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Conserved domains on  [gi|58428941|gb|AAW77933|]
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viral ankyrin [Bracoviriform demolitoris]

Protein Classification

PHA02736 superfamily protein( domain architecture ID 1018433)

PHA02736 superfamily protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA02736 super family cl31498
Viral ankyrin protein; Provisional
 1-154 1.85e-100

Viral ankyrin protein; Provisional


The actual alignment was detected with superfamily member PHA02736:

Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 285.62  E-value: 1.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941    1 MVPPEEIASASNPDIEGENILHFLCREGDITDLMAFKNVISDANRHLVLQFNRHGKQCVHIVSNPGIADPQEKLKLLMEW 80
Cdd:PHA02736   1 MWPPEEIIFASEPDIEGENILHYLCRNGGVTDLLAFKNAISDENRYLVLEYNRHGKQCVHIVSNPDKADPQEKLKLLMEW 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58428941   81 GADINGQERVFGNTPLHIAAYTQNHKLATWLCNQPGINMGISNYLFKTPYYVACERHDIKIMNILRAKGGQCRI 154
Cdd:PHA02736  81 GADINGKERVFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
 
Name Accession Description Interval E-value
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 1-154 1.85e-100

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 285.62  E-value: 1.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941    1 MVPPEEIASASNPDIEGENILHFLCREGDITDLMAFKNVISDANRHLVLQFNRHGKQCVHIVSNPGIADPQEKLKLLMEW 80
Cdd:PHA02736   1 MWPPEEIIFASEPDIEGENILHYLCRNGGVTDLLAFKNAISDENRYLVLEYNRHGKQCVHIVSNPDKADPQEKLKLLMEW 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58428941   81 GADINGQERVFGNTPLHIAAYTQNHKLATWLCNQPGINMGISNYLFKTPYYVACERHDIKIMNILRAKGGQCRI 154
Cdd:PHA02736  81 GADINGKERVFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-149 3.70e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 3.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941   8 ASASNPDIEGENILHFLCREGDITDLMAFKNVISDANrhlvlQFNRHGKQCVHIVSNPGIAdpqEKLKLLMEWGADINGQ 87
Cdd:COG0666  78 ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-----ARDKDGETPLHLAAYNGNL---EIVKLLLEAGADVNAQ 149

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58428941  88 ERvFGNTPLHIAAYTQNHKLATWLCNQpGINMGISNYLFKTPYYVACERHDIKIMNILRAKG 149
Cdd:COG0666 150 DN-DGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
Ank_2 pfam12796
Ankyrin repeats (3 copies);
72-149 7.68e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 7.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58428941    72 EKLKLLMEWGADINGQERvFGNTPLHIAAYTQNHKLATWLCNQPGINMGISNYlfkTPYYVACERHDIKIMNILRAKG 149
Cdd:pfam12796  11 ELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLLLEKG 84
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-109 8.98e-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: 41.54  E-value: 8.98e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 58428941  60 HIVSNPGIADPQEKLKLLMEWGADINGQERvFGNTPLHIAAYTQNHKLAT 109
Cdd:cd22192 138 HPLSFAACVGNEEIVRLLIEHGADIRAQDS-LGNTVLHILVLQPNKTFAC 186
 
Name Accession Description Interval E-value
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 1-154 1.85e-100

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 285.62  E-value: 1.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941    1 MVPPEEIASASNPDIEGENILHFLCREGDITDLMAFKNVISDANRHLVLQFNRHGKQCVHIVSNPGIADPQEKLKLLMEW 80
Cdd:PHA02736   1 MWPPEEIIFASEPDIEGENILHYLCRNGGVTDLLAFKNAISDENRYLVLEYNRHGKQCVHIVSNPDKADPQEKLKLLMEW 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58428941   81 GADINGQERVFGNTPLHIAAYTQNHKLATWLCNQPGINMGISNYLFKTPYYVACERHDIKIMNILRAKGGQCRI 154
Cdd:PHA02736  81 GADINGKERVFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 16-152 2.19e-42

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 138.80  E-value: 2.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941   16 EGENILHFLCREGDITDLMAFKNVISdANRHLVLQFNRHGKQCVHIVSNPGIADPQEKLKLLMEWGADINGQERVFGNTP 95
Cdd:PHA02743  19 DEQNTFLRICRTGNIYELMEVAPFIS-GDGHLLHRYDHHGRQCTHMVAWYDRANAVMKIELLVNMGADINARELGTGNTL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 58428941   96 LHIAAYTQNHKLATWLCNQPGINMGISNYLFKTPYYVACERHDIKIMNILRAKGGQC 152
Cdd:PHA02743  98 LHIAASTKNYELAEWLCRQLGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGAVC 154
PHA02741 PHA02741
hypothetical protein; Provisional
 1-155 1.12e-26

