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Conserved domains on  [gi|966952245|ref|XP_014997964|]
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protein fem-1 homolog B isoform X1 [Macaca mulatta]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 18460031)

ankyrin repeat (ANK) domain-containing protein mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-203 4.19e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 4.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  24 DGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGH 103
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 104 TDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSHADCD 182
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVnAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                        170       180
                 ....*....|....*....|.
gi 966952245 183 RRSRIEALELLGASFANDREN 203
Cdd:COG0666  246 NAKDKDGLTALLLAAAAGAAL 266
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
414-514 6.85e-08

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 6.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 414 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 493
Cdd:COG0666  113 VNARDKDGETPLHLAAYNG---------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL--------EIV 169

                         90       100
                 ....*....|....*....|.
gi 966952245 494 ISLVEAGAHTDMTNKQNKTPL 514
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPL 190
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-203 4.19e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 4.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  24 DGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGH 103
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 104 TDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSHADCD 182
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVnAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                        170       180
                 ....*....|....*....|.
gi 966952245 183 RRSRIEALELLGASFANDREN 203
Cdd:COG0666  246 NAKDKDGLTALLLAAAAGAAL 266
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-184 9.31e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 9.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245   95 LMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKwRAAIVVNGHGMTPLKVAAESCKADVVEL 174
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 966952245  175 LLSH-ADCDRR 184
Cdd:pfam12796  80 LLEKgADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-180 6.80e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 6.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  36 GHFEVVKLLVSHGANVNHTTVTNSTPLRAA--CFDGRLDIVKYLVENNANISIANKydntclmiaaykghtdvVRYLLEQ 113
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNR-----------------VNYLLSY 181

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966952245 114 RADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSHAD 180
Cdd:PHA03100 182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
414-514 6.85e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 6.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 414 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 493
Cdd:COG0666  113 VNARDKDGETPLHLAAYNG---------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL--------EIV 169

                         90       100
                 ....*....|....*....|.
gi 966952245 494 ISLVEAGAHTDMTNKQNKTPL 514
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPL 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
 412-550 4.50e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 412 IHLDPRTREGFTLLHLAVNSNTPVDdfhtndvcsfpnalVTKLLLDCGAEVNAVDNEGNSALHIIvqynrpISDFLTLHS 491
Cdd:PHA03095  74 ADVNAPERCGFTPLHLYLYNATTLD--------------VIKLLIKAGADVNAKDKVGRTPLHVY------LSGFNINPK 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966952245 492 IIISLVEAGAHTDMTNKQNKTPLDK--STTGVSEILLKtqmkmsLKCLAARAVRANDINYQ 550
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLR------LLIDAGADVYAVDDRFR 188
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-164 9.70e-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: 45.39  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  25 GATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNStplraaCFDGRLDIVKYlvennanisiankYDNTCLMIAAYKGHT 104
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGT------FFRPGPKNLIY-------------YGEHPLSFAACVGNE 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966952245 105 DVVRYLLEQRADPNAKAHCGATALH---------FAAEAghIDIV----KELIKWRAAIVVNGHGMTPLKVAA 164
Cdd:cd22192  150 EIVRLLIEHGADIRAQDSLGNTVLHilvlqpnktFACQM--YDLIlsydKEDDLQPLDLVPNNQGLTPFKLAA 220
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 25-176 1.30e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245   25 GATALWCAAGAGHFEVVKLLVSHGANVN------------HTTVTNSTPLR---AACFdGRLDIVKYLVENNANISIANK 89
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFYHGESPlnaAACL-GSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245   90 YDNTCLMIAAYKGhtdvvryllEQRADPNAKA-HCGATALHFAAeagHIDIVKELikwraAIVVNGHGMTPLKVAAESCK 168
Cdd:TIGR00870 207 LGNTLLHLLVMEN---------EFKAEYEELScQMYNFALSLLD---KLRDSKEL-----EVILNHQGLTPLKLAAKEGR 269


