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Conserved domains on  [gi|2499793868|ref|XP_055555881|]
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SMC5-SMC6 complex localization factor protein 1 isoform X1 [Falco cherrug]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 8-93 5.00e-40

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 cd17750:

Pssm-ID: 469589  Cd Length: 81  Bit Score: 142.26  E-value: 5.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868   8 GQKRIIQLTRFNKQEKRALRKWLLKLDCVFLDSKvlftkEYRNCTHLIAKKLCRSEKFLAACAAGKWILTKEYVINSAES 87
Cdd:cd17750     1 VQKHIIQLTGFKGEEKEALVKLLLKLDCVFIKSE-----KYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKS 75


                  ....*.
gi 2499793868  88 GRWLDE 93
Cdd:cd17750    76 GRWLDE 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
666-790 3.81e-21

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 666 YLLTKEVHFCKRNIKGETALHNACISNKVERLIQLLSSpGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLS 745
Cdd:COG0666    72 LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2499793868 746 QvDGVTPLHEALSNGHVEIGKLLLQHGGPVllQQRDSNGNLPLDY 790
Cdd:COG0666   151 N-DGNTPLHLAAANGNLEIVKLLLEAGADV--NARDNDGETPLHL 192
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 135-205 2.87e-04

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: 40.33  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 135 WKVVLSVkkGDKRMASITRVLEAGKATIC----SSENVEHNVTHIF---------SSLQTFPMQKRKCLSEvqyyplQYL 201
Cdd:cd17728     2 WKVLLVV--DIAKEDGFKRLLEAGGAKVIpsspPYSLKLKDATHAFvdltkdtsvDLISLLAKAGVPCLKP------EYI 73


                  ....
gi 2499793868 202 GDYL 205
Cdd:cd17728    74 AEYL 77
 
Name Accession Description Interval E-value
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 8-93 5.00e-40

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: 142.26  E-value: 5.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868   8 GQKRIIQLTRFNKQEKRALRKWLLKLDCVFLDSKvlftkEYRNCTHLIAKKLCRSEKFLAACAAGKWILTKEYVINSAES 87
Cdd:cd17750     1 VQKHIIQLTGFKGEEKEALVKLLLKLDCVFIKSE-----KYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKS 75


                  ....*.
gi 2499793868  88 GRWLDE 93
Cdd:cd17750    76 GRWLDE 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
666-790 3.81e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 666 YLLTKEVHFCKRNIKGETALHNACISNKVERLIQLLSSpGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLS 745
Cdd:COG0666    72 LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2499793868 746 QvDGVTPLHEALSNGHVEIGKLLLQHGGPVllQQRDSNGNLPLDY 790
Cdd:COG0666   151 N-DGNTPLHLAAANGNLEIVKLLLEAGADV--NARDNDGETPLHL 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
685-772 2.45e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 2.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 685 LHNACISNKVErLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQrcpEVDLLSQVDGVTPLHEALSNGHVEI 764
Cdd:pfam12796   1 LHLAAKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                  ....*...
gi 2499793868 765 GKLLLQHG 772
Cdd:pfam12796  77 VKLLLEKG 84
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 677-801 9.15e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 9.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 677 RNIKGETALHNACISNKVErLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVR-------EILQRCPE--------- 740
Cdd:PHA02874  153 EDDNGCYPIHIAIKHNFFD-IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKllidhgnHIMNKCKNgftplhnai 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 741 ------VDLL--------SQVDGVTPLHEALSNG-HVEIGKLLLQHGGPVLLqqRDSNGNLPLD----YVESVPVKQELL 801
Cdd:PHA02874  232 ihnrsaIELLinnasindQDIDGSTPLHHAINPPcDIDIIDILLYHKADISI--KDNKGENPIDtafkYINKDPVIKDII 309
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 17-96 2.52e-07

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: 49.44  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868  17 RFNKQEKRALRKwllkldcvfLDskVLFTKEYRNCTHLIAKKLCRSEKFLAACAAGKWILTKEYVINSAESGRWLDETTY 96
Cdd:pfam16770  21 DKEDLDKKKLRL---------LG--IKIVQDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 667-788 1.34e-05

