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Conserved domains on  [gi|7657265|ref|NP_056137|]
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protein fem-1 homolog B [Homo sapiens]

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];
4-256 9.84e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 9.84e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    4 LAGYVYKAASEGKVLTLAALLLNRSESDIRYLLG---YVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYrvqtqqtgtVR 80
Cdd:COG0666  42 LALLALALADALGALLLLAAALAGDLLVALLLLAagaDINAKDDGGNTLLHAAARNGDLEIVKLLLEAG---------AD 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   81 FDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMI 160
Cdd:COG0666 113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  161 AAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL 239
Cdd:COG0666 193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLnAKDKDGLTALLLAAAAGAALIVKLLL 272

                       250
                ....*....|....*..
gi 7657265  240 SHADCDRRSRIEALELL 256
Cdd:COG0666 273 LALLLLAAALLDLLTLL 289
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
477-577 6.56e-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: 54.57  E-value: 6.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  477 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 556
Cdd:COG0666 113 VNARDKDGETPLHLAAYNG---------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL--------EIV 169

                        90       100
                ....*....|....*....|.
gi 7657265  557 ISLVEAGAHTDMTNKQNKTPL 577
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPL 190
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-256 9.84e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 9.84e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    4 LAGYVYKAASEGKVLTLAALLLNRSESDIRYLLG---YVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYrvqtqqtgtVR 80
Cdd:COG0666  42 LALLALALADALGALLLLAAALAGDLLVALLLLAagaDINAKDDGGNTLLHAAARNGDLEIVKLLLEAG---------AD 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   81 FDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMI 160
Cdd:COG0666 113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  161 AAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL 239
Cdd:COG0666 193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLnAKDKDGLTALLLAAAAGAALIVKLLL 272

                       250
                ....*....|....*..
gi 7657265  240 SHADCDRRSRIEALELL 256
Cdd:COG0666 273 LALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
158-247 4.48e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 4.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    158 LMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKwRAAIVVNGHGMTPLKVAAESCKADVVEL 237
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 7657265    238 LLSH-ADCDRR 247
Cdd:pfam12796  80 LLEKgADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 47-243 3.53e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 3.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    47 STPLIIAARNGHA-----KVVRLLLEHyrvqtqqtgTVRFDGYVIDGATALWCAAGA--GHFEVVKLLVSHGANVNHTTV 119
Cdd:PHA03100  69 STPLHYLSNIKYNltdvkEIVKLLLEY---------GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   120 TNSTPLRAA--CFDGRLDIVKYLVENNANISIANKydntclmiaaykghtdvVRYLLEQRADPNAKAHCGATALHFAAEA 197
Cdd:PHA03100 140 DGENLLHLYleSNKIDLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYN 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 7657265   198 GHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSHAD 243
Cdd:PHA03100 203 NNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 38-227 3.79e-08

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: 56.56  E-value: 3.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   38 YVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYRVQTQQTGTVrfdgyvidGATALWCAAGAGHFEVVKLLVSHGANVNHT 117
Cdd:cd22192   9 HLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGAL--------GETALHVAALYDNLEAAVVLMEAAPELVNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  118 TVTNS-----TPLRAACFDGRLDIVKYLVENNANISIAN--------KYDNTC------LMIAAYKGHTDVVRYLLEQRA 178
Cdd:cd22192  81 PMTSDlyqgeTALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpGPKNLIyygehpLSFAACVGNEEIVRLLIEHGA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657265  179 DPNAKAHCGATALH---------FAAEAghIDIV----KELIKWRAAIVVNGHGMTPLKVAA 227
Cdd:cd22192 161 DIRAQDSLGNTVLHilvlqpnktFACQM--YDLIlsydKEDDLQPLDLVPNNQGLTPFKLAA 220
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-577 6.56e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 6.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  477 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 556
Cdd:COG0666 113 VNARDKDGETPLHLAAYNG---------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL--------EIV 169

                        90       100
                ....*....|....*....|.
gi 7657265  557 ISLVEAGAHTDMTNKQNKTPL 577
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPL 190
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 11-239 9.01e-07

