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Conserved domains on  [gi|755545199|ref|XP_011242756|]
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SMC5-SMC6 complex localization factor protein 1 isoform X2 [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; ...
 7-85 2.27e-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: 2.27e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545199    7 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDE 85
Cdd:cd17750     3 KHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLDE 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
804-957 7.17e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 7.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  804 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 883
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545199  884 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 957
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 127-198 2.22e-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: 2.22e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545199  127 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 198
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSppysLKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
 
Name Accession Description Interval E-value
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 7-85 2.27e-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: 2.27e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545199    7 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDE 85
Cdd:cd17750     3 KHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLDE 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
804-957 7.17e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 7.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  804 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 883
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545199  884 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 957
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
816-903 2.13e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 2.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199   816 LHRVCIKNQVEKLIILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 895
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                   ....*...
gi 755545199   896 GKLLLQRG 903
Cdd:pfam12796   77 VKLLLEKG 84
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 127-198 2.22e-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: 2.22e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545199  127 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 198
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSppysLKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 803-904 1.30e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  803 MNFHKTNLKGETALHRV----CIKNQVEKLII--------------LLSLpGIDINVKDNAGWTPLHEACNYGNTECVQE 864
Cdd:PHA03100  132 ANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 755545199  865 ILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQRGG 904
Cdd:PHA03100  211 LLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 822-904 2.51e-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: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  822 KNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEvdLLTQV------DGVTPLHDALSNGHVEI 895
Cdd:cd22192    27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHIAVVNQNLNL 104


                  ....*....
gi 755545199  896 GKLLLQRGG 904
Cdd:cd22192   105 VRELIARGA 113
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 12-88 1.46e-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: 1.46e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545199    12 MTGFKMEEK--EALVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDETTY 88
Cdd:pfam16770   13 LTGCERWIDkeDLDKKKLRLLGIKIV--QDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 846-874 7.77e-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: 7.77e-04
                            10        20
                    ....*....|....*....|....*....
gi 755545199    846 GWTPLHEACNYGNTECVQEILQRCPEVDL 874
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
BRCT smart00292
breast cancer carboxy-terminal domain;
15-74 1.12e-03

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 38.90  E-value: 1.12e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545199     15 FKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERL-CKSEKFLAACAAGKWVLTKDYII 74
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; ...
 7-85 2.27e-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: 2.27e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545199    7 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDE 85
Cdd:cd17750     3 KHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLDE 81
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 7-80 4.47e-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: 4.47e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755545199    7 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYK-NCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSG 80
Cdd:cd17738     1 KPVFLLSGFSEDEKKELISIIEKLGGKVLDSDEFDpKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
804-957 7.17e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 7.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  804 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 883
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545199  884 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 957
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
806-921 7.35e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 7.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  806 HKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLH 885
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLH 158

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 755545199  886 DALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 921
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGAD--VNARDNDGETPLHL 192
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
804-948 1.77e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  804 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 883
Cdd:COG0666   145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTA 222

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755545199  884 LHDALSNGHVEIGKLLLQRGGPELLQQRNSKGELPLDYVLSPKDKEELFAITNIDDTVDNFHAKT 948
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
816-903 2.13e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 2.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199   816 LHRVCIKNQVEKLIILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 895
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                   ....*...
gi 755545199   896 GKLLLQRG 903
Cdd:pfam12796   77 VKLLLEKG 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
799-921 4.97e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.06  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  799 LVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRcpEVDLLTQ- 877
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARd 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 755545199  878 VDGVTPLHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 921
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGAD--VNAQDNDGNTPLHL 159
BRCT_BRC1_like_rpt5 cd17743
fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 12-80 1.17e-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: 1.17e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545199   12 MTGFKMEEKEaLVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSG 80
Cdd:cd17743     5 FTGYKLWTEK-EIKKLKKLGISIV--EDPDECTHLVAPKIVRTEKFLCALAYAPVIVTTDWLEACLKAG 70
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 9-76 6.81e-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: 6.81e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755545199    9 IIQMTGFKMEEKEALVKLLLKLDCTFIKSeKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHS 76
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 ...
 127-198 2.22e-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: 2.22e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545199  127 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 198
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSppysLKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
804-874 5.15e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 5.15e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545199   804 NFHKTNLKGETALHRVCIKNQVEKLIILLSlpGIDINVKDNaGWTPLHEACNYGNTECVQEILQRCPEVDL 874
Cdd:pfam12796   22 DANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 803-904 1.30e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  803 MNFHKTNLKGETALHRV----CIKNQVEKLII--------------LLSLpGIDINVKDNAGWTPLHEACNYGNTECVQE 864
Cdd:PHA03100  132 ANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 755545199  865 ILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQRGG 904
Cdd:PHA03100  211 LLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_4 pfam13637
Ankyrin repeats (many copies);
846-900 1.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755545199   846 GWTPLHEACNYGNTECVQEILQRCPEVDLlTQVDGVTPLHDALSNGHVEIGKLLL 900
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
BRCT_PAXIP1_rpt5 cd17712
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 13-83 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 755545199   13 TGFKMEEKEALVKLLLKLDCTFIKSEKykNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWL 83
Cdd:cd17712     7 TGFDPVQVRKLTKKVTILGGEVVESPQ--ECTHLVAPKVSRTVKFLTAISVCKHIVTPEWLEESFKQGKFL 75
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 822-904 2.51e-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: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  822 KNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEvdLLTQV------DGVTPLHDALSNGHVEI 895
Cdd:cd22192    27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHIAVVNQNLNL 104