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: 48.86  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 667 LLTKEVHFCKRNIKGETALHNACISNKVERLIQLLSSPGTDINV----QDYAGWTPLHEASYHGSTVCVREILQRCPEVD 742
Cdd:cd22192    37 LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVNQNLNLVRELIARGADVV 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2499793868 743 ---------LLSQVD----GVTPLHEALSNGHVEIGKLLLQHGGPvlLQQRDSNGNLPL 788
Cdd:cd22192   117 spratgtffRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLGNTVL 173
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 135-205 2.87e-04

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: 40.33  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 135 WKVVLSVkkGDKRMASITRVLEAGKATIC----SSENVEHNVTHIF---------SSLQTFPMQKRKCLSEvqyyplQYL 201
Cdd:cd17728     2 WKVLLVV--DIAKEDGFKRLLEAGGAKVIpsspPYSLKLKDATHAFvdltkdtsvDLISLLAKAGVPCLKP------EYI 73


                  ....
gi 2499793868 202 GDYL 205
Cdd:cd17728    74 AEYL 77
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 715-743 8.46e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 8.46e-03
                           10        20
                   ....*....|....*....|....*....
gi 2499793868  715 GWTPLHEASYHGSTVCVREILQRCPEVDL 743
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 8-93 5.00e-40

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: 142.26  E-value: 5.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868   8 GQKRIIQLTRFNKQEKRALRKWLLKLDCVFLDSKvlftkEYRNCTHLIAKKLCRSEKFLAACAAGKWILTKEYVINSAES 87
Cdd:cd17750     1 VQKHIIQLTGFKGEEKEALVKLLLKLDCVFIKSE-----KYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKS 75


                  ....*.
gi 2499793868  88 GRWLDE 93
Cdd:cd17750    76 GRWLDE 81
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 10-88 8.28e-27

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: 104.19  E-value: 8.28e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499793868  10 KRIIQLTRFNKQEKRALRKWLLKLDCVFLDSKVLftkeYRNCTHLIAKKLCRSEKFLAACAAGKWILTKEYVINSAESG 88
Cdd:cd17738     1 KPVFLLSGFSEDEKKELISIIEKLGGKVLDSDEF----DPKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
666-790 3.81e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 666 YLLTKEVHFCKRNIKGETALHNACISNKVERLIQLLSSpGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLS 745
Cdd:COG0666    72 LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2499793868 746 QvDGVTPLHEALSNGHVEIGKLLLQHGGPVllQQRDSNGNLPLDY 790
Cdd:COG0666   151 N-DGNTPLHLAAANGNLEIVKLLLEAGADV--NARDNDGETPLHL 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
685-772 2.45e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 2.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 685 LHNACISNKVErLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQrcpEVDLLSQVDGVTPLHEALSNGHVEI 764
Cdd:pfam12796   1 LHLAAKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                  ....*...
gi 2499793868 765 GKLLLQHG 772
Cdd:pfam12796  77 VKLLLEKG 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
666-788 3.77e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 3.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 666 YLLTKEVHFCKRNIKGETALHNACISNKVErLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLS 745
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLE-IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2499793868 746 QvDGVTPLHEALSNGHVEIGKLLLQHGGPVLLQQRDSNGNLPL 788
Cdd:COG0666   217 N-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
629-790 1.56e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.21  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 629 VKMLPDLPDLSKSLPLKQRLRAKAKVKVETAGAVENCYLLTKEVHFCKRNIKGETALHNACISNKVERLIQLLSSPGTDI 708
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 709 NVQDYAGWTPLHEASYHGSTVCVREILQRcpEVDLLSQ-VDGVTPLHEALSNGHVEIGKLLLQHGGPVLLQqrDSNGNLP 787
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ--DNDGNTP 156