                  ....*...
gi 966952245  169 ADVVELLL 176
Cdd:TIGR00870 270 IVLFRLKL 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 90-119 4.41e-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: 4.41e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 966952245    90 YDNTCLMIAAYKGHTDVVRYLLEQRADPNA 119
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
455-515 7.56e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 7.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966952245  455 LLDCG-AEVNAVDNEGNSALHIIVQYNRPIsdfltlhsIIISLVEAGAHTDMTNKQNKTPLD 515
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALE--------IVRVLLAYGVDLNLKDEEGLTALD 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-203 4.19e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 4.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  24 DGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGH 103
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 104 TDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSHADCD 182
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVnAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                        170       180
                 ....*....|....*....|.
gi 966952245 183 RRSRIEALELLGASFANDREN 203
Cdd:COG0666  246 NAKDKDGLTALLLAAAAGAAL 266
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-193 1.72e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 1.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  24 DGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGH 103
Cdd:COG0666  119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 104 TDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSHADCD 182
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLnAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                        170
                 ....*....|.
gi 966952245 183 RRSRIEALELL 193
Cdd:COG0666  279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-202 2.67e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.01  E-value: 2.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  23 IDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKG 102
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 103 HTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-AD 180
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVnARDNDGETPLHLAAENGHLEIVKLLLEAgAD 211

                        170       180
                 ....*....|....*....|..
gi 966952245 181 CDRRSRIEALELLGASFANDRE 202
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLE 233
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-208 1.63e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 1.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  32 AAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLL 111
Cdd:COG0666   28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 112 EQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-ADCDRRSRIEA 189
Cdd:COG0666  108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAgADVNARDNDGE 187

                        170
                 ....*....|....*....
gi 966952245 190 LELLGASFANdreNYDIIK 208
Cdd:COG0666  188 TPLHLAAENG---HLEIVK 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-184 9.31e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 9.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245   95 LMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKwRAAIVVNGHGMTPLKVAAESCKADVVEL 174
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 966952245  175 LLSH-ADCDRR 184
Cdd:pfam12796  80 LLEKgADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-153 1.33e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245   62 LRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQrADPNAKAHcGATALHFAAEAGHIDIVK 141
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 966952245  142 ELIKWRAAIVVN 153
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
29-120 2.43e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 2.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245   29 LWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVEnNANISIANkYDNTCLMIAAYKGHTDVVR 108
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 966952245  109 YLLEQRADPNAK 120
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-180 6.80e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 6.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  36 GHFEVVKLLVSHGANVNHTTVTNSTPLRAA--CFDGRLDIVKYLVENNANISIANKydntclmiaaykghtdvVRYLLEQ 113
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNR-----------------VNYLLSY 181

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966952245 114 RADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSHAD 180
Cdd:PHA03100 182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-202 6.51e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.29  E-value: 6.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  38 FEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADP 117
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 118 NAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-ADCDRRSRIEALELLGA 195
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDNDGNTPLHLA 160


                 ....*..
gi 966952245 196 SFANDRE 202
Cdd:COG0666  161 AANGNLE 167
PHA03095 PHA03095
ankyrin-like protein; Provisional
 39-186 2.51e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 2.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  39 EVVKLLVSHGANVNHTTVTNSTPLRA-ACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAyKG---HTDVVRYLLEQR 114
Cdd:PHA03095  64 DIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYL-SGfniNPKVIRLLLRKG 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966952245 115 ADPNAKAHCGATALHFAAEAGHIDI--VKELIKWRAAIV-VNGHGMTPLKVAAESCK--ADVVELLLShADCDRRSR 186
Cdd:PHA03095 143 ADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYaVDDRFRSLLHHHLQSFKprARIVRELIR-AGCDPAAT 218
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 25-163 2.94e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  25 GATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIA-AYKGH 103
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKD 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966952245 104 TDVVRYLLEQRADPNAKAHC-GATALHFAAEAGhiDIVKELIKWRAAI-VVNGHGMTPLKVA 163
Cdd:PHA02878 248 YDILKLLLEHGVDVNAKSYIlGLTALHSSIKSE--RKLKLLLEYGADInSLNSYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
92-144 9.63e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 9.63e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 966952245   92 NTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELI 144
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 17-180 2.02e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.14  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  17 CFKRYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISI---------- 86
Cdd:PHA02874  27 CINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpipciekdm 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  87 -------------ANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRA-AIVV 152
Cdd:PHA02874 107 iktildcgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyANVK 186