                  ....*....
gi 755545199  896 GKLLLQRGG 904
Cdd:cd22192   105 VRELIARGA 113
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 8-83 5.13e-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: 5.13e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545199    8 HIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWL 83
Cdd:cd17736     1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
Ank_4 pfam13637
Ankyrin repeats (many copies);
814-863 8.13e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 8.13e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 755545199   814 TALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQ 863
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; ...
 17-83 1.00e-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: 44.53  E-value: 1.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755545199   17 MEEKEALVKLLLKLDCTFIKSekYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWL 83
Cdd:cd17744     8 VSDKEEGEKIIKKLGGSVVDS--VEDCTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKANKFL 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
 808-902 1.29e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  808 TNLKGETALHRV-----CIKNQVEKLIIllslPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVT 882
Cdd:PHA03095  218 TDMLGNTPLHSMatgssCKRSLVLPLLI----AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNT 292

                          90       100
                  ....*....|....*....|
gi 755545199  883 PLHDALSNGHVEIGKLLLQR 902
Cdd:PHA03095  293 PLSLMVRNNNGRAVRAALAK 312
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 12-88 1.46e-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: 1.46e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755545199    12 MTGFKMEEK--EALVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDETTY 88
Cdd:pfam16770   13 LTGCERWIDkeDLDKKKLRLLGIKIV--QDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 819-925 3.93e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  819 VCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKL 898
Cdd:PHA02874  163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHNRSAIELL 241

                          90       100
                  ....*....|....*....|....*..
gi 755545199  899 LLQRGgpelLQQRNSKGELPLDYVLSP 925
Cdd:PHA02874  242 INNAS----INDQDIDGSTPLHHAINP 264
Ank_5 pfam13857
Ankyrin repeats (many copies);
865-922 5.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 5.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 755545199   865 ILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQRGGPELLqqRNSKGELPLDYV 922
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; ...
 9-80 8.07e-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: 8.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545199    9 IIQMTGFKMEEKEALVKLLLKLDCTFIKSEKyKNCTHLIAERLcKSEKFLAACaagKW----VLTKDYIIHSAKSG 80
Cdd:cd17731     7 VICVTGFDSEERKEIQQLVEQNGGSYSPDLS-KNCTHLIAGSP-SGQKYEFAR---KWnsihIVTPEWLYDSIEAG 77
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 18-73 1.85e-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: 1.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755545199   18 EEKEALVKLLLKLDCTFIKsEKYKNCTHLIAERLCKSEKFLAACAAGKWVLTKDYI 73
Cdd:cd17741    13 EEKKKLKQIIAKLGGKVVN-EWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYL 67
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 820-921 1.86e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  820 CIKNQVEKLIILlslPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLL 899
Cdd:PHA02874  101 CIEKDMIKTILD---CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLL 176

                          90       100
                  ....*....|....*....|..
gi 755545199  900 LQRGGpeLLQQRNSKGELPLDY 921
Cdd:PHA02874  177 LEKGA--YANVKDNNGESPLHN 196
Ank_5 pfam13857
Ankyrin repeats (many copies);
803-853 2.00e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.00e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 755545199   803 MNFHKTNLKGETALHRVCIKNQVEKLIILLsLPGIDINVKDNAGWTPLHEA 853
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
799-921 3.38e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  799 LVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQv 878
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD- 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 755545199  879 DGVTPLHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 921
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGAD--VNARDKDGETPLHL 126
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 807-903 4.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  807 KTNLKGETALHRVCiKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVdGVTPLHD 886
Cdd:PHA02878  163 KDRHKGNTALHYAT-ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKC-GNTPLHI 240

