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Conserved domains on  [gi|665402930|ref|NP_611720|]
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uncharacterized protein Dmel_CG42284, isoform D [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dpy-30 super family cl04973
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 289-330 2.66e-13

Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).


The actual alignment was detected with superfamily member pfam05186:

Pssm-ID: 428357  Cd Length: 42  Bit Score: 64.17  E-value: 2.66e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 665402930  289 EQGKYLADSLADPLIKALTEIANKRPRDPVAYLTNYLQHFMG 330
Cdd:pfam05186   1 PARQYLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKNNP 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
135-231 6.37e-13

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 6.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930  135 HDAARDGGLLALQQALDRRkfaIAKNDISPNGSTPLHVAVLFGHTDIVRYLASRFPETMtitDNDGRTPLHYAAtikDNG 214
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENG---ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAA---RSG 72

                          90
                  ....*....|....*....
gi 665402930  215 HF--YNMLLQLGANPKSLD 231
Cdd:pfam12796  73 HLeiVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
533-630 2.49e-07

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930  533 LHQMIRENNMERVVELTNVANAkwlIRTKNYYGRTALHIAVLKESEEMVQHMVKICPegLKITDNlERTVLHYAMGTNAL 612
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDN-GRTALHYAARSGHL 74

                          90
                  ....*....|....*...
gi 665402930  613 ESVsRILIQNGAKRTAKD 630
Cdd:pfam12796  75 EIV-KLLLEKGADINVKD 91
 
Name Accession Description Interval E-value
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 289-330 2.66e-13

Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).


Pssm-ID: 428357  Cd Length: 42  Bit Score: 64.17  E-value: 2.66e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 665402930  289 EQGKYLADSLADPLIKALTEIANKRPRDPVAYLTNYLQHFMG 330
Cdd:pfam05186   1 PARQYLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKNNP 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
135-231 6.37e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 6.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930  135 HDAARDGGLLALQQALDRRkfaIAKNDISPNGSTPLHVAVLFGHTDIVRYLASRFPETMtitDNDGRTPLHYAAtikDNG 214
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENG---ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAA---RSG 72

                          90
                  ....*....|....*....
gi 665402930  215 HF--YNMLLQLGANPKSLD 231
Cdd:pfam12796  73 HLeiVKLLLEKGADINVKD 91
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
 291-328 4.01e-12

dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like family; The DYDC-like family includes DYDC1 and DYDC2, as well as Chlamydomonas reinhardtii flagellar radial spoke protein 2 (RSP2) and similar proteins. DYDC1 plays a crucial role during acrosome biogenesis. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. Members of this family contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438535  Cd Length: 44  Bit Score: 60.86  E-value: 4.01e-12
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 665402930 291 GKYLADSLADPLIKALTEIANKRPRDPVAYLTNYLQHF 328
Cdd:cd22966    2 SAYLKETVGDVLTKALAEVALKRPADPIEFLANWLLKY 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
135-237 7.60e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 7.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 135 HDAARDGGLLALQQALDRRkfaIAKNDISPNGSTPLHVAVLFGHTDIVRYLASRFPEtMTITDNDGRTPLHYAAtikDNG 214
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAG---ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAA---ANG 164

                         90       100
                 ....*....|....*....|....*
gi 665402930 215 HFY--NMLLQLGANPKSLDKLGHSA 237
Cdd:COG0666  165 NLEivKLLLEAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
533-630 2.49e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930  533 LHQMIRENNMERVVELTNVANAkwlIRTKNYYGRTALHIAVLKESEEMVQHMVKICPegLKITDNlERTVLHYAMGTNAL 612
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDN-GRTALHYAARSGHL 74

                          90
                  ....*....|....*...
gi 665402930  613 ESVsRILIQNGAKRTAKD 630
Cdd:pfam12796  75 EIV-KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 165-249 2.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 165 NGSTPLHVAVLFGHTDIVRYL--ASRFPetmTITDNDGRTPLHYAATIKdNGHFYNMLLQLGANPKSLDKlghsaefYLD 242
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLldLGANP---NLVNKYGDTPLHIAILNN-NKEIFKLLLNNGPSIKTIIE-------TLL 259