                  ...
gi 2499793868 788 LDY 790
Cdd:COG0666   157 LHL 159
BRCT_BRC1_like_rpt5 cd17743
fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 14-88 2.15e-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: 60.34  E-value: 2.15e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499793868  14 QLTRFNKQEKRALRKwllkldcvfLDskVLFTKEYRNCTHLIAKKLCRSEKFLAACAAGKWILTKEYVINSAESG 88
Cdd:cd17743     7 GYKLWTEKEIKKLKK---------LG--ISIVEDPDECTHLVAPKIVRTEKFLCALAYAPVIVTTDWLEACLKAG 70
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 12-84 5.56e-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: 5.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499793868  12 IIQLTRFNKQEKRALRKWLLKLDCVFLDSKVlftkeyRNCTHLIAKKLCRSEKFLAACAAGKWILTKEYVINS 84
Cdd:cd00027     2 VICFSGLDDEEREELKKLIEALGGKVSESLS------SKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLDC 68
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
677-786 2.81e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.20  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 677 RNIKGETALHNACISNKVErLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLSQvDGVTPLHEA 756
Cdd:COG0666   182 RDNDGETPLHLAAENGHLE-IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK-DGLTALLLA 259

                          90       100       110
                  ....*....|....*....|....*....|
gi 2499793868 757 LSNGHVEIGKLLLQHGGPVLLQQRDSNGNL 786
Cdd:COG0666   260 AAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
666-743 8.47e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 8.47e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499793868 666 YLLTKEVHFCKRNIKGETALHNACISNKVERLIQLLSSPgtDINVQDYaGWTPLHEASYHGSTVCVREILQRCPEVDL 743
Cdd:pfam12796  15 LLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 677-801 9.15e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 9.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 677 RNIKGETALHNACISNKVErLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVR-------EILQRCPE--------- 740
Cdd:PHA02874  153 EDDNGCYPIHIAIKHNFFD-IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKllidhgnHIMNKCKNgftplhnai 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 741 ------VDLL--------SQVDGVTPLHEALSNG-HVEIGKLLLQHGGPVLLqqRDSNGNLPLD----YVESVPVKQELL 801
Cdd:PHA02874  232 ihnrsaIELLinnasindQDIDGSTPLHHAINPPcDIDIIDILLYHKADISI--KDNKGENPIDtafkYINKDPVIKDII 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
683-732 1.06e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 1.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2499793868 683 TALHNACISNKVErLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVR 732
Cdd:pfam13637   3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 17-96 2.52e-07

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: 49.44  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868  17 RFNKQEKRALRKwllkldcvfLDskVLFTKEYRNCTHLIAKKLCRSEKFLAACAAGKWILTKEYVINSAESGRWLDETTY 96
Cdd:pfam16770  21 DKEDLDKKKLRL---------LG--IKIVQDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 698-806 2.64e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 698 IQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLSQvDGVTPLHEALSNGHVEIGKLLLQHggpvll 777
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK-DGKTPLELAEENGFREVVQLLSRH------ 170

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2499793868 778 QQRDSNG--NLPLDYVESVPVKQEL--LNVVHP 806
Cdd:PTZ00322  171 SQCHFELgaNAKPDSFTGKPPSLEDspISSHHP 203
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 52-91 6.08e-07

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: 47.58  E-value: 6.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2499793868  52 THLIAKKLCRSEKFLAACAAGKWILTKEYVINSAESGRWL 91
Cdd:cd17736    37 THVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 680-775 1.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 680 KGETALHNACiSNKVERLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLSQVdGVTPLHEALSN 759
Cdd:PHA02878  167 KGNTALHYAT-ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKC-GNTPLHISVGY 244

                          90
                  ....*....|....*..
gi 2499793868 760 -GHVEIGKLLLQHGGPV 775
Cdd:PHA02878  245 cKDYDILKLLLEHGVDV 261
BRCT_PAXIP1_rpt5 cd17712
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 15-91 1.65e-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: 1.65e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499793868  15 LTRFNKQEKRALRKWLLKLDCVFLDSKvlftkeyRNCTHLIAKKLCRSEKFLAACAAGKWILTKEYVINSAESGRWL 91
Cdd:cd17712     6 FTGFDPVQVRKLTKKVTILGGEVVESP-------QECTHLVAPKVSRTVKFLTAISVCKHIVTPEWLEESFKQGKFL 75
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 687-773 1.66e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 687 NACisNKVERLIQLlsspGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLSqVDGVTPLHEALSNGHVEIGK 766
Cdd:PHA03100  170 NAK--NRVNYLLSY----GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEIFK 242