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 98.96  E-value: 1.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941    1 MVPPEEIASASNPdiEGENILHFLCREGDITDLMAFKNVI-SDANRHLVLQFNRHGKQCVHIVSNPGIADPQEKL-KLLM 78
Cdd:PHA02741   7 MTCLEEMIAEKNS--EGENFFHEAARCGCFDIIARFTPFIrGDCHAAALNATDDAGQMCIHIAAEKHEAQLAAEIiDHLI 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58428941   79 EWGADINGQERVFGNTPLHIAAYTQNHKLATWLCNQPGINMGISNYLFKTPYYVACERHDIKIMNILRAKGGQCRIY 155
Cdd:PHA02741  85 ELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVATSRGF 161
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-149 3.70e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 3.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941   8 ASASNPDIEGENILHFLCREGDITDLMAFKNVISDANrhlvlQFNRHGKQCVHIVSNPGIAdpqEKLKLLMEWGADINGQ 87
Cdd:COG0666  78 ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-----ARDKDGETPLHLAAYNGNL---EIVKLLLEAGADVNAQ 149

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58428941  88 ERvFGNTPLHIAAYTQNHKLATWLCNQpGINMGISNYLFKTPYYVACERHDIKIMNILRAKG 149
Cdd:COG0666 150 DN-DGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
Ank_2 pfam12796
Ankyrin repeats (3 copies);
72-149 7.68e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 7.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58428941    72 EKLKLLMEWGADINGQERvFGNTPLHIAAYTQNHKLATWLCNQPGINMGISNYlfkTPYYVACERHDIKIMNILRAKG 149
Cdd:pfam12796  11 ELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLLLEKG 84
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 72-149 7.72e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 7.72e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58428941   72 EKLKLLMEWGADINGQERVFGNTPLHIAAYTQNHKLATWLCNQpGINMGISNYLFKTPYYVACERHDIKIMNILRAKG 149
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSY-GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 72-151 1.51e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941   72 EKLKLLMEWGADINGQERVFgNTPLHIAAYTQNHKLATWLCNQPGINMGISNYLFKTPYYVACERHDIKIMNILRAKGGQ 151
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLY-ITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-109 8.98e-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: 41.54  E-value: 8.98e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 58428941  60 HIVSNPGIADPQEKLKLLMEWGADINGQERvFGNTPLHIAAYTQNHKLAT 109
Cdd:cd22192 138 HPLSFAACVGNEEIVRLLIEHGADIRAQDS-LGNTVLHILVLQPNKTFAC 186
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
68-149 2.97e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 39.94  E-value: 2.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941  68 ADPQEKLKLLMEWGADINGQERvFGNTPLHIAAYTQNHKLATWLCNQpGINMGISNYLFKTPYYVACERHDIKIMNILRA 147
Cdd:COG0666  64 AGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLE 141


                ..
gi 58428941 148 KG 149
Cdd:COG0666 142 AG 143
Ank_4 pfam13637
Ankyrin repeats (many copies);
67-111 4.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 4.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 58428941    67 IADPQEKLKLLMEWGADINGQERvFGNTPLHIAAYTQNHKLATWL 111
Cdd:pfam13637  10 ASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 72-149 1.26e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.11  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941   72 EKLKLLMEWGADINGQERVfGNTPLHIAAYT--QNHKLATWLCNQpGINMGISNYLFKTP--YYVACERHDIKIMNILRA 147
Cdd:PHA03100  87 EIVKLLLEYGANVNAPDNN-GITPLLYAISKksNSYSIVEYLLDN-GANVNIKNSDGENLlhLYLESNKIDLKILKLLID 164


                 ..
gi 58428941  148 KG 149
Cdd:PHA03100 165 KG 166
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 18-145 1.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.94  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58428941   18 ENILHFLCREGDITDLMafknvisdanrhlvlqfNRHGKQCVHIVSnpGIADPQEKLKLLMEWGADINGQERVFGNTPLH 97
Cdd:PHA02878 214 KPIVHILLENGASTDAR-----------------DKCGNTPLHISV--GYCKDYDILKLLLEHGVDVNAKSYILGLTALH 274

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 58428941   98 IAAYTQNhklATWLCNQPGINMGISNYLFKTPYYVAC-ERHDIKIMNIL 145
Cdd:PHA02878 275 SSIKSER---KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRIL 320
 
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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