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Conserved domains on  [gi|568982910|ref|XP_006517098|]
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SMC5-SMC6 complex localization factor protein 1 isoform X3 [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 2.62e-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: 160.37  E-value: 2.62e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568982910   13 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDE 91
Cdd:cd17750     3 KHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLDE 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
801-954 9.30e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 9.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  801 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 880
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982910  881 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 954
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 2.35e-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: 2.35e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568982910  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 2.62e-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: 160.37  E-value: 2.62e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568982910   13 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDE 91
Cdd:cd17750     3 KHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLDE 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
801-954 9.30e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 9.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  801 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 880
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982910  881 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 954
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
813-900 2.30e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 2.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910   813 LHRVCIKNQVEKLIILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 892
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                   ....*...
gi 568982910   893 GKLLLQRG 900
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 2.35e-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: 2.35e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568982910  133 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 204
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSppysLKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 800-901 1.46e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.06  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  800 MNFHKTNLKGETALHRV----CIKNQVEKLII--------------LLSLpGIDINVKDNAGWTPLHEACNYGNTECVQE 861
Cdd:PHA03100  132 ANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568982910  862 ILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQRGG 901
Cdd:PHA03100  211 LLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 819-901 2.48e-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: 51.55  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  819 KNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEvdLLTQV------DGVTPLHDALSNGHVEI 892
Cdd:cd22192    27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHIAVVNQNLNL 104


                  ....*....
gi 568982910  893 GKLLLQRGG 901
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 1.61e-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: 1.61e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568982910    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 ...
 843-871 8.22e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 8.22e-04
                            10        20
                    ....*....|....*....|....*....
gi 568982910    843 GWTPLHEACNYGNTECVQEILQRCPEVDL 871
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
BRCT smart00292
breast cancer carboxy-terminal domain;
21-80 1.14e-03

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 38.90  E-value: 1.14e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568982910     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 2.62e-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: 160.37  E-value: 2.62e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568982910   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 4.63e-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: 108.04  E-value: 4.63e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568982910   13 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYK-NCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSG 86
Cdd:cd17738     1 KPVFLLSGFSEDEKKELISIIEKLGGKVLDSDEFDpKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
801-954 9.30e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 9.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  801 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 880
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982910  881 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 954
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
803-918 9.26e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.78  E-value: 9.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  803 HKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLH 882
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLH 158

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568982910  883 DALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 918
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGAD--VNARDNDGETPLHL 192
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
801-945 2.29e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  801 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 880
Cdd:COG0666   145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTA 222

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568982910  881 LHDALSNGHVEIGKLLLQRGGPELLQQRNSKGELPLDYVLSPKDKEELFAITNIDDTVDNFHAKT 945
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
813-900 2.30e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 2.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910   813 LHRVCIKNQVEKLIILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 892
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                   ....*...
gi 568982910   893 GKLLLQRG 900
Cdd:pfam12796   77 VKLLLEKG 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
796-918 6.12e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 6.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  796 LVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRcpEVDLLTQ- 874
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARd 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568982910  875 VDGVTPLHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 918
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 1.25e-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: 1.25e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568982910   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 7.13e-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: 7.13e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568982910   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 2.35e-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: 2.35e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568982910  133 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 204
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSppysLKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
801-871 5.55e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 5.55e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568982910   801 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpgIDINVKDNaGWTPLHEACNYGNTECVQEILQRCPEVDL 871
Cdd:pfam12796   22 DANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 800-901 1.46e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.06  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  800 MNFHKTNLKGETALHRV----CIKNQVEKLII--------------LLSLpGIDINVKDNAGWTPLHEACNYGNTECVQE 861
Cdd:PHA03100  132 ANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568982910  862 ILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQRGG 901
Cdd:PHA03100  211 LLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_4 pfam13637
Ankyrin repeats (many copies);
843-897 1.54e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.54e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568982910   843 GWTPLHEACNYGNTECVQEILQRCPEVDLlTQVDGVTPLHDALSNGHVEIGKLLL 897
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
BRCT_PAXIP1_rpt5 cd17712
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 19-89 1.66e-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: 1.66e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568982910   19 TGFKMEEKEALVKLLLKLDCTFIKSEKykNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWL 89
Cdd:cd17712     7 TGFDPVQVRKLTKKVTILGGEVVESPQ--ECTHLVAPKVSRTVKFLTAISVCKHIVTPEWLEESFKQGKFL 75
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 819-901 2.48e-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: 51.55  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  819 KNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEvdLLTQV------DGVTPLHDALSNGHVEI 892
Cdd:cd22192    27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHIAVVNQNLNL 104