                  ....*..
gi 2499793868 767 LLLQHGG 773
Cdd:PHA03100  243 LLLNNGP 249
PHA03095 PHA03095
ankyrin-like protein; Provisional
 677-769 2.40e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 677 RNIKGETALHNACISNKVERLI--QLLSSpGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLSQvDGVTPLH 754
Cdd:PHA03095  218 TDMLGNTPLHSMATGSSCKRSLvlPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLS 295

                          90
                  ....*....|....*
gi 2499793868 755 EALSNGHVEIGKLLL 769
Cdd:PHA03095  296 LMVRNNNGRAVRAAL 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
715-769 8.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 8.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2499793868 715 GWTPLHEASYHGSTVCVREILQRCPEVDLLSqVDGVTPLHEALSNGHVEIGKLLL 769
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 672-802 9.15e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 9.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 672 VHFckRNIKGETALHN--ACISNKVERLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCpEVDLLSQVD- 748
Cdd:PHA03095   40 VNF--RGEYGKTPLHLylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA-GADVNAKDKv 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499793868 749 GVTPLHEALSNG--HVEIGKLLLQHGGPVllQQRDSNGNLPLD-YVESVPVKQELLN 802
Cdd:PHA03095  117 GRTPLHVYLSGFniNPKVIRLLLRKGADV--NALDLYGMTPLAvLLKSRNANVELLR 171
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 666-742 1.06e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 666 YLLTKEVHFCKRNIKGETALHNACISNKVE---RLIQLlsspGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVD 742
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEfvkYLLDL----GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 667-788 1.34e-05

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: 48.86  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 667 LLTKEVHFCKRNIKGETALHNACISNKVERLIQLLSSPGTDINV----QDYAGWTPLHEASYHGSTVCVREILQRCPEVD 742
Cdd:cd22192    37 LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVNQNLNLVRELIARGADVV 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2499793868 743 ---------LLSQVD----GVTPLHEALSNGHVEIGKLLLQHGGPvlLQQRDSNGNLPL 788
Cdd:cd22192   117 spratgtffRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLGNTVL 173
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 51-91 1.45e-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: 43.76  E-value: 1.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2499793868  51 CTHLIAKKLCRSEKFLAACAAGKWILTKEYVINSAESGRWL 91
Cdd:cd17744    32 CTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKANKFL 72
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 631-790 1.82e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 631 MLPDLPDLS---KSLPLKQRLRAKAKVKVETagavencyLLTKEVHFCKRNIKGETALH----NACISNKVERLIQLLSS 703
Cdd:PHA03100   23 MEDDLNDYSykkPVLPLYLAKEARNIDVVKI--------LLDNGADINSSTKNNSTPLHylsnIKYNLTDVKEIVKLLLE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 704 PGTDINVQDYAGWTPLHEASYH--GSTVCVREILQRCPEVDLLSqVDGVTPLHEALSNGHV--EIGKLLLQHGG------ 773
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKN-SDGENLLHLYLESNKIdlKILKLLIDKGVdinakn 173

                         170       180
                  ....*....|....*....|....*
gi 2499793868 774 --------PVLLQQRDSNGNLPLDY 790
Cdd:PHA03100  174 rvnyllsyGVPINIKDVYGFTPLHY 198
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 17-80 2.21e-05

BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage syndrome protein 1 (NBS1), or cell cycle regulatory protein p95, is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The BRCT (Breast Cancer Suppressor Protein BRCA1, carboxy-terminal) domain is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions within DNA strand breaks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is absent in this group.


Pssm-ID: 349372 [Multi-domain]  Cd Length: 74  Bit Score: 43.36  E-value: 2.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499793868  17 RFNKQEKRALRKWLLKLDCVFLdskvlftKEY-RNCTHLIAKKLCRSEKFLAACAAGKWILTKEY 80
Cdd:cd17741     9 CLDSEEKKKLKQIIAKLGGKVV-------NEWtEECTHLVMSKIKVTVKVICALISGKPIVTPEY 66
Ank_5 pfam13857
Ankyrin repeats (many copies);
734-791 4.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2499793868 734 ILQRCPEVDLLSQVDGVTPLHEALSNGHVEIGKLLLQHGGPVLLqqRDSNGNLPLDYV 791
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL--KDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 676-790 5.60e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 5.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 676 KRNIKGETALHNACISNKVERLIQLLSSPGTDINVQDYAGWTPLHeasYHGSTVCVREilqrcPEVDLL---------SQ 746
Cdd:PHA03095   78 APERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLH---VYLSGFNINP-----KVIRLLlrkgadvnaLD 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2499793868 747 VDGVTPLHEALSNGHVEIG--KLLLQHGGPVLlqQRDSNGNLPLDY 790
Cdd:PHA03095  150 LYGMTPLAVLLKSRNANVEllRLLIDAGADVY--AVDDRFRSLLHH 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 671-775 5.76e-05