                        170       180
                 ....*....|....*....|....*...
gi 966952245 153 NGHGMTPLKVAAESCKADVVELLLSHAD 180
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGN 214
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 39-176 2.28e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 2.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  39 EVVKLLVSHGANVNHTTVTNSTPL-----RAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYK--GHTDVVRYLL 111
Cdd:PHA03100  49 DVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 112 EQRADPNAKAHCGATALHFAAEAGHID--IVKELIKWRAAI-----------------VVNGHGMTPLKVAAESCKADVV 172
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDInaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFV 208


                 ....
gi 966952245 173 ELLL 176
Cdd:PHA03100 209 KYLL 212
PHA03095 PHA03095
ankyrin-like protein; Provisional
 38-186 4.01e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 4.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  38 FEVVKLLVSHGANVNHTTVTNSTPL----RAACFDgRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHT-DVVRYLLE 112
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLhlylHYSSEK-VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966952245 113 QRADPNAKAHCGATALH--FAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAES--CKADVVELLLShADCDRRSR 186
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVnALDLYGMTPLAVLLKSrnANVELLRLLID-AGADVYAV 183
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 27-178 5.68e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 5.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  27 TALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDV 106
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966952245 107 VRYLLEQRADPNAKAHCGATALHFAAEAGHiDIVKELIKWRAAIVVNGHGMTPLKVAAE-SCKADVVELLLSH 178
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYH 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
24-88 7.96e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 7.96e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966952245   24 DGATALWCAAGAGHFEVVKLLVSHgANVNHTTvTNSTPLRAACFDGRLDIVKYLVENNANISIAN 88
Cdd:pfam12796  29 NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
58-111 2.38e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 2.38e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966952245   58 NSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLL 111
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 22-201 2.40e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  22 VIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANIS-IANKYDNTCLMIAAY 100
Cdd:PHA02875  32 IYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATI 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 101 KGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL-SH 178
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLdIEDCCGCTPLIIAMAKGDIAICKMLLdSG 191

                        170       180
                 ....*....|....*....|...
gi 966952245 179 ADCDRRSRIEALELLGASFANDR 201
Cdd:PHA02875 192 ANIDYFGKNGCVAALCYAIENNK 214
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 23-179 3.66e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 3.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  23 IDGATALWCAAGAGH-FEVVKLLVSHGANVNHTTVTNSTPL-RAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAY 100
Cdd:PHA02876 305 IKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLhQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAV 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 101 KGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDI-VKELIKwRAAIV--VNGHGMTPLKVAAE-SCKADVVELLL 176
Cdd:PHA02876 385 RNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLID-RGANVnsKNKDLSTPLHYACKkNCKLDVIEMLL 463


                 ...
gi 966952245 177 SHA 179
Cdd:PHA02876 464 DNG 466
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 99-182 3.70e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 3.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  99 AYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRA-AIVVNGHGMTPLKVAAESCKADVVELLLS 177
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAdPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                 ....*
gi 966952245 178 HADCD 182
Cdd:PTZ00322 170 HSQCH 174
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 39-178 3.97e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 3.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  39 EVVKLLVSHGANVNHTTV-TNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADP 117
Cdd:PHA02878 148 EITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966952245 118 NAKAHCGATALHFA-AEAGHIDIVKELIKWRAAIVVNGH--GMTPLKVAAESckADVVELLLSH 178
Cdd:PHA02878 228 DARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYilGLTALHSSIKS--ERKLKLLLEY 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 24-145 4.04e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 4.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  24 DGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGH 103
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966952245 104 TDVVRYLLEQRADPNAKAHCG-ATALHFAAEAGHIDIVKELIK 145
Cdd:PHA02875 181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 41-119 4.55e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 4.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966952245  41 VKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNA 119
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 25-144 9.62e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 9.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  25 GATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNaniSIANKY---DNTCLmiAAYK 101
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFA---SISDPHaagDLLCT--AAKR 632

