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Conserved domains on  [gi|1039742992|ref|XP_017170841|]
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SMC5-SMC6 complex localization factor protein 1 isoform X8 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
701-854 7.00e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 7.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 701 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 780
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039742992 781 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 854
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 24-95 1.60e-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: 55.35  E-value: 1.60e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039742992  24 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 95
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSppysLKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
701-854 7.00e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 7.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 701 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 780
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039742992 781 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 854
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
713-800 1.92e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 713 LHRVCIKNQVEKLIILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 792
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                  ....*...
gi 1039742992 793 GKLLLQRG 800
Cdd:pfam12796  77 VKLLLEKG 84
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 24-95 1.60e-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: 55.35  E-value: 1.60e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039742992  24 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 95
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSppysLKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 700-801 1.10e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 700 MNFHKTNLKGETALHRV----CIKNQVEKLII--------------LLSLpGIDINVKDNAGWTPLHEACNYGNTECVQE 761
Cdd:PHA03100  132 ANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039742992 762 ILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQRGG 801
Cdd:PHA03100  211 LLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 719-801 2.33e-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: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 719 KNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEvdLLTQV------DGVTPLHDALSNGHVEI 792
Cdd:cd22192    27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHIAVVNQNLNL 104


                  ....*....
gi 1039742992 793 GKLLLQRGG 801
Cdd:cd22192   105 VRELIARGA 113
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 743-771 7.17e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 7.17e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039742992  743 GWTPLHEACNYGNTECVQEILQRCPEVDL 771
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
701-854 7.00e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 7.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 701 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 780
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039742992 781 LHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDYVLSPKDKE--ELFAITNIDDTVDNFHAKTQKHFYHQQL 854
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAD--VNAKDNDGKTALDLAAENGNLEivKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
703-818 7.17e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 7.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 703 HKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLH 782
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLH 158

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039742992 783 DALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 818
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGAD--VNARDNDGETPLHL 192
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
701-845 1.69e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 701 NFHKTNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTP 780
Cdd:COG0666   145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTA 222

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039742992 781 LHDALSNGHVEIGKLLLQRGGPELLQQRNSKGELPLDYVLSPKDKEELFAITNIDDTVDNFHAKT 845
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
713-800 1.92e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 713 LHRVCIKNQVEKLIILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 792
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                  ....*...
gi 1039742992 793 GKLLLQRG 800
Cdd:pfam12796  77 VKLLLEKG 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
696-818 4.72e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 4.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 696 LVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRcpEVDLLTQ- 774
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARd 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039742992 775 VDGVTPLHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 818
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGAD--VNAQDNDGNTPLHL 159
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 24-95 1.60e-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: 55.35  E-value: 1.60e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039742992  24 WKVVLLVRADKRsDSLVRVLEAGKANVILPK----NSPSGITHVIASNARISAEREQENFKAPFYP---IQYLGDFLLE 95
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSppysLKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
701-771 4.63e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 4.63e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039742992 701 NFHKTNLKGETALHRVCIKNQVEKLIILLSlpGIDINVKDNaGWTPLHEACNYGNTECVQEILQRCPEVDL 771
Cdd:pfam12796  22 DANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 700-801 1.10e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 700 MNFHKTNLKGETALHRV----CIKNQVEKLII--------------LLSLpGIDINVKDNAGWTPLHEACNYGNTECVQE 761
Cdd:PHA03100  132 ANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039742992 762 ILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQRGG 801
Cdd:PHA03100  211 LLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_4 pfam13637
Ankyrin repeats (many copies);
743-797 1.33e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039742992 743 GWTPLHEACNYGNTECVQEILQRCPEVDLlTQVDGVTPLHDALSNGHVEIGKLLL 797
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 719-801 2.33e-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: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 719 KNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEvdLLTQV------DGVTPLHDALSNGHVEI 792
Cdd:cd22192    27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHIAVVNQNLNL 104


                  ....*....
gi 1039742992 793 GKLLLQRGG 801
Cdd:cd22192   105 VRELIARGA 113
Ank_4 pfam13637
Ankyrin repeats (many copies);
711-760 6.98e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 6.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039742992 711 TALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQ 760
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLK 51
PHA03095 PHA03095
ankyrin-like protein; Provisional
 705-799 1.24e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 705 TNLKGETALHRV-----CIKNQVEKLIIllslPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVT 779
Cdd:PHA03095  218 TDMLGNTPLHSMatgssCKRSLVLPLLI----AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNT 292