                          90
                  ....*....|....*...
gi 755545199  887 ALSN-GHVEIGKLLLQRG 903
Cdd:PHA02878  241 SVGYcKDYDILKLLLEHG 258
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 808-873 4.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.27  E-value: 4.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545199  808 TNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVD 873
Cdd:PHA03100  188 KDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_5 pfam13857
Ankyrin repeats (many copies);
831-885 4.58e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.58e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755545199   831 LLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRcPEVDLLTQVDGVTPLH 885
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 830-900 6.48e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 6.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545199  830 ILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKLLL 900
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 ...
 846-874 7.77e-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: 7.77e-04
                            10        20
                    ....*....|....*....|....*....
gi 755545199    846 GWTPLHEACNYGNTECVQEILQRCPEVDL 874
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 13-83 1.05e-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: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545199   13 TGFKMEEKEALVKLLLKLDCTfIKSEKYKNCTHLIAE----RLCKSE-KFLAACAAGKWVLTKDYIIHSAKSGRWL 83
Cdd:cd17734     6 SGLSSEQKKLLEKLAQLLKAK-VVTEFSPEVTHVVVPaderGVCPRTmKYLMGILAGKWIVSFEWVEACLKAKKLV 80
BRCT smart00292
breast cancer carboxy-terminal domain;
15-74 1.12e-03

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 38.90  E-value: 1.12e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755545199     15 FKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERL-CKSEKFLAACAAGKWVLTKDYII 74
Cdd:smart00292   15 FDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPeGGKLELLKAIALGIPIVKEEWLL 75
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 13-89 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 755545199   13 TGFKMEEKEALVKLLLKLDCTFiKSEKYKNCTHLI----AERLC-KSEKFLAACAAGKWVLTKDYIIHSAKSGRWLDETT 87
Cdd:cd17735     6 SGLTPEELMLVQKFARKTGSTL-TSQFTEETTHVImktdAELVCeRTLKYFLGIAGRKWVVSYQWITQSIKEGKILPEHD 84


                  ..
gi 755545199   88 YE 89
Cdd:cd17735    85 FE 86
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 824-939 1.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  824 QVEKLII--LLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQ 901
Cdd:PHA02876  154 QQDELLIaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIA-LDDLSVLECAVDSKNIDTIKAIID 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755545199  902 RggpellQQRNSKGELPLDYVLSPKDKEEL-------FAITNIDD 939
Cdd:PHA02876  233 N------RSNINKNDLSLLKAIRNEDLETSlllydagFSVNSIDD 271
PHA03095 PHA03095
ankyrin-like protein; Provisional
 812-903 1.61e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  812 GETALHrVCIKNQVEKL--IILLSL-PGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCpEVDLLTQVD-GVTPLHDA 887
Cdd:PHA03095   47 GKTPLH-LYLHYSSEKVkdIVRLLLeAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA-GADVNAKDKvGRTPLHVY 124

                          90
                  ....*....|....*...
gi 755545199  888 LSNG--HVEIGKLLLQRG 903
Cdd:PHA03095  125 LSGFniNPKVIRLLLRKG 142
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 813-929 2.20e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545199  813 ETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGH 892
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD-IPNTDKFSPLHLAVMMGD 147

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 755545199  893 VEIGKLLLQRGGpeLLQQRNSKGELPLDYVLSPKDKE 929
Cdd:PHA02875  148 IKGIELLIDHKA--CLDIEDCCGCTPLIIAMAKGDIA 182
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 836-901 2.69e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 2.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545199  836 GIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLLLQ 901
Cdd:PLN03192  548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH-IRDANGNTALWNAISAKHHKIFRILYH 612
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 846-873 2.85e-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: 2.85e-03
                           10        20
                   ....*....|....*....|....*...
gi 755545199   846 GWTPLHEACNYGNTECVQEILQRCPEVD 873
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 846-876 3.07e-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: 3.07e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 755545199   846 GWTPLHEAC-NYGNTECVQEILQRCPEVDLLT 876
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 828-903 8.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 8.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755545199  828 LIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQRG 903
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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