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966952245 102 GHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELI 144
Cdd:PLN03192 633 NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
Ank_4 pfam13637
Ankyrin repeats (many copies);
27-78 2.04e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 2.04e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 966952245   27 TALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLV 78
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 38-155 4.37e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 55.61  E-value: 4.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  38 FEVVKLLVSHGANVNHTTVTNSTPLraaC--------FDGRLDIVKYLVENNANISIANKYDNT---CLMIAAYKGHTDV 106
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsnikdYKHMLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEI 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 966952245 107 VRYLLEQRADPNAKAHCGATALHFAAEAGH---IDIVKELIKwrAAIVVNGH 155
Cdd:PHA02798 128 LLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLE--KGVDINTH 177
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
414-514 6.85e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 6.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 414 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 493
Cdd:COG0666  113 VNARDKDGETPLHLAAYNG---------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL--------EIV 169

                         90       100
                 ....*....|....*....|.
gi 966952245 494 ISLVEAGAHTDMTNKQNKTPL 514
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
414-515 1.19e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.42  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 414 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 493
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANG---------------NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL--------EIV 202

                         90       100
                 ....*....|....*....|..
gi 966952245 494 ISLVEAGAHTDMTNKQNKTPLD 515
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALD 224
PHA03095 PHA03095
ankyrin-like protein; Provisional
 39-145 1.59e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  39 EVVKLLVSHGANVNHTTVTNSTPLRAA---CFDGRLDIVKYLvENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRA 115
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLL-IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281

                         90       100       110
                 ....*....|....*....|....*....|
gi 966952245 116 DPNAKAHCGATALHFAAEAGHIDIVKELIK 145
Cdd:PHA03095 282 DINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 39-179 1.92e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  39 EVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPN 118
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966952245 119 AKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVN-GHGMTPLKVAAESCKAdVVELLLSHA 179
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNRS-AIELLINNA 245
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-164 3.36e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  37 HFEVVKLLVSHGANVNHTTVTNSTPLraACF----DGRLDIVKYLVENNANISIANKYDNTCLMIAA--YKGHTDVVRYL 110
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPL--AVLlksrNANVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVREL 208

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 966952245 111 LEQRADPNAKAHCGATALHFAAEAG---HIDIVKELIKWRAAIVVNGHGMTPLKVAA 164
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGISINARNRYGQTPLHYAA 265
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-131 3.40e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 3.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 966952245   77 LVEN-NANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFA 131
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
403-514 3.30e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.18  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 403 KINKQIYNLIHLDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRP 482
Cdd:COG0666   69 VALLLLAAGADINAKDDGGNTLLHAAARNG---------------DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110
                 ....*....|....*....|....*....|..
gi 966952245 483 isdfltlhSIIISLVEAGAHTDMTNKQNKTPL 514
Cdd:COG0666  134 --------EIVKLLLEAGADVNAQDNDGNTPL 157
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-253 3.46e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  26 ATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTD 105
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 106 VVR--YLLEQRADPnakaHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-ADC 181
Cdd:PLN03192 606 IFRilYHFASISDP----HAAGDLLCTAAKRNDLTAMKELLKQGLNVdSEDHQGATALQVAMAEDHVDMVRLLIMNgADV 681