                 ....*..
gi 665402930 243 KEKAKNI 249
Cdd:PHA03100 260 YFKDKDL 266
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
513-649 4.14e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 513 NAALGEFLANLKALEESREELHQMIRENNMERVVELTNVANAKWLIRTKNYYGRTALHIAVLKESEEMVQHMVKicpEGL 592
Cdd:COG0666   35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE---AGA 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665402930 593 KI--TDNLERTVLHYAMGTNALESVsRILIQNGAKRTAKDLKGRQPSYY--FINKADILRL 649
Cdd:COG0666  112 DVnaRDKDGETPLHLAAYNGNLEIV-KLLLEAGADVNAQDNDGNTPLHLaaANGNLEIVKL 171
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 165-188 1.87e-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: 36.03  E-value: 1.87e-03
                           10        20
                   ....*....|....*....|....
gi 665402930   165 NGSTPLHVAVLFGHTDIVRYLASR 188
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 533-630 1.99e-03

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: 41.15  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 533 LHQMIRENNMERVVELTNvaNAKWLIR---TKNYY-GRTALHIAVLKESEEMVQHMVK-----ICPEG-----LKITDNL 598
Cdd:cd22192   55 LHVAALYDNLEAAVVLME--AAPELVNepmTSDLYqGETALHIAVVNQNLNLVRELIArgadvVSPRAtgtffRPGPKNL 132

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 665402930 599 ----ERtVLHYAMGTNaLESVSRILIQNGAKRTAKD 630
Cdd:cd22192  133 iyygEH-PLSFAACVG-NEEIVRLLIEHGADIRAQD 166
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 166-226 2.58e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 2.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665402930 166 GSTPLHVAVLFGHTDIVRYLA--SRFPETMTITDNDGRTPLHYAATIKDNG--------HFYNMLLQLGAN 226
Cdd:cd22193  123 GELPLSLAACTNQPDIVQYLLenEHQPADIEAQDSRGNTVLHALVTVADNTkentkfvtRMYDMILIRGAK 193
PHA03095 PHA03095
ankyrin-like protein; Provisional
 558-646 5.76e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 558 IRTKNYYGRTALHIAVL-KESEEMVQHMVKiCPEGLKITDNLERTVLH-YAMGTNALESVSRILIQNGAKRTAKDLKGRQ 635
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYnATTLDVIKLLIK-AGADVNAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                         90
                 ....*....|.
gi 665402930 636 PSYYFINKADI 646
Cdd:PHA03095 155 PLAVLLKSRNA 165
 
Name Accession Description Interval E-value
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 289-330 2.66e-13

Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).


Pssm-ID: 428357  Cd Length: 42  Bit Score: 64.17  E-value: 2.66e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 665402930  289 EQGKYLADSLADPLIKALTEIANKRPRDPVAYLTNYLQHFMG 330
Cdd:pfam05186   1 PARQYLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKNNP 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
135-231 6.37e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 6.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930  135 HDAARDGGLLALQQALDRRkfaIAKNDISPNGSTPLHVAVLFGHTDIVRYLASRFPETMtitDNDGRTPLHYAAtikDNG 214
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENG---ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAA---RSG 72

                          90
                  ....*....|....*....
gi 665402930  215 HF--YNMLLQLGANPKSLD 231
Cdd:pfam12796  73 HLeiVKLLLEKGADINVKD 91
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
 291-328 4.01e-12

dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like family; The DYDC-like family includes DYDC1 and DYDC2, as well as Chlamydomonas reinhardtii flagellar radial spoke protein 2 (RSP2) and similar proteins. DYDC1 plays a crucial role during acrosome biogenesis. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. Members of this family contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438535  Cd Length: 44  Bit Score: 60.86  E-value: 4.01e-12
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 665402930 291 GKYLADSLADPLIKALTEIANKRPRDPVAYLTNYLQHF 328
Cdd:cd22966    2 SAYLKETVGDVLTKALAEVALKRPADPIEFLANWLLKY 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
135-237 7.60e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 7.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 135 HDAARDGGLLALQQALDRRkfaIAKNDISPNGSTPLHVAVLFGHTDIVRYLASRFPEtMTITDNDGRTPLHYAAtikDNG 214
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAG---ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAA---ANG 164

                         90       100
                 ....*....|....*....|....*
gi 665402930 215 HFY--NMLLQLGANPKSLDKLGHSA 237
Cdd:COG0666  165 NLEivKLLLEAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
136-271 9.44e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 9.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 136 DAARDGGLLALQQALDRRKFAIAK---------NDISPNGSTPLHVAVLFGHTDIVRYLASRFPETmTITDNDGRTPLHY 206
Cdd:COG0666  147 NAQDNDGNTPLHLAAANGNLEIVKllleagadvNARDNDGETPLHLAAENGHLEIVKLLLEAGADV-NAKDNDGKTALDL 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402930 207 AAtIKDNGHFYNMLLQLGANPKSLDKLGHSAEFYLDKEKAKNILNYTELLNIFGAEELENQLLND 271
Cdd:COG0666  226 AA-ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
533-630 2.49e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930  533 LHQMIRENNMERVVELTNVANAkwlIRTKNYYGRTALHIAVLKESEEMVQHMVKICPegLKITDNlERTVLHYAMGTNAL 612
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDN-GRTALHYAARSGHL 74

