-849 1.31e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 705 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 784
Cdd:COG0666  145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTA 222

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755545204 785 LHDALSNGHVEIGKLLLQRGGPELLQQRNSKGELPLDYVLSPKDKEELFAITNIDDTVDNFHAKT 849
Cdd:COG0666  223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
717-804 2.18e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 2.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204  717 LHRVCIKNQVEKLIILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 796
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                  ....*...
gi 755545204  797 GKLLLQRG 804
Cdd:pfam12796  77 VKLLLEKG 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
700-822 3.80e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.06  E-value: 3.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 700 LVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRcpEVDLLTQ- 778
Cdd:COG0666   40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARd 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755545204 779 VDGVTPLHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 822
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGAD--VNAQDNDGNTPLHL 159
BRCT_BRC1_like_rpt5 cd17743
fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 18-86 1.12e-11

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: 61.11  E-value: 1.12e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545204  18 MTGFKMEEKEaLVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSG 86
Cdd:cd17743    5 FTGYKLWTEK-EIKKLKKLGISIV--EDPDECTHLVAPKIVRTEKFLCALAYAPVIVTTDWLEACLKAG 70
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 15-82 6.28e-11

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


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 58.91  E-value: 6.28e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755545204  15 IIQMTGFKMEEKEALVKLLLKLDCTFIKSeKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHS 82
Cdd:cd00027    2 VICFSGLDDEEREELKKLIEALGGKVSES-LSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 133-204 2.13e-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: 54.97  E-value: 2.13e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545204 133 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 204
Cdd:cd17728    2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSppysLKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
705-775 5.18e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 5.18e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545204  705 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpgIDINVKDNaGWTPLHEACNYGNTECVQEILQRCPEVDL 775
Cdd:pfam12796  22 DANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 704-805 6.36e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 6.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 704 MNFHKTNLKGETALHRV----CIKNQVEKLII--------------LLSLpGIDINVKDNAGWTPLHEACNYGNTECVQE 765
Cdd:PHA03100 132 ANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755545204 766 ILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQRGG 805
Cdd:PHA03100 211 LLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
BRCT_PAXIP1_rpt5 cd17712
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 19-89 1.58e-06

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: 46.46  E-value: 1.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545204  19 TGFKMEEKEALVKLLLKLDCTFIKSEKykNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWL 89
Cdd:cd17712    7 TGFDPVQVRKLTKKVTILGGEVVESPQ--ECTHLVAPKVSRTVKFLTAISVCKHIVTPEWLEESFKQGKFL 75
Ank_4 pfam13637
Ankyrin repeats (many copies);
747-801 1.67e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755545204  747 GWTPLHEACNYGNTECVQEILQRCPEVDLlTQVDGVTPLHDALSNGHVEIGKLLL 801
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 723-805 2.73e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 723 KNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEvdLLTQV------DGVTPLHDALSNGHVEI 796
Cdd:cd22192   27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHIAVVNQNLNL 104


                 ....*....
gi 755545204 797 GKLLLQRGG 805
Cdd:cd22192  105 VRELIARGA 113
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 14-89 4.42e-06

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


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 45.27  E-value: 4.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545204  14 HIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWL 89
Cdd:cd17736    1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
Ank_4 pfam13637
Ankyrin repeats (many copies);
715-764 8.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 8.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 755545204  715 TALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQ 764
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLK 51
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 23-89 8.99e-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: 44.53  E-value: 8.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755545204  23 MEEKEALVKLLLKLDCTFIKSekYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWL 89
Cdd:cd17744    8 VSDKEEGEKIIKKLGGSVVDS--VEDCTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKANKFL 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
 709-803 1.03e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 709 TNLKGETALHRV-----CIKNQVEKLIIllslPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVT 783
Cdd:PHA03095 218 TDMLGNTPLHSMatgssCKRSLVLPLLI----AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNT 292

                         90       100
                 ....*....|....*....|
gi 755545204 784 PLHDALSNGHVEIGKLLLQR 803
Cdd:PHA03095 293 PLSLMVRNNNGRAVRAALAK 312
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 18-94 1.27e-05

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: 44.43  E-value: 1.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545204   18 MTGFKMEEK--EALVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDETTY 94
Cdd:pfam16770  13 LTGCERWIDkeDLDKKKLRLLGIKIV--QDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 720-826 2.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 720 VCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKL 799
Cdd:PHA02874 163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHNRSAIELL 241

                         90       100
                 ....*....|....*....|....*..
gi 755545204 800 LLQRGgpelLQQRNSKGELPLDYVLSP 826
Cdd:PHA02874 242 INNAS----INDQDIDGSTPLHHAINP 264
Ank_5 pfam13857
Ankyrin repeats (many copies);
766-823 5.42e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 5.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755545204  766 ILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQRGGPELLqqRNSKGELPLDYV 823
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL--KDEEGLTALDLA 56
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 15-86 7.08e-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: 42.14  E-value: 7.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545204  15 IIQMTGFKMEEKEALVKLLLKLDCTFIKSEKyKNCTHLIAERLcKSEKFLAACaagKW----VLTKDYIIHSAKSG 86
Cdd:cd17731    7 VICVTGFDSEERKEIQQLVEQNGGSYSPDLS-KNCTHLIAGSP-SGQKYEFAR---KWnsihIVTPEWLYDSIEAG 77
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 721-822 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 755545204 721 CIKNQVEKLIILlslPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLL 800
Cdd:PHA02874 101 CIEKDMIKTILD---CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLL 176