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: 46.93  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 671 EVHFCKRNIKGETALHNACISNKVERLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPE---VDLLSQV 747
Cdd:cd22192     7 ELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnEPMTSDL 86

                          90       100
                  ....*....|....*....|....*....
gi 2499793868 748 -DGVTPLHEALSNGHVEIGKLLLQHGGPV 775
Cdd:cd22192    87 yQGETALHIAVVNQNLNLVRELIARGADV 115
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 682-793 6.68e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 6.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 682 ETALHNACISNKVERLIQLLSSpGTDINVQDYA-GWTPLHEASYHGSTVCVREILQRCPEVDLlSQVDGVTPLHEALSNG 760
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDL-GKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDI-PNTDKFSPLHLAVMMG 146

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2499793868 761 HVEIGKLLLQHGGPVLLQqrDSNGNLPLDYVES 793
Cdd:PHA02875  147 DIKGIELLIDHKACLDIE--DCCGCTPLIIAMA 177
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 677-788 8.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 8.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 677 RNIKGETALHNACISNKVErLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDlLSQVDGVTPLHEA 756
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLE-SIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNA 197

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2499793868 757 LSNGHVEIGKLLLQHGGPVLLQQRdsNGNLPL 788
Cdd:PHA02874  198 AEYGDYACIKLLIDHGNHIMNKCK--NGFTPL 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 683-790 2.39e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 683 TALHNACISNKVERLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLSQVDGvTPLHEAL--SNG 760
Cdd:PHA02876  343 TPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALcgTNP 421

                          90       100       110
                  ....*....|....*....|....*....|
gi 2499793868 761 HVEIgKLLLQHGGPVllQQRDSNGNLPLDY 790
Cdd:PHA02876  422 YMSV-KTLIDRGANV--NSKNKDLSTPLHY 448
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 135-205 2.87e-04

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: 40.33  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 135 WKVVLSVkkGDKRMASITRVLEAGKATIC----SSENVEHNVTHIF---------SSLQTFPMQKRKCLSEvqyyplQYL 201
Cdd:cd17728     2 WKVLLVV--DIAKEDGFKRLLEAGGAKVIpsspPYSLKLKDATHAFvdltkdtsvDLISLLAKAGVPCLKP------EYI 73


                  ....
gi 2499793868 202 GDYL 205
Cdd:cd17728    74 AEYL 77
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 16-97 3.18e-04

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 40.79  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868  16 TRFNKQEKRALRKWLLKLDCVFLDSkvlFTKeyrNCTHLIAKK----LC-RSEKFLAACAAGKWILTKEYVINSAESGRW 90
Cdd:cd17735     6 SGLTPEELMLVQKFARKTGSTLTSQ---FTE---ETTHVIMKTdaelVCeRTLKYFLGIAGRKWVVSYQWITQSIKEGKI 79


                  ....*..
gi 2499793868  91 LDETTYE 97
Cdd:cd17735    80 LPEHDFE 86
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 697-772 3.77e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 3.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499793868 697 LIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLSQVDGVTPLHEALSNGHVEIGKLLLQHG 772
Cdd:PHA02875   50 AIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG 125
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 680-772 7.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 680 KGETALHNACISNKVErLIQLLSSPGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDlLSQVDGVTPLHEALSN 759
Cdd:PHA02875  101 DGMTPLHLATILKKLD-IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD-IEDCCGCTPLIIAMAK 178