                          90
                  ....*....|....*...
gi 665402930  613 ESVsRILIQNGAKRTAKD 630
Cdd:pfam12796  75 EIV-KLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
166-216 1.22e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.22e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665402930  166 GSTPLHVAVLFGHTDIVRYLASRFPEtMTITDNDGRTPLHYAATikdNGHF 216
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAAS---NGNV 47
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-237 4.92e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.80  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 119 AFLNNVPSYMEKIHRVHDAARDGGLLALQQALDRRKFAIAKNDisPNGSTPLHVAVLFGHTDIVRYLASRfPETMTITDN 198
Cdd:COG0666   42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD--DGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDK 118

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 665402930 199 DGRTPLHYAAtIKDNGHFYNMLLQLGANPKSLDKLGHSA 237
Cdd:COG0666  119 DGETPLHLAA-YNGNLEIVKLLLEAGADVNAQDNDGNTP 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
170-216 1.40e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 1.40e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 665402930  170 LHVAVLFGHTDIVRYLASRFPEtMTITDNDGRTPLHYAATikdNGHF 216
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAK---NGHL 43
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 165-249 2.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 165 NGSTPLHVAVLFGHTDIVRYL--ASRFPetmTITDNDGRTPLHYAATIKdNGHFYNMLLQLGANPKSLDKlghsaefYLD 242
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLldLGANP---NLVNKYGDTPLHIAILNN-NKEIFKLLLNNGPSIKTIIE-------TLL 259


                 ....*..
gi 665402930 243 KEKAKNI 249
Cdd:PHA03100 260 YFKDKDL 266
Ank_5 pfam13857
Ankyrin repeats (many copies);
153-207 2.73e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665402930  153 RKFAIAKNDISPNGSTPLHVAVLFGHTDIVRYLAsRFPETMTITDNDGRTPLHYA 207
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 134-212 3.00e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 134 VHDAARDGGLLALQQALDRRKFAiakND-ISPNGSTPLHVAVLFGHTDIVRYLASRFPETmTITDNDGRTPLHYAATIKD 212
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFA---DDvFYKDGMTPLHLATILKKLDIMKLLIARGADP-DIPNTDKFSPLHLAVMMGD 147
DD_DPY30_SDC1-like cd22958
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ...
 293-325 6.32e-05

dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like family includes DPY30 from animals and its homolog SDC1 from yeast, DPY30 domain-containing protein (DYDC), adenylate kinase 7 (AK7), IQ domain-containing protein K (IQCK), nucleoside diphosphate kinase homolog 5 (NDKH5), EF-hand calcium-binding domain-containing protein 5 (EFCAB5), and Chlamydomonas reinhardtii flagellar radial spoke proteins, RSP2 and RSP23. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately allosterically regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. Yeast SDC1, also called complex proteins associated with SET1 protein SDC1, Set1C component SDC1, or suppressor of CDC25 protein 1, is the smallest subunit of COMPASS (COMplex of Proteins ASsociated with Set1) and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. DYDC1 plays a crucial role during acrosome biogenesis. AK7 (EC2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 7, is a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is involved in maintaining ciliary structure and function. IQ motif-containing proteins may play an active role in cell polarization and migration, and even in ciliary function. The function of IQCK remains unclear. NDKH5, also called NME5, NDP kinase homolog 5, inhibitor of p53-induced apoptosis-beta (IPIA-beta), testis-specific nm23 homolog, or nm23-H5, is specifically expressed in testis germinal cells. It may not have NDK kinase activity. It confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. It may play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from the flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. Members of this family contain a DPY30/SDC1 helical bundle domain that is formed by two alpha-helices. The DPY30/SDC1 helical bundle domain is also called D/D domain and might be analogous to the D/D domain found in the regulatory subunit of cAMP-dependent protein kinase (PKA).