                         90       100
                 ....*....|....*....|..
gi 755545204 801 LQRGGpeLLQQRNSKGELPLDY 822
Cdd:PHA02874 177 LEKGA--YANVKDNNGESPLHN 196
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 24-79 1.90e-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: 40.66  E-value: 1.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755545204  24 EEKEALVKLLLKLDCTFIKsEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYI 79
Cdd:cd17741   13 EEKKKLKQIIAKLGGKVVN-EWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYL 67
Ank_5 pfam13857
Ankyrin repeats (many copies);
704-754 2.02e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755545204  704 MNFHKTNLKGETALHRVCIKNQVEKLIILLsLPGIDINVKDNAGWTPLHEA 754
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 708-804 2.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 708 KTNLKGETALHRVCiKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVdGVTPLHD 787
Cdd:PHA02878 163 KDRHKGNTALHYAT-ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKC-GNTPLHI 240

                         90
                 ....*....|....*...
gi 755545204 788 ALSN-GHVEIGKLLLQRG 804
Cdd:PHA02878 241 SVGYcKDYDILKLLLEHG 258
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 709-774 2.57e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 2.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545204 709 TNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVD 774
Cdd:PHA03100 188 KDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
700-822 2.71e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.17  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 700 LVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQv 779
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD- 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755545204 780 DGVTPLHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 822
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGAD--VNARDKDGETPLHL 126
Ank_5 pfam13857
Ankyrin repeats (many copies);
732-786 4.58e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 4.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755545204  732 LLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRcPEVDLLTQVDGVTPLH 786
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 731-801 5.76e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 5.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545204 731 ILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKLLL 801
Cdd:PTZ00322 100 ILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK-DGKTPLELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 747-775 6.72e-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: 37.95  E-value: 6.72e-04
                           10        20
                   ....*....|....*....|....*....
gi 755545204   747 GWTPLHEACNYGNTECVQEILQRCPEVDL 775
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 19-95 9.17e-04

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: 39.25  E-value: 9.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204  19 TGFKMEEKEALVKLLLKLDCTFiKSEKYKNCTHLI----AERLC-KSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDETT 93
Cdd:cd17735    6 SGLTPEELMLVQKFARKTGSTL-TSQFTEETTHVImktdAELVCeRTLKYFLGIAGRKWVVSYQWITQSIKEGKILPEHD 84


                 ..
gi 755545204  94 YE 95
Cdd:cd17735   85 FE 86
BRCT smart00292
breast cancer carboxy-terminal domain;
21-80 1.01e-03

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 38.90  E-value: 1.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545204    21 FKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERL-CKSEKFLAACAAGKWVLTKDYII 80
Cdd:smart00292  15 FDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPeGGKLELLKAIALGIPIVKEEWLL 75
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 19-89 1.06e-03

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: 38.74  E-value: 1.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545204  19 TGFKMEEKEALVKLLLKLDCTfIKSEKYKNCTHLIAE----RLCKSE-KFLAACAAGKWVLTKDYIIHSAKSGRWL 89
Cdd:cd17734    6 SGLSSEQKKLLEKLAQLLKAK-VVTEFSPEVTHVVVPaderGVCPRTmKYLMGILAGKWIVSFEWVEACLKAKKLV 80
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 725-840 1.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 725 QVEKLII--LLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQ 802
Cdd:PHA02876 154 QQDELLIaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIA-LDDLSVLECAVDSKNIDTIKAIID 232

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 755545204 803 RggpellQQRNSKGELPLDYVLSPKDKEEL-------FAITNIDD 840
Cdd:PHA02876 233 N------RSNINKNDLSLLKAIRNEDLETSlllydagFSVNSIDD 271
PHA03095 PHA03095
ankyrin-like protein; Provisional
 713-804 1.35e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 713 GETALHrVCIKNQVEKL--IILLSL-PGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCpEVDLLTQVD-GVTPLHDA 788
Cdd:PHA03095  47 GKTPLH-LYLHYSSEKVkdIVRLLLeAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA-GADVNAKDKvGRTPLHVY 124

                         90
                 ....*....|....*...
gi 755545204 789 LSNG--HVEIGKLLLQRG 804
Cdd:PHA03095 125 LSGFniNPKVIRLLLRKG 142
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 714-830 1.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 714 ETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGH 793
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD-IPNTDKFSPLHLAVMMGD 147

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755545204 794 VEIGKLLLQRGGpeLLQQRNSKGELPLDYVLSPKDKE 830
Cdd:PHA02875 148 IKGIELLIDHKA--CLDIEDCCGCTPLIIAMAKGDIA 182
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 737-802 2.30e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 2.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545204 737 GIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLLLQ 802
Cdd:PLN03192 548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH-IRDANGNTALWNAISAKHHKIFRILYH 612
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 747-777 2.60e-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: 36.11  E-value: 2.60e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 755545204  747 GWTPLHEAC-NYGNTECVQEILQRCPEVDLLT 777
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 747-774 2.88e-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: 36.08  E-value: 2.88e-03
                          10        20
                  ....*....|....*....|....*...
gi 755545204  747 GWTPLHEACNYGNTECVQEILQRCPEVD 774
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 729-804 6.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 6.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545204 729 LIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQRG 804
Cdd:PHA02875  50 AIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG 125
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 722-804 7.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 7.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 722 IKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNY--GNTECVQEILQRCPEVDLLTqVDGVTPLHDALSNGHV--EIG 797
Cdd:PHA03100  81 NLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKN-SDGENLLHLYLESNKIdlKIL 159


                 ....*..
gi 755545204 798 KLLLQRG 804
Cdd:PHA03100 160 KLLIDKG 166
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 715-804 9.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 9.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545204 715 TALHRVCIKNQVeKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVDGVTPLHDALSNGHV 794
Cdd:PHA02875 137 SPLHLAVMMGDI-KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKI 215

                         90
                 ....*....|
gi 755545204 795 EIGKLLLQRG 804
Cdd:PHA02875 216 DIVRLFIKRG 225
 
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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