                  ....*....
gi 568982910  893 GKLLLQRGG 901
Cdd:cd22192   105 VRELIARGA 113
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 14-89 5.07e-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: 5.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982910   14 HIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWL 89
Cdd:cd17736     1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
Ank_4 pfam13637
Ankyrin repeats (many copies);
811-860 8.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 8.35e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568982910   811 TALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQ 860
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 1.07e-05

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: 44.15  E-value: 1.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568982910   23 MEEKEALVKLLLKLDCTFIKSekYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWL 89
Cdd:cd17744     8 VSDKEEGEKIIKKLGGSVVDS--VEDCTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKANKFL 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
 805-899 1.35e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  805 TNLKGETALHRV-----CIKNQVEKLIIllslPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVT 879
Cdd:PHA03095  218 TDMLGNTPLHSMatgssCKRSLVLPLLI----AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNT 292

                          90       100
                  ....*....|....*....|
gi 568982910  880 PLHDALSNGHVEIGKLLLQR 899
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 1.61e-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: 1.61e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568982910    18 MTGFKMEEK--EALVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDETTY 94
Cdd:pfam16770   13 LTGCERWIDkeDLDKKKLRLLGIKIV--QDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 816-922 3.99e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  816 VCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKL 895
Cdd:PHA02874  163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHNRSAIELL 241

                          90       100
                  ....*....|....*....|....*..
gi 568982910  896 LLQRGgpelLQQRNSKGELPLDYVLSP 922
Cdd:PHA02874  242 INNAS----INDQDIDGSTPLHHAINP 264
Ank_5 pfam13857
Ankyrin repeats (many copies);
862-919 5.79e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 5.79e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568982910   862 ILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQRGGPELLqqRNSKGELPLDYV 919
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 8.12e-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: 41.76  E-value: 8.12e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982910   15 IIQMTGFKMEEKEALVKLLLKLDCTFIKSEKyKNCTHLIAERLcKSEKFLAACaagKW----VLTKDYIIHSAKSG 86
Cdd:cd17731     7 VICVTGFDSEERKEIQQLVEQNGGSYSPDLS-KNCTHLIAGSP-SGQKYEFAR---KWnsihIVTPEWLYDSIEAG 77
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 24-79 1.87e-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: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568982910   24 EEKEALVKLLLKLDCTFIKsEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYI 79
Cdd:cd17741    13 EEKKKLKQIIAKLGGKVVN-EWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYL 67
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 817-918 1.97e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  817 CIKNQVEKLIILlslPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLL 896
Cdd:PHA02874  101 CIEKDMIKTILD---CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLL 176

                          90       100
                  ....*....|....*....|..
gi 568982910  897 LQRGGpeLLQQRNSKGELPLDY 918
Cdd:PHA02874  177 LEKGA--YANVKDNNGESPLHN 196
Ank_5 pfam13857
Ankyrin repeats (many copies);
800-850 2.23e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568982910   800 MNFHKTNLKGETALHRVCIKNQVEKLIILLsLPGIDINVKDNAGWTPLHEA 850
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
796-918 3.78e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  796 LVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQv 875
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD- 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568982910  876 DGVTPLHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 918
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGAD--VNARDKDGETPLHL 126
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 804-900 4.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  804 KTNLKGETALHRVCiKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVdGVTPLHD 883
Cdd:PHA02878  163 KDRHKGNTALHYAT-ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKC-GNTPLHI 240