Pssm-ID: 438527  Cd Length: 40  Bit Score: 40.51  E-value: 6.32e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 665402930 293 YLADSLADPLIKALTEIANKRPRDPVAYLTNYL 325
Cdd:cd22958    4 YLSETVLPTLIPALAELLKARPEDPLEWLAEYL 36
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-232 1.66e-04

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: 39.19  E-value: 1.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 665402930  199 DGRTPLHYAATIKDNGHFYNMLLQLGANPKSLDK 232
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
513-649 4.14e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 513 NAALGEFLANLKALEESREELHQMIRENNMERVVELTNVANAKWLIRTKNYYGRTALHIAVLKESEEMVQHMVKicpEGL 592
Cdd:COG0666   35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE---AGA 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665402930 593 KI--TDNLERTVLHYAMGTNALESVsRILIQNGAKRTAKDLKGRQPSYY--FINKADILRL 649
Cdd:COG0666  112 DVnaRDKDGETPLHLAAYNGNLEIV-KLLLEAGADVNAQDNDGNTPLHLaaANGNLEIVKL 171
Ank_4 pfam13637
Ankyrin repeats (many copies);
134-185 4.64e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 4.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665402930  134 VHDAARDGGLLALQQALDRRKFAIAKNDispNGSTPLHVAVLFGHTDIVRYL 185
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDG---NGETALHFAASNGNVEVLKLL 53
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
 292-325 4.67e-04

dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate kinase (AK7, EC2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 7, is a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. It also displays broad nucleoside diphosphate kinase activity. AK7 is involved in maintaining ciliary structure and function. This model corresponds to the C-terminal domain of AK7, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438536 [Multi-domain]  Cd Length: 41  Bit Score: 38.24  E-value: 4.67e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 665402930 292 KYLADSLADPLIKALTEIANKRPRDPVAYLTNYL 325
Cdd:cd22967    4 NYLMKYVMPTLTEGLVEVCKVRPEDPVDFLAEYL 37
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 160-257 4.95e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 160 NDISPNGSTPLHVAVLFGHTD--IVRYLASR-----------------FPetMTITDNDGRTPLHYAAtIKDNGHFYNML 220
Cdd:PHA03100 135 NIKNSDGENLLHLYLESNKIDlkILKLLIDKgvdinaknrvnyllsygVP--INIKDVYGFTPLHYAV-YNNNPEFVKYL 211

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 665402930 221 LQLGANPKSLDKLGHSAEFYLDKEKAKNILNytELLN 257
Cdd:PHA03100 212 LDLGANPNLVNKYGDTPLHIAILNNNKEIFK--LLLN 246
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 165-207 1.31e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 665402930 165 NGSTPLHVAVLFGHTDIVRYLAsRFPETMTITDNDGRTPLHYA 207
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELA 155
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 165-188 1.87e-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: 36.03  E-value: 1.87e-03
                           10        20
                   ....*....|....*....|....
gi 665402930   165 NGSTPLHVAVLFGHTDIVRYLASR 188
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
PHA03095 PHA03095
ankyrin-like protein; Provisional
 166-227 1.91e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402930 166 GSTPLHVAVLFG---HTDIVRYLASRFpeTMTITDNDGRTPLHYAAtIKDNGHFYNMLLQLGANP 227
Cdd:PHA03095 222 GNTPLHSMATGSsckRSLVLPLLIAGI--SINARNRYGQTPLHYAA-VFNNPRACRRLIALGADI 283
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 533-630 1.99e-03

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: 41.15  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 533 LHQMIRENNMERVVELTNvaNAKWLIR---TKNYY-GRTALHIAVLKESEEMVQHMVK-----ICPEG-----LKITDNL 598
Cdd:cd22192   55 LHVAALYDNLEAAVVLME--AAPELVNepmTSDLYqGETALHIAVVNQNLNLVRELIArgadvVSPRAtgtffRPGPKNL 132

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 665402930 599 ----ERtVLHYAMGTNaLESVSRILIQNGAKRTAKD 630
Cdd:cd22192  133 iyygEH-PLSFAACVG-NEEIVRLLIEHGADIRAQD 166
DD_DPY30_SDC1 cd22965
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ...
 292-325 2.05e-03

dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 from animals and its homologs, including SDC1 from yeast. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately allosterically regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. DPY30 is the core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. As part of the MLL1/MLL complex, DPY30 is involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. In a teratocarcinoma cell, DPY30 plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. It may also play an indirect or direct role in endosomal transport. Yeast SDC1, also called complex proteins associated with SET1 (COMPASS) protein SDC1, Set1C component SDC1, or suppressor of CDC25 protein 1, is the smallest subunit of COMPASS and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. This model corresponds to the C-terminal helical bundle domain of DPY30/SDC1, which is called dimerization/docking (D/D) domain. It forms a homodimer, which directly interacts with the Ash2L (Bre2 in yeast) subunit of COMPASS through its DPY30-binding motif (DBM).