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: 52.01  E-value: 9.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265     11 AASEGKVLTLAALLLNRSEsdirylLGYVSQQggqrstpLIIAARNGHAKVVRLLLEHYRVQTQQTGTVRfdgYVID--- 87
Cdd:TIGR00870  59 AAIENENLELTELLLNLSC------RGAVGDT-------LLHAISLEYVDAVEAILLHLLAAFRKSGPLE---LANDqyt 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265     88 -----GATALWCAAGAGHFEVVKLLVSHGANVN------------HTTVTNSTPLR---AACFdGRLDIVKYLVENNANI 147
Cdd:TIGR00870 123 seftpGITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFYHGESPlnaAACL-GSPSIVALLSEDPADI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    148 SIANKYDNTCLMIAAYKGhtdvvryllEQRADPNAKA-HCGATALHFAAeagHIDIVKELikwraAIVVNGHGMTPLKVA 226
Cdd:TIGR00870 202 LTADSLGNTLLHLLVMEN---------EFKAEYEELScQMYNFALSLLD---KLRDSKEL-----EVILNHQGLTPLKLA 264

                         250
                  ....*....|...
gi 7657265    227 AESCKADVVELLL 239
Cdd:TIGR00870 265 AKEGRIVLFRLKL 277
PHA03095 PHA03095
ankyrin-like protein; Provisional
 475-613 2.97e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   475 IHLDPRTREGFTLLHLAVNSNTPVDdfhtndvcsfpnalVTKLLLDCGAEVNAVDNEGNSALHIivqYnrpISDFLTLHS 554
Cdd:PHA03095  74 ADVNAPERCGFTPLHLYLYNATTLD--------------VIKLLIKAGADVNAKDKVGRTPLHV---Y---LSGFNINPK 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657265   555 IIISLVEAGAHTDMTNKQNKTPLDK--STTGVSEILLKtqmkmsLKCLAARAVRANDINYQ 613
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLR------LLIDAGADVYAVDDRFR 188
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 153-182 2.61e-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: 38.34  E-value: 2.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 7657265     153 YDNTCLMIAAYKGHTDVVRYLLEQRADPNA 182
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
518-578 5.96e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 5.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657265    518 LLDCG-AEVNAVDNEGNSALHIIVQYNRPIsdfltlhsIIISLVEAGAHTDMTNKQNKTPLD 578
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALE--------IVRVLLAYGVDLNLKDEEGLTALD 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-256 9.84e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 9.84e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    4 LAGYVYKAASEGKVLTLAALLLNRSESDIRYLLG---YVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYrvqtqqtgtVR 80
Cdd:COG0666  42 LALLALALADALGALLLLAAALAGDLLVALLLLAagaDINAKDDGGNTLLHAAARNGDLEIVKLLLEAG---------AD 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   81 FDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMI 160
Cdd:COG0666 113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  161 AAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL 239
Cdd:COG0666 193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLnAKDKDGLTALLLAAAAGAALIVKLLL 272

                       250
                ....*....|....*..
gi 7657265  240 SHADCDRRSRIEALELL 256
Cdd:COG0666 273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
48-266 2.19e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 2.19e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   48 TPLIIAARNGHAKVVRLLLEHYRVQTQQTgtvrfdgyvIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRA 127
Cdd:COG0666  56 LLLLAAALAGDLLVALLLLAAGADINAKD---------DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  128 ACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELI 207
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  208 KWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSHADCDRRSRIEALELLGASFANDREN 266
Cdd:COG0666 207 EAGADVnAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-271 1.36e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 1.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   95 AAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLL 174
Cdd:COG0666  28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  175 EQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-ADCDRRSRIEA 252
Cdd:COG0666 108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAgADVNARDNDGE 187