                          90       100
                  ....*....|....*....|
gi 1039742992 780 PLHDALSNGHVEIGKLLLQR 799
Cdd:PHA03095  293 PLSLMVRNNNGRAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 716-822 3.86e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 716 VCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKL 795
Cdd:PHA02874  163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHNRSAIELL 241

                          90       100
                  ....*....|....*....|....*..
gi 1039742992 796 LLQRGgpelLQQRNSKGELPLDYVLSP 822
Cdd:PHA02874  242 INNAS----INDQDIDGSTPLHHAINP 264
Ank_5 pfam13857
Ankyrin repeats (many copies);
762-819 5.67e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 5.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039742992 762 ILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQRGGPELLqqRNSKGELPLDYV 819
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL--KDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 717-818 1.88e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 717 CIKNQVEKLIILlslPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLL 796
Cdd:PHA02874  101 CIEKDMIKTILD---CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLL 176

                          90       100
                  ....*....|....*....|..
gi 1039742992 797 LQRGGpeLLQQRNSKGELPLDY 818
Cdd:PHA02874  177 LEKGA--YANVKDNNGESPLHN 196
Ank_5 pfam13857
Ankyrin repeats (many copies);
700-750 2.20e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039742992 700 MNFHKTNLKGETALHRVCIKNQVEKLIILLsLPGIDINVKDNAGWTPLHEA 750
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
696-818 3.16e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 696 LVTKMNFHKTNLKGETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQv 775
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD- 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039742992 776 DGVTPLHDALSNGHVEIGKLLLQRGGPelLQQRNSKGELPLDY 818
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGAD--VNARDKDGETPLHL 126
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 704-800 3.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 704 KTNLKGETALHRVCiKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQVdGVTPLHD 783
Cdd:PHA02878  163 KDRHKGNTALHYAT-ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKC-GNTPLHI 240

                          90
                  ....*....|....*...
gi 1039742992 784 ALSN-GHVEIGKLLLQRG 800
Cdd:PHA02878  241 SVGYcKDYDILKLLLEHG 258
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 705-770 3.55e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.27  E-value: 3.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039742992 705 TNLKGETALHRVCIKNQVEKLIILLSLpGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVD 770
Cdd:PHA03100  188 KDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_5 pfam13857
Ankyrin repeats (many copies);
728-782 4.88e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 4.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039742992 728 LLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRcPEVDLLTQVDGVTPLH 782
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 727-797 5.74e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 5.74e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039742992 727 ILLSlPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKLLL 797
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 ...
 743-771 7.17e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 7.17e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039742992  743 GWTPLHEACNYGNTECVQEILQRCPEVDL 771
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 709-800 1.64e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 709 GETALHrVCIKNQVEKL--IILLSL-PGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCpEVDLLTQVD-GVTPLHDA 784
Cdd:PHA03095   47 GKTPLH-LYLHYSSEKVkdIVRLLLeAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA-GADVNAKDKvGRTPLHVY 124

                          90
                  ....*....|....*...
gi 1039742992 785 LSNG--HVEIGKLLLQRG 800
Cdd:PHA03095  125 LSGFniNPKVIRLLLRKG 142
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 721-836 1.65e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 721 QVEKLII--LLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQ 798
Cdd:PHA02876  154 QQDELLIaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIA-LDDLSVLECAVDSKNIDTIKAIID 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1039742992 799 RggpellQQRNSKGELPLDYVLSPKDKEEL-------FAITNIDD 836
Cdd:PHA02876  233 N------RSNINKNDLSLLKAIRNEDLETSlllydagFSVNSIDD 271
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 710-826 1.85e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039742992 710 ETALHRVCIKNQVEKLIILLSLPGIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGH 789
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD-IPNTDKFSPLHLAVMMGD 147

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039742992 790 VEIGKLLLQRGGpeLLQQRNSKGELPLDYVLSPKDKE 826
Cdd:PHA02875  148 IKGIELLIDHKA--CLDIEDCCGCTPLIIAMAKGDIA 182
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 733-798 2.51e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 2.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039742992 733 GIDINVKDNAGWTPLHEACNYGNTECVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLLLQ 798
Cdd:PLN03192  548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH-IRDANGNTALWNAISAKHHKIFRILYH 612
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 743-770 2.79e-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: 2.79e-03
                          10        20
                  ....*....|....*....|....*...
gi 1039742992 743 GWTPLHEACNYGNTECVQEILQRCPEVD 770
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 743-773 2.91e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 2.91e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039742992 743 GWTPLHEAC-NYGNTECVQEILQRCPEVDLLT 773
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
 
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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