Pssm-ID: 438534  Cd Length: 41  Bit Score: 36.25  E-value: 2.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 665402930 292 KYLADSLADPLIKALTEIANKRPRDPVAYLTNYL 325
Cdd:cd22965    3 QYLDKTVVPVLLEGLKELAKERPEDPLEFLAEYL 36
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
550-655 2.09e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 550 NVANAKWLIR------TKNYYGRTALHIAVLKESEEMVQHMVKicpEG--LKITDNLERTVLHYAMGTNALESVsRILIQ 621
Cdd:COG0666  165 NLEIVKLLLEagadvnARDNDGETPLHLAAENGHLEIVKLLLE---AGadVNAKDNDGKTALDLAAENGNLEIV-KLLLE 240

                         90       100       110
                 ....*....|....*....|....*....|....
gi 665402930 622 NGAKRTAKDLKGRQPSYYFINKADILRLQEEEEE 655
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 166-226 2.58e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 2.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665402930 166 GSTPLHVAVLFGHTDIVRYLA--SRFPETMTITDNDGRTPLHYAATIKDNG--------HFYNMLLQLGAN 226
Cdd:cd22193  123 GELPLSLAACTNQPDIVQYLLenEHQPADIEAQDSRGNTVLHALVTVADNTkentkfvtRMYDMILIRGAK 193
DD_NDKH5-like cd22970
dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5) ...
 293-325 2.77e-03

dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5)-like family; The NDKH5 family includes NDKH5, Chlamydomonas reinhardtii flagellar radial spoke protein 23 (RSP23) and similar proteins. NDKH5, also called NME5, NDP kinase homolog 5, inhibitor of p53-induced apoptosis-beta (IPIA-beta), testis-specific nm23 homolog, or nm23-H5, is specifically expressed in testis germinal cells. It may not have NDK kinase activity. It confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. It may play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from the flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. Members of this family contain a C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438539  Cd Length: 45  Bit Score: 35.97  E-value: 2.77e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 665402930 293 YLADSLADPLIKALTEIANKRPRDPVAYLTNYL 325
Cdd:cd22970    8 YLSKHVNPTLLKGLTELCKEKPADPVTWLADWL 40
PHA03095 PHA03095
ankyrin-like protein; Provisional
 160-259 4.57e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 160 NDISPNGSTPLHVAVLFGHT-DIVRYLASRFPETmTITDNDGRTPLH-YAATIKDNGHFYNMLLQLGANPKSLDKLGHSA 237
Cdd:PHA03095  77 NAPERCGFTPLHLYLYNATTlDVIKLLIKAGADV-NAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDLYGMTP 155

                         90       100
                 ....*....|....*....|..
gi 665402930 238 EFYLDKEKAKNIlnytELLNIF 259
Cdd:PHA03095 156 LAVLLKSRNANV----ELLRLL 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
 558-646 5.76e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 558 IRTKNYYGRTALHIAVL-KESEEMVQHMVKiCPEGLKITDNLERTVLH-YAMGTNALESVSRILIQNGAKRTAKDLKGRQ 635
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYnATTLDVIKLLIK-AGADVNAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                         90
                 ....*....|.
gi 665402930 636 PSYYFINKADI 646
Cdd:PHA03095 155 PLAVLLKSRNA 165
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 179-236 6.58e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 6.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665402930 179 TDIVRYLASRFPETMTITDNDGRTPLHYAATIKDNgHFYNMLLQLGANPKSLDKLGHS 236
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKGNTALHYATENKDQ-RLTELLLSYGANVNIPDKTNNS 203
Ank_4 pfam13637
Ankyrin repeats (many copies);
533-582 8.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 8.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665402930  533 LHQMIRENNMERVVELtnvANAKWLIRTKNYYGRTALHIAVLKESEEMVQ 582
Cdd:pfam13637   5 LHAAAASGHLELLRLL---LEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 116-207 9.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.79  E-value: 9.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402930 116 EIQAFLNNVPSYMEKihRVHDAARDGGLLALQQALDRRKFAIAKNDispNGSTPLHVAVLFGHTDIVRYLASRfpeTMTI 195
Cdd:PHA02874 178 EKGAYANVKDNNGES--PLHNAAEYGDYACIKLLIDHGNHIMNKCK---NGFTPLHNAIIHNRSAIELLINNA---SIND 249

                         90
                 ....*....|..
gi 665402930 196 TDNDGRTPLHYA 207
Cdd:PHA02874 250 QDIDGSTPLHHA 261
 
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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