                       170
                ....*....|....*....
gi 7657265  253 LELLGASFANdreNYDIIK 271
Cdd:COG0666 188 TPLHLAAENG---HLEIVK 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
158-247 4.48e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 4.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    158 LMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKwRAAIVVNGHGMTPLKVAAESCKADVVEL 237
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 7657265    238 LLSH-ADCDRR 247
Cdd:pfam12796  80 LLEKgADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-216 6.60e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 6.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    125 LRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQrADPNAKAHcGATALHFAAEAGHIDIVK 204
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 7657265    205 ELIKWRAAIVVN 216
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
92-183 1.22e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265     92 LWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVEnNANISIANkYDNTCLMIAAYKGHTDVVR 171
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 7657265    172 YLLEQRADPNAK 183
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 47-243 3.53e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 3.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    47 STPLIIAARNGHA-----KVVRLLLEHyrvqtqqtgTVRFDGYVIDGATALWCAAGA--GHFEVVKLLVSHGANVNHTTV 119
Cdd:PHA03100  69 STPLHYLSNIKYNltdvkEIVKLLLEY---------GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   120 TNSTPLRAA--CFDGRLDIVKYLVENNANISIANKydntclmiaaykghtdvVRYLLEQRADPNAKAHCGATALHFAAEA 197
Cdd:PHA03100 140 DGENLLHLYleSNKIDLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYN 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 7657265   198 GHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSHAD 243
Cdd:PHA03100 203 NNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-151 1.07e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265     50 LIIAARNGHAKVVRLLLEHyrvqtqqtgTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHgANVNHTTvTNSTPLRAAC 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN---------GADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAA 69

                          90       100
                  ....*....|....*....|..
gi 7657265    130 FDGRLDIVKYLVENNANISIAN 151
Cdd:pfam12796  70 RSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-265 5.98e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.68  E-value: 5.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  101 FEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADP 180
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  181 NAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-ADCDRRSRIEALELLGA 258
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDNDGNTPLHLA 160


                ....*..
gi 7657265  259 SFANDRE 265
Cdd:COG0666 161 AANGNLE 167
Ank_2 pfam12796
Ankyrin repeats (3 copies);
11-117 7.69e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 7.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265     11 AASEGKVLTLAALLLNRSESDIRYLLGYvsqqggqrsTPLIIAARNGHAKVVRLLLEHYRVQTQQtgtvrfdgyviDGAT 90
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGR---------TALHLAAKNGHLEIVKLLLEHADVNLKD-----------NGRT 63

                          90       100
                  ....*....|....*....|....*..
gi 7657265     91 ALWCAAGAGHFEVVKLLVSHGANVNHT 117
Cdd:pfam12796  64 ALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 59-226 2.70e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 2.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    59 AKVVRLLLEH---YRVQTQQTGTvrfdgyvidgaTALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLD 135
Cdd:PHA02878 147 AEITKLLLSYgadINMKDRHKGN-----------TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKP 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   136 IVKYLVENNANISIANKYDNTCLMIA-AYKGHTDVVRYLLEQRADPNAKAHC-GATALHFAAEAGhiDIVKELIKWRAAI 213
Cdd:PHA02878 216 IVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSE--RKLKLLLEYGADI 293

                        170
                 ....*....|....
gi 7657265   214 -VVNGHGMTPLKVA 226
Cdd:PHA02878 294 nSLNSYKLTPLSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 102-249 1.37e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.05  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   102 EVVKLLVSHGANVNHTTVTNSTPLRA-ACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAyKG---HTDVVRYLLEQR 177
Cdd:PHA03095  64 DIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYL-SGfniNPKVIRLLLRKG 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7657265   178 ADPNAKAHCGATALHFAAEAGHIDI--VKELIKWRAAIV-VNGHGMTPLKVAAESCK--ADVVELLLShADCDRRSR 249
Cdd:PHA03095 143 ADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYaVDDRFRSLLHHHLQSFKprARIVRELIR-AGCDPAAT 218
Ank_4 pfam13637
Ankyrin repeats (many copies);
155-207 5.52e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 5.52e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7657265    155 NTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELI 207
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-239 5.59e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.15  E-value: 5.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   102 EVVKLLVSHGANVNHTTVTNSTPL-----RAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYK--GHTDVVRYLL 174
Cdd:PHA03100  49 DVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   175 EQRADPNAKAHCGATALHFAAEAGHID--IVKELIKWRAAI-----------------VVNGHGMTPLKVAAESCKADVV 235
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDInaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFV 208


