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Conserved domains on  [gi|15239917|ref|NP_196789|]
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CCCH-type zinc finger protein with ARM repeat domain-containing protein [Arabidopsis thaliana]

Protein Classification

zinc finger CCCH domain-containing protein( domain architecture ID 12122282)

zinc finger CCCH domain-containing protein similar to Arabidopsis CCCH-containing zinc-finger proteins that possess nuclease activity; also contains ankyrin repeats

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-191 5.99e-14

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.06  E-value: 5.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239917  85 RTPLMVASLYGSLDVVKFILSFPeAELNLScGPDKSTALHCAASGasvNSLDVVKLLLSVGADPNIPDAHGNRPVDVLVV 164
Cdd:COG0666 154 NTPLHLAAANGNLEIVKLLLEAG-ADVNAR-DNDGETPLHLAAEN---GHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                        90       100
                ....*....|....*....|....*..
gi 15239917 165 SPHAPGLRTILEEILKKDEIISEDLHA 191
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAKDKDGLTA 255
ZnF_C3H1 smart00356
zinc finger;
301-322 9.71e-06

zinc finger;


:

Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 42.62  E-value: 9.71e-06
                           10        20
                   ....*....|....*....|..
gi 15239917    301 VPCPDFKKGSCKQGDMCEYAHG 322
Cdd:smart00356   5 ELCKFFKRGYCPRGDRCKFAHP 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-191 5.99e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.06  E-value: 5.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239917  85 RTPLMVASLYGSLDVVKFILSFPeAELNLScGPDKSTALHCAASGasvNSLDVVKLLLSVGADPNIPDAHGNRPVDVLVV 164
Cdd:COG0666 154 NTPLHLAAANGNLEIVKLLLEAG-ADVNAR-DNDGETPLHLAAEN---GHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                        90       100
                ....*....|....*....|....*..
gi 15239917 165 SPHAPGLRTILEEILKKDEIISEDLHA 191
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-152 5.70e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 5.70e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239917    85 RTPLMVASLYGSLDVVKFILSFPEAELNLscgpDKSTALHCAASGasvNSLDVVKLLLSVGADPNIPD 152
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARS---GHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-169 1.37e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239917   86 TPLMVASLYGS-LDVVKFILSFpEAELNLSCGPDKsTALHCAASGASVNSlDVVKLLLSVGADPNIPDAHGNRPVDVLVV 164
Cdd:PHA03095  85 TPLHLYLYNATtLDVIKLLIKA-GADVNAKDKVGR-TPLHVYLSGFNINP-KVIRLLLRKGADVNALDLYGMTPLAVLLK 161


                 ....*
gi 15239917  165 SPHAP 169
Cdd:PHA03095 162 SRNAN 166
ZnF_C3H1 smart00356
zinc finger;
301-322 9.71e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 42.62  E-value: 9.71e-06
                           10        20
                   ....*....|....*....|..
gi 15239917    301 VPCPDFKKGSCKQGDMCEYAHG 322
Cdd:smart00356   5 ELCKFFKRGYCPRGDRCKFAHP 26
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
 303-321 7.28e-04

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 37.01  E-value: 7.28e-04
                          10
                  ....*....|....*....
gi 15239917   303 CPDFKKGSCKQGDMCEYAH 321
Cdd:pfam18345   1 CKFFLKGRCRYGDKCRFAH 19
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 40-155 9.66e-04

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: 42.31  E-value: 9.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239917  40 SALLEFAADNDVEGFRRQLSDVSCINqmglwyrrqrFVRRMVLEqrTPLMVASLYGSLDVVKFILSFPEAELNLSCGPD- 118
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDL----------FQRGALGE--TALHVAALYDNLEAAVVLMEAAPELVNEPMTSDl 86