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966952245 182 DRRSRIEALellgaSFANDREnydiiktyhylylaMLERFQDGDNILEKEVLPPIHAYGNRTECRNPQELES 253
Cdd:PLN03192 682 DKANTDDDF-----SPTELRE--------------LLQKRELGHSITIVDSVPADEPDLGRDGGSRPGRLQG 734
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 41-111 4.25e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 4.25e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966952245  41 VKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLL 111
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 32-201 4.57e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.49  E-value: 4.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  32 AAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAAC--------------------------------------------- 66
Cdd:PHA02878  44 AVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikdafnnrnveifkiiltn 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  67 -FDGRLD------------------IVKYLVENNANISIANKY-DNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGAT 126
Cdd:PHA02878 124 rYKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966952245 127 ALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKA-DVVELLLSH-ADCDRRSRIEALELLGASFANDR 201
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTdARDKCGNTPLHISVGYCKDyDILKLLLEHgVDVNAKSYILGLTALHSSIKSER 281
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 24-55 3.14e-05

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: 41.12  E-value: 3.14e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 966952245   24 DGATALWCAAG-AGHFEVVKLLVSHGANVNHTT 55
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 412-550 4.50e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 412 IHLDPRTREGFTLLHLAVNSNTPVDdfhtndvcsfpnalVTKLLLDCGAEVNAVDNEGNSALHIIvqynrpISDFLTLHS 491
Cdd:PHA03095  74 ADVNAPERCGFTPLHLYLYNATTLD--------------VIKLLIKAGADVNAKDKVGRTPLHVY------LSGFNINPK 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966952245 492 IIISLVEAGAHTDMTNKQNKTPLDK--STTGVSEILLKtqmkmsLKCLAARAVRANDINYQ 550
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLR------LLIDAGADVYAVDDRFR 188
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-163 8.65e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 8.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 966952245  110 LLEQR-ADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVA 163
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLnLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-164 9.70e-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: 45.39  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  25 GATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNStplraaCFDGRLDIVKYlvennanisiankYDNTCLMIAAYKGHT 104
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGT------FFRPGPKNLIY-------------YGEHPLSFAACVGNE 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966952245 105 DVVRYLLEQRADPNAKAHCGATALH---------FAAEAghIDIV----KELIKWRAAIVVNGHGMTPLKVAA 164
Cdd:cd22192  150 EIVRLLIEHGADIRAQDSLGNTVLHilvlqpnktFACQM--YDLIlsydKEDDLQPLDLVPNNQGLTPFKLAA 220
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 23-179 1.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  23 IDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYkg 102
Cdd:PHA02874 155 DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-- 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 103 HTDVVRYLLEQRADPNAKAHCGATALHFAAE-AGHIDIVKELIKWRAAIVV-NGHGMTPLKVAAESCKAD-VVELLLSHA 179
Cdd:PHA02874 233 HNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIkDNKGENPIDTAFKYINKDpVIKDIIANA 312
Ank_4 pfam13637
Ankyrin repeats (many copies);
126-176 1.05e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 966952245  126 TALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL 176
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 25-176 1.30e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245   25 GATALWCAAGAGHFEVVKLLVSHGANVN------------HTTVTNSTPLR---AACFdGRLDIVKYLVENNANISIANK 89
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFYHGESPlnaAACL-GSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245   90 YDNTCLMIAAYKGhtdvvryllEQRADPNAKA-HCGATALHFAAeagHIDIVKELikwraAIVVNGHGMTPLKVAAESCK 168
Cdd:TIGR00870 207 LGNTLLHLLVMEN---------EFKAEYEELScQMYNFALSLLD---KLRDSKEL-----EVILNHQGLTPLKLAAKEGR 269


                  ....*...
gi 966952245  169 ADVVELLL 176
Cdd:TIGR00870 270 IVLFRLKL 277
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 92-120 1.50e-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: 1.50e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 966952245   92 NTCLMIAAYK-GHTDVVRYLLEQRADPNAK 120
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 25-90 3.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 3.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966952245  25 GATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKY 90
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 23-116 4.38e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  23 IDGATALWCAAGAGHFEVVKLLVsHGANVNHTTVTNSTpLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKG 102
Cdd:PLN03192 589 ANGNTALWNAISAKHHKIFRILY-HFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAED 666