                          90
                  ....*....|....*...
gi 568982910  884 ALSN-GHVEIGKLLLQRG 900
Cdd:PHA02878  241 SVGYcKDYDILKLLLEHG 258
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 805-870 4.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 4.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982910  805 TNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVD 870
Cdd:PHA03100  188 KDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_5 pfam13857
Ankyrin repeats (many copies);
828-882 4.94e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.94e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568982910   828 LLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRcPEVDLLTQVDGVTPLH 882
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 827-897 6.45e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 6.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568982910  827 ILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKLLL 897
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 ...
 843-871 8.22e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 8.22e-04
                            10        20
                    ....*....|....*....|....*....
gi 568982910    843 GWTPLHEACNYGNTECVQEILQRCPEVDL 871
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 19-89 1.03e-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: 1.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982910   19 TGFKMEEKEALVKLLLKLDCTfIKSEKYKNCTHLIAE----RLCKSE-KFLAACAAGKWVLTKDYIIHSAKSGRWL 89
Cdd:cd17734     6 SGLSSEQKKLLEKLAQLLKAK-VVTEFSPEVTHVVVPaderGVCPRTmKYLMGILAGKWIVSFEWVEACLKAKKLV 80
BRCT smart00292
breast cancer carboxy-terminal domain;
21-80 1.14e-03

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 38.90  E-value: 1.14e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568982910     21 FKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERL-CKSEKFLAACAAGKWVLTKDYII 80
Cdd:smart00292   15 FDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPeGGKLELLKAIALGIPIVKEEWLL 75
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 19-95 1.14e-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: 39.25  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910   19 TGFKMEEKEALVKLLLKLDCTFiKSEKYKNCTHLI----AERLC-KSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDETT 93
Cdd:cd17735     6 SGLTPEELMLVQKFARKTGSTL-TSQFTEETTHVImktdAELVCeRTLKYFLGIAGRKWVVSYQWITQSIKEGKILPEHD 84


                  ..
gi 568982910   94 YE 95
Cdd:cd17735    85 FE 86
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 821-936 1.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  821 QVEKLII--LLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQ 898
Cdd:PHA02876  154 QQDELLIaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIA-LDDLSVLECAVDSKNIDTIKAIID 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568982910  899 RggpellQQRNSKGELPLDYVLSPKDKEEL-------FAITNIDD 936
Cdd:PHA02876  233 N------RSNINKNDLSLLKAIRNEDLETSlllydagFSVNSIDD 271
PHA03095 PHA03095
ankyrin-like protein; Provisional
 809-900 1.81e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  809 GETALHrVCIKNQVEKL--IILLSL-PGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCpEVDLLTQVD-GVTPLHDA 884
Cdd:PHA03095   47 GKTPLH-LYLHYSSEKVkdIVRLLLeAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA-GADVNAKDKvGRTPLHVY 124

                          90
                  ....*....|....*...
gi 568982910  885 LSNG--HVEIGKLLLQRG 900
Cdd:PHA03095  125 LSGFniNPKVIRLLLRKG 142
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 810-926 2.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982910  810 ETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGH 889
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD-IPNTDKFSPLHLAVMMGD 147

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568982910  890 VEIGKLLLQRGGpeLLQQRNSKGELPLDYVLSPKDKE 926
Cdd:PHA02875  148 IKGIELLIDHKA--CLDIEDCCGCTPLIIAMAKGDIA 182
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 833-898 2.66e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 2.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982910  833 GIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLLLQ 898
Cdd:PLN03192  548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH-IRDANGNTALWNAISAKHHKIFRILYH 612
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 843-870 2.96e-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: 2.96e-03
                           10        20
                   ....*....|....*....|....*...
gi 568982910   843 GWTPLHEACNYGNTECVQEILQRCPEVD 870
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 843-873 3.21e-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: 3.21e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 568982910   843 GWTPLHEAC-NYGNTECVQEILQRCPEVDLLT 873
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 825-900 8.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 8.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982910  825 LIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQRG 900
Cdd:PHA02875   50 AIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG 125
 
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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