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15239917 119 --KSTALHCAASGASVNSldvVKLLLSVGADPNIPDAHG 155
Cdd:cd22192  87 yqGETALHIAVVNQNLNL---VRELIARGADVVSPRATG 122
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 118-150 1.01e-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: 36.80  E-value: 1.01e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 15239917    118 DKSTALHCAASGasvNSLDVVKLLLSVGADPNI 150
Cdd:smart00248   1 DGRTPLHLAAEN---GNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-191 5.99e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.06  E-value: 5.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239917  85 RTPLMVASLYGSLDVVKFILSFPeAELNLScGPDKSTALHCAASGasvNSLDVVKLLLSVGADPNIPDAHGNRPVDVLVV 164
Cdd:COG0666 154 NTPLHLAAANGNLEIVKLLLEAG-ADVNAR-DNDGETPLHLAAEN---GHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                        90       100
                ....*....|....*....|....*..
gi 15239917 165 SPHAPGLRTILEEILKKDEIISEDLHA 191
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-152 5.70e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 5.70e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239917    85 RTPLMVASLYGSLDVVKFILSFPEAELNLscgpDKSTALHCAASGasvNSLDVVKLLLSVGADPNIPD 152
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARS---GHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
83-158 3.16e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 3.16e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239917  83 EQRTPLMVASLYGSLDVVKFILSFPeAELNLScGPDKSTALHCAASGasvNSLDVVKLLLSVGADPNIPDAHGNRP 158
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAG-ADVNAR-DKDGETPLHLAAYN---GNLEIVKLLLEAGADVNAQDNDGNTP 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-169 1.37e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239917   86 TPLMVASLYGS-LDVVKFILSFpEAELNLSCGPDKsTALHCAASGASVNSlDVVKLLLSVGADPNIPDAHGNRPVDVLVV 164
Cdd:PHA03095  85 TPLHLYLYNATtLDVIKLLIKA-GADVNAKDKVGR-TPLHVYLSGFNINP-KVIRLLLRKGADVNALDLYGMTPLAVLLK 161


                 ....*
gi 15239917  165 SPHAP 169
Cdd:PHA03095 162 SRNAN 166
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 121-152 3.09e-06

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: 44.20  E-value: 3.09e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 15239917   121 TALHCAAsgASVNSLDVVKLLLSVGADPNIPD 152
Cdd:pfam00023   4 TPLHLAA--GRRGNLEIVKLLLSKGADVNARD 33
ZnF_C3H1 smart00356
zinc finger;
301-322 9.71e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 42.62  E-value: 9.71e-06
                           10        20
                   ....*....|....*....|..
gi 15239917    301 VPCPDFKKGSCKQGDMCEYAHG 322
Cdd:smart00356   5 ELCKFFKRGYCPRGDRCKFAHP 26
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-142 6.39e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 6.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15239917    84 QRTPLMVASLYGSLDVVKFILSFPeAELNLSCGpDKSTALHCAASGasvNSLDVVKLLL 142
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDG-NGETALHFAASN---GNVEVLKLLL 54
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
 303-321 7.28e-04

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 37.01  E-value: 7.28e-04
                          10
                  ....*....|....*....
gi 15239917   303 CPDFKKGSCKQGDMCEYAH 321
Cdd:pfam18345   1 CKFFLKGRCRYGDKCRFAH 19
Ank_5 pfam13857
Ankyrin repeats (many copies);
109-161 8.67e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 8.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15239917   109 AELNLSCGpDKSTALHCAASGasvNSLDVVKLLLSVGADPNIPDAHGNRPVDV 161
Cdd:pfam13857   7 IDLNRLDG-EGYTPLHVAAKY---GALEIVRVLLAYGVDLNLKDEEGLTALDL 55
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 40-155 9.66e-04

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: 42.31  E-value: 9.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239917  40 SALLEFAADNDVEGFRRQLSDVSCINqmglwyrrqrFVRRMVLEqrTPLMVASLYGSLDVVKFILSFPEAELNLSCGPD- 118
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDL----------FQRGALGE--TALHVAALYDNLEAAVVLMEAAPELVNEPMTSDl 86

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15239917 119 --KSTALHCAASGASVNSldvVKLLLSVGADPNIPDAHG 155
Cdd:cd22192  87 yqGETALHIAVVNQNLNL---VRELIARGADVVSPRATG 122
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 118-150 1.01e-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: 36.80  E-value: 1.01e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 15239917    118 DKSTALHCAASGasvNSLDVVKLLLSVGADPNI 150
Cdd:smart00248   1 DGRTPLHLAAEN---GNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 98-176 6.72e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 6.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15239917   98 DVVKFILSFpEAELNLSCGPDKSTALHCAASGASVnslDVVKLLLSVGADPNIPDAHGNRPVDVLVVSPHAPGLRTILE 176
Cdd:PHA02878 148 EITKLLLSY-GADINMKDRHKGNTALHYATENKDQ---RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLE 222
Ank_2 pfam12796
Ankyrin repeats (3 copies);
79-113 7.49e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.25  E-value: 7.49e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 15239917    79 RMVLEQRTPLMVASLYGSLDVVKFILSfPEAELNL 113
Cdd:pfam12796  56 NLKDNGRTALHYAARSGHLEIVKLLLE-KGADINV 89
 
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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