                         90
                 ....*....|....
gi 966952245 103 HTDVVRYLLEQRAD 116
Cdd:PLN03192 667 HVDMVRLLIMNGAD 680
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 90-119 4.41e-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: 4.41e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 966952245    90 YDNTCLMIAAYKGHTDVVRYLLEQRADPNA 119
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
414-516 4.52e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 42.63  E-value: 4.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 414 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRpisdfltlHSII 493
Cdd:COG0666  179 VNARDNDGETPLHLAAENG---------------HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGN--------LEIV 235

                         90       100
                 ....*....|....*....|...
gi 966952245 494 ISLVEAGAHTDMTNKQNKTPLDK 516
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLL 258
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 34-116 5.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  34 GAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDG-RLDIVKYLVENNANISIANKYDNTCLMIAAykGHTDVVRYLLE 112
Cdd:PHA02876 418 GTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLH 495


                 ....
gi 966952245 113 QRAD 116
Cdd:PHA02876 496 YGAE 499
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 71-176 5.71e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs 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 Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.92  E-value: 5.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  71 LDIVKYLVENNANISIA------NKYDNTC-------LMIAAYKGHTDVVRYLLEQRADP---NAKAHCGATALH---FA 131
Cdd:cd22197  107 LQCVKLLVENGADVHARacgrffQKKQGTCfyfgelpLSLAACTKQWDVVNYLLENPHQPaslQAQDSLGNTVLHalvMI 186

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966952245 132 AE------AGHIDIVKELIKWRAAI--------VVNGHGMTPLKVAAESCKADVVELLL 176
Cdd:cd22197  187 ADnspensALVIKMYDGLLQAGARLcptvqleeISNHEGLTPLKLAAKEGKIEIFRHIL 245
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 24-52 7.06e-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: 37.18  E-value: 7.06e-04
                           10        20
                   ....*....|....*....|....*....
gi 966952245    24 DGATALWCAAGAGHFEVVKLLVSHGANVN 52
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 71-177 7.64e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs 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: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 7.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  71 LDIVKYLVENNANISI---------ANKYD-----NTCLMIAAYKGHTDVVRYLLEQRADPNAKAHC-GATALHFAAEAG 135
Cdd:cd22194  154 GDIVKLLIAKGADVNAhakgvffnpKYKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDITSQDSrGNTVLHALVTVA 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 966952245 136 -----HIDIVKELI--------KWRAAIVVNGHGMTPLKVAAESCKADVVELLLS 177
Cdd:cd22194  234 edsktQNDFVKRMYdmillkseNKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 60-186 7.68e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  60 TPLRAACFDGRLDIVKYLVENNANISIA------NKYDNTC-------LMIAAYKGHTDVVRYLLEQRADP---NAKAHC 123
Cdd:cd21882   75 TALHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNLfyfgelpLSLAACTNQEEIVRLLLENGAQPaalEAQDSL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 124 GATALHFAAEAGH---------IDIVKELIKWRAAI--------VVNGHGMTPLKVAAESCKADVVELLLS---HADCDR 183
Cdd:cd21882  155 GNTVLHALVLQADntpensafvCQMYNLLLSYGAHLdptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQrefSGPYQP 234


                 ...
gi 966952245 184 RSR 186
Cdd:cd21882  235 LSR 237
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 27-209 8.15e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  27 TALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANI---------SIANKYDNTCLM- 96
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNInkndlsllkAIRNEDLETSLLl 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  97 ---------IAAYKGH-----------TDVVRYLLEQRADPNAKAHCGATALHFAAEAGH-IDIVKELIKWRAAI-VVNG 154
Cdd:PHA02876 260 ydagfsvnsIDDCKNTplhhasqapslSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVnAADR 339