                          90
                  ....*....|...
gi 2499793868 760 GHVEIGKLLLQHG 772
Cdd:PHA02875  179 GDIAICKMLLDSG 191
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 719-792 1.40e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499793868 719 LHEASYHGSTVCVREILQ---RCPEVDLlsqvDGVTPLHEALSNGHVEIGKLLLQHGGPVLLQQRDsnGNLPLDYVE 792
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTggaDPNCRDY----DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD--GKTPLELAE 156
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 16-91 2.04e-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: 37.97  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868  16 TRFNKQEKRALRKwLLKLdcvfLDSKVlfTKEYRNC-THLIA-----KKLCRSEKFLAACAAGKWILTKEYVINSAESGR 89
Cdd:cd17734     6 SGLSSEQKKLLEK-LAQL----LKAKV--VTEFSPEvTHVVVpaderGVCPRTMKYLMGILAGKWIVSFEWVEACLKAKK 78


                  ..
gi 2499793868  90 WL 91
Cdd:cd17734    79 LV 80
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 748-778 2.10e-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: 36.50  E-value: 2.10e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2499793868 748 DGVTPLHEA-LSNGHVEIGKLLLQHGGPVLLQ 778
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNAR 32
PHA03095 PHA03095
ankyrin-like protein; Provisional
 677-744 2.16e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 2.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2499793868 677 RNIKGETALHNACISNK---VERLIQLlsspGTDINVQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLL 744
Cdd:PHA03095  253 RNRYGQTPLHYAAVFNNpraCRRLIAL----GADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 663-775 3.08e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 663 ENCYL-LTKevHFCKRNIK---GETALHNAcISNKVERLIQLL------SSPgtdinvqdYAGWTPLHEASYHGSTVCVR 732
Cdd:PLN03192  571 EDCVLvLLK--HACNVHIRdanGNTALWNA-ISAKHHKIFRILyhfasiSDP--------HAAGDLLCTAAKRNDLTAMK 639

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2499793868 733 EILQRCPEVDLLSQvDGVTPLHEALSNGHVEIGKLLLQHGGPV 775
Cdd:PLN03192  640 ELLKQGLNVDSEDH-QGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 638-788 3.40e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.02  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 638 LSKSLPLKQRLRAKAKVKVETAGAVencylltkevhfckrnikGETALH----------NACI------SNKVERLIQLL 701
Cdd:cd21882     1 LEELLGLLECLRWYLTDSAYQRGAT------------------GKTCLHkaalnlndgvNEAImllleaAPDSGNPKELV 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 702 SSPGTDinvQDYAGWTPLHEASYHGSTVCVREILQRCPEVDLLSQVD------------GVTPLHEALSNGHVEIGKLLL 769
Cdd:cd21882    63 NAPCTD---EFYQGQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLL 139

                         170       180
                  ....*....|....*....|
gi 2499793868 770 QHGG-PVLLQQRDSNGNLPL 788
Cdd:cd21882   140 ENGAqPAALEAQDSLGNTVL 159
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 748-772 3.97e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 3.97e-03
                          10        20
                  ....*....|....*....|....*
gi 2499793868 748 DGVTPLHEALSNGHVEIGKLLLQHG 772
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENG 25
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 667-775 5.96e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499793868 667 LLTKEVHFCKRNIKGETALHNACISNKVERLIQLLSSPGTDINVQDYAGWTPLHEAS----YHGSTVCVREILQRCPEVD 742
Cdd:PHA02876  293 LLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStldrNKDIVITLLELGANVNARD 372

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2499793868 743 LLSQvdgvTPLHEALSNGHVEIGKLLLQHGGPV 775
Cdd:PHA02876  373 YCDK----TPIHYAAVRNNVVIINTLLDYGADI 401
Ank_5 pfam13857
Ankyrin repeats (many copies);
677-722 7.11e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 7.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2499793868 677 RNIKGETALHNACISNKVErLIQLLSSPGTDINVQDYAGWTPLHEA 722
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALE-IVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 715-743 8.46e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 8.46e-03
                           10        20
                   ....*....|....*....|....*....
gi 2499793868  715 GWTPLHEASYHGSTVCVREILQRCPEVDL 743
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 748-773 1.00e-02

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: 34.49  E-value: 1.00e-02
                           10        20
                   ....*....|....*....|....*.
gi 2499793868  748 DGVTPLHEALSNGHVEIGKLLLQHGG 773
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
 
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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