                 ....
gi 7657265   236 ELLL 239
Cdd:PHA03100 209 KYLL 212
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 49-241 1.60e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    49 PLIIAARNGHAKVVRLLL--------------EHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANV 114
Cdd:PHA02874  71 PLLTAIKIGAHDIIKLLIdngvdtsilpipciEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADV 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   115 NHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFA 194
Cdd:PHA02874 151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 7657265   195 AEAGHiDIVKELIKWRAAIVVNGHGMTPLKVAAE-SCKADVVELLLSH 241
Cdd:PHA02874 231 IIHNR-SAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYH 277
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 85-243 1.74e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    85 VIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISI--------------- 149
Cdd:PHA02874  32 VDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpipciekdmiktil 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   150 --------ANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRA-AIVVNGHGM 220
Cdd:PHA02874 112 dcgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyANVKDNNGE 191

                        170       180
                 ....*....|....*....|...
gi 7657265   221 TPLKVAAESCKADVVELLLSHAD 243
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGN 214
PHA03095 PHA03095
ankyrin-like protein; Provisional
 101-249 2.38e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   101 FEVVKLLVSHGANVNHTTVTNSTPL----RAACFDgRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHT-DVVRYLLE 175
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLhlylHYSSEK-VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7657265   176 QRADPNAKAHCGATALH--FAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAES--CKADVVELLLShADCDRRSR 249
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVnALDLYGMTPLAVLLKSrnANVELLRLLID-AGADVYAV 183
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-208 2.99e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 2.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    48 TPLIIAARNGHAKVVRLLLEhyrvqtqqTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRA 127
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLD--------LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   128 ACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCG-ATALHFAAEAGHIDIVKEL 206
Cdd:PHA02875 142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLF 221


                 ..
gi 7657265   207 IK 208
Cdd:PHA02875 222 IK 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-174 1.43e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 1.43e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 7657265    121 NSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLL 174
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 85-264 1.57e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    85 VIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANIS-IANKYDNTCLMIAAY 163
Cdd:PHA02875  32 IYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATI 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   164 KGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL-SH 241
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLdIEDCCGCTPLIIAMAKGDIAICKMLLdSG 191

                        170       180
                 ....*....|....*....|...
gi 7657265   242 ADCDRRSRIEALELLGASFANDR 264
Cdd:PHA02875 192 ANIDYFGKNGCVAALCYAIENNK 214
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-242 2.59e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.54  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    86 IDGATALWCAAGAGH-FEVVKLLVSHGANVNHTTVTNSTPL-RAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAY 163
Cdd:PHA02876 305 IKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLhQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAV 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   164 KGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDI-VKELIKwRAAIV--VNGHGMTPLKVAAE-SCKADVVELLL 239
Cdd:PHA02876 385 RNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLID-RGANVnsKNKDLSTPLHYACKkNCKLDVIEMLL 463


                 ...
gi 7657265   240 SHA 242
Cdd:PHA02876 464 DNG 466
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 162-245 4.44e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 4.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   162 AYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRA-AIVVNGHGMTPLKVAAESCKADVVELLLS 240
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAdPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                 ....*
gi 7657265   241 HADCD 245
Cdd:PTZ00322 170 HSQCH 174
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 101-182 1.81e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   101 FEVVKLLVSHGANVNHTTVTN----------------STPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYK 164
Cdd:PHA03100 156 LKILKLLIDKGVDINAKNRVNyllsygvpinikdvygFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235

                         90
                 ....*....|....*...
gi 7657265   165 GHTDVVRYLLEQRADPNA 182
Cdd:PHA03100 236 NNKEIFKLLLNNGPSIKT 253
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 88-207 9.55e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 9.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    88 GATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNaniSIANKY---DNTCLmiAAYK 164
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFA---SISDPHaagDLLCT--AAKR 632

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 7657265   165 GHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELI 207
Cdd:PLN03192 633 NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
Ank_4 pfam13637
Ankyrin repeats (many copies);
90-141 1.28e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7657265     90 TALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLV 141
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-218 1.74e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.15  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   101 FEVVKLLVSHGANVNHTTVTNSTPLraaC--------FDGRLDIVKYLVENNANISIANKYDNT---CLMIAAYKGHTDV 169
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsnikdYKHMLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEI 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 7657265   170 VRYLLEQRADPNAKAHCGATALHFAAEAGH---IDIVKELIKwrAAIVVNGH 218
Cdd:PHA02798 128 LLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLE--KGVDINTH 177
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 38-227 3.79e-08