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 966952245 155 HGMTPLKVAA--ESCKADVVELLLSHADCDRRSRIEALELlgaSFANDRENYDIIKT 209
Cdd:PHA02876 340 LYITPLHQAStlDRNKDIVITLLELGANVNARDYCDKTPI---HYAAVRNNVVIINT 393
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 71-177 1.51e-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: 41.32  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  71 LDIVKYLVENNANISIA-------NKYDNTC-------LMIAAYKGHTDVVRYLLE---QRADPNAKAHCGATALHFAAE 133
Cdd:cd22193   89 GDIVALLVENGADVHAHakgrffqPKYQGEGfyfgelpLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVT 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966952245 134 AG-----HIDIVKEL--------IKWRAAI----VVNGHGMTPLKVAAESCKADVVELLLS 177
Cdd:cd22193  169 VAdntkeNTKFVTRMydmilirgAKLCPTVeleeIRNNDGLTPLQLAAKMGKIEILKYILQ 229
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 25-145 1.54e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs 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 Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.38  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  25 GATALWCAAGAGHFEVVKLLVSHGANVN----------HTTVT---NSTPLRAACFDGRLDIVKYLVENNANISIANKYD 91
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQD 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966952245  92 ---NTCL----MIA-AYKGHTDVVRYLLEQ------RADPNAKA-----HCGATALHFAAEAGHIDIVKELIK 145
Cdd:cd22197  174 slgNTVLhalvMIAdNSPENSALVIKMYDGllqagaRLCPTVQLeeisnHEGLTPLKLAAKEGKIEIFRHILQ 246
PHA03095 PHA03095
ankyrin-like protein; Provisional
 453-522 2.15e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 2.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 453 KLLLDCGAEVNAVDNEGNSALHIIVQYNRPISdfltlhSIIISLVEAGAHTDMTNKQNKTPLDKSTTGVS 522
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLHHHLQSFKPRA------RIVRELIRAGCDPAATDMLGNTPLHSMATGSS 234
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 412-517 2.46e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 412 IHLDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNrpisdfltLHS 491
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKG---------------DLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN--------FFD 171

                         90       100
                 ....*....|....*....|....*.
gi 966952245 492 IIISLVEAGAHTDMTNKQNKTPLDKS 517
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNA 197
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 25-92 2.91e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.62  E-value: 2.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966952245  25 GATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDN 92
Cdd:PLN03192 622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 24-53 3.69e-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: 34.93  E-value: 3.69e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 966952245   24 DGATALWCAAGAGHFEVVKLLVSHGANVNH 53
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 71-153 4.14e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 4.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  71 LDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI 150
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237


                 ...
gi 966952245 151 VVN 153
Cdd:PHA02876 238 NKN 240
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 90-119 4.67e-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: 34.93  E-value: 4.67e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 966952245   90 YDNTCLMIAAYKGHTDVVRYLLEQRADPNA 119
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-176 5.56e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245  40 VVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYL--------- 110
Cdd:PHA02874  17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsi 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 111 --------------LEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELL 175
Cdd:PHA02874  97 lpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVnIEDDNGCYPIHIAIKHNFFDIIKLL 176


                 .
gi 966952245 176 L 176
Cdd:PHA02874 177 L 177
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 402-489 6.46e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966952245 402 CKINKQIYNLIHLDPRTREGFTLLHLAVNSNTPvdDFhtndvcsfpnalvTKLLLDCGAEVNAVDNEGNSALHIIVQYNr 481
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNP--EF-------------VKYLLDLGANPNLVNKYGDTPLHIAILNN- 236


                 ....*...
gi 966952245 482 pISDFLTL 489
Cdd:PHA03100 237 -NKEIFKL 243
Ank_5 pfam13857
Ankyrin repeats (many copies);
44-98 6.71e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 6.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 966952245   44 LVSHG-ANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIA 98
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
455-515 7.56e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 7.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966952245  455 LLDCG-AEVNAVDNEGNSALHIIVQYNRPIsdfltlhsIIISLVEAGAHTDMTNKQNKTPLD 515
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALE--------IVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 24-77 9.72e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.73  E-value: 9.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 966952245  24 DGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYL 77
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
 
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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