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: 56.56  E-value: 3.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   38 YVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYRVQTQQTGTVrfdgyvidGATALWCAAGAGHFEVVKLLVSHGANVNHT 117
Cdd:cd22192   9 HLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGAL--------GETALHVAALYDNLEAAVVLMEAAPELVNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  118 TVTNS-----TPLRAACFDGRLDIVKYLVENNANISIAN--------KYDNTC------LMIAAYKGHTDVVRYLLEQRA 178
Cdd:cd22192  81 PMTSDlyqgeTALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpGPKNLIyygehpLSFAACVGNEEIVRLLIEHGA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657265  179 DPNAKAHCGATALH---------FAAEAghIDIV----KELIKWRAAIVVNGHGMTPLKVAA 227
Cdd:cd22192 161 DIRAQDSLGNTVLHilvlqpnktFACQM--YDLIlsydKEDDLQPLDLVPNNQGLTPFKLAA 220
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-577 6.56e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 6.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  477 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 556
Cdd:COG0666 113 VNARDKDGETPLHLAAYNG---------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL--------EIV 169

                        90       100
                ....*....|....*....|.
gi 7657265  557 ISLVEAGAHTDMTNKQNKTPL 577
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-578 1.12e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 1.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  477 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 556
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANG---------------NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL--------EIV 202

                        90       100
                ....*....|....*....|..
gi 7657265  557 ISLVEAGAHTDMTNKQNKTPLD 578
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALD 224
PHA03095 PHA03095
ankyrin-like protein; Provisional
 102-208 1.23e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.65  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   102 EVVKLLVSHGANVNHTTVTNSTPLRAA---CFDGRLDIVKYLvENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRA 178
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLL-IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281

                         90       100       110
                 ....*....|....*....|....*....|
gi 7657265   179 DPNAKAHCGATALHFAAEAGHIDIVKELIK 208
Cdd:PHA03095 282 DINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-179 1.85e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    48 TPLIIAARNGHAKVVRLLLEHY-RVQTQQtgtvrfdgyvIDGATALWCAAGAGHFEVVKLLVsHGANVNHTTVTNSTpLR 126
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHAcNVHIRD----------ANGNTALWNAISAKHHKIFRILY-HFASISDPHAAGDL-LC 627

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 7657265   127 AACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRAD 179
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA03095 PHA03095
ankyrin-like protein; Provisional
 100-227 2.60e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   100 HFEVVKLLVSHGANVNHTTVTNSTPLraACF----DGRLDIVKYLVENNANISIANKYDNTCLMIAA--YKGHTDVVRYL 173
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPL--AVLlksrNANVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVREL 208

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 7657265   174 LEQRADPNAKAHCGATALHFAAEAG---HIDIVKELIKWRAAIVVNGHGMTPLKVAA 227
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGISINARNRYGQTPLHYAA 265
Ank_5 pfam13857
Ankyrin repeats (many copies);
140-194 2.69e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 2.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 7657265    140 LVEN-NANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFA 194
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 11-239 9.01e-07

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: 52.01  E-value: 9.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265     11 AASEGKVLTLAALLLNRSEsdirylLGYVSQQggqrstpLIIAARNGHAKVVRLLLEHYRVQTQQTGTVRfdgYVID--- 87
Cdd:TIGR00870  59 AAIENENLELTELLLNLSC------RGAVGDT-------LLHAISLEYVDAVEAILLHLLAAFRKSGPLE---LANDqyt 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265     88 -----GATALWCAAGAGHFEVVKLLVSHGANVN------------HTTVTNSTPLR---AACFdGRLDIVKYLVENNANI 147
Cdd:TIGR00870 123 seftpGITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFYHGESPlnaAACL-GSPSIVALLSEDPADI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    148 SIANKYDNTCLMIAAYKGhtdvvryllEQRADPNAKA-HCGATALHFAAeagHIDIVKELikwraAIVVNGHGMTPLKVA 226
Cdd:TIGR00870 202 LTADSLGNTLLHLLVMEN---------EFKAEYEELScQMYNFALSLLD---KLRDSKEL-----EVILNHQGLTPLKLA 264

                         250
                  ....*....|...
gi 7657265    227 AESCKADVVELLL 239
Cdd:TIGR00870 265 AKEGRIVLFRLKL 277
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 95-264 2.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    95 AAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAAC--------------------------------------------- 129
Cdd:PHA02878  44 AVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikdafnnrnveifkiiltn 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   130 -FDGRLD------------------IVKYLVENNANISIANKY-DNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGAT 189
Cdd:PHA02878 124 rYKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7657265   190 ALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKA-DVVELLLSH-ADCDRRSRIEALELLGASFANDR 264
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTdARDKCGNTPLHISVGYCKDyDILKLLLEHgVDVNAKSYILGLTALHSSIKSER 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
466-577 3.04e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.57  E-value: 3.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  466 KINKQIYNLIHLDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRP 545
Cdd:COG0666  69 VALLLLAAGADINAKDDGGNTLLHAAARNG---------------DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                        90       100       110
                ....*....|....*....|....*....|..
gi 7657265  546 isdfltlhSIIISLVEAGAHTDMTNKQNKTPL 577
Cdd:COG0666 134 --------EIVKLLLEAGADVNAQDNDGNTPL 157
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 89-316 3.41e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 3.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    89 ATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTD 168
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   169 VVR--YLLEQRADPnakaHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-ADC 244
Cdd:PLN03192 606 IFRilYHFASISDP----HAAGDLLCTAAKRNDLTAMKELLKQGLNVdSEDHQGATALQVAMAEDHVDMVRLLIMNgADV 681

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657265   245 DRRSRIEALellgaSFANDREnydiiktyhylylaMLERFQDGDNILEKEVLPPIHAYGNRTECRNPQELES 316
Cdd:PLN03192 682 DKANTDDDF-----SPTELRE--------------LLQKRELGHSITIVDSVPADEPDLGRDGGSRPGRLQG 734
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 104-174 5.01e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 5.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657265   104 VKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLL 174
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 87-118 2.38e-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: 41.51  E-value: 2.38e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 7657265     87 DGATALWCAAG-AGHFEVVKLLVSHGANVNHTT 118
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 475-613 2.97e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   475 IHLDPRTREGFTLLHLAVNSNTPVDdfhtndvcsfpnalVTKLLLDCGAEVNAVDNEGNSALHIivqYnrpISDFLTLHS 554
Cdd:PHA03095  74 ADVNAPERCGFTPLHLYLYNATTLD--------------VIKLLIKAGADVNAKDKVGRTPLHV---Y---LSGFNINPK 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657265   555 IIISLVEAGAHTDMTNKQNKTPLDK--STTGVSEILLKtqmkmsLKCLAARAVRANDINYQ 613
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLR------LLIDAGADVYAVDDRFR 188
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-272 5.04e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 5.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    48 TPLIIAARNGHAKVVRLLLEHyrvqtqqtgTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNhttvTNSTPLRA 127
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSY---------GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   128 ACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGH-TDVVRYLLEQRADPNAKAHCGATALHFAAEAGH-IDIVKE 205
Cdd:PHA02876 247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRT 326

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   206 LIKWRAAI-VVNGHGMTPLKVAA--ESCKADVVELLLSHADCDRRSRIEALELlgaSFANDRENYDIIKT 272
Cdd:PHA02876 327 LIMLGADVnAADRLYITPLHQAStlDRNKDIVITLLELGANVNARDYCDKTPI---HYAAVRNNVVIINT 393
Ank_5 pfam13857
Ankyrin repeats (many copies);
173-226 6.83e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 6.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 7657265    173 LLEQR-ADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVA 226
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLnLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
189-239 7.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 7.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7657265    189 TALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL 239
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-108 7.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 7.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657265     46 RSTPLIIAARNGHAKVVRLLLEHyrvqtqqtgTVRFDGYVIDGATALWCAAGAGHFEVVKLLV 108
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK---------GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 83-153 9.17e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.43  E-value: 9.17e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7657265    83 GYVID-----GATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKY 153
Cdd:PHA03100 182 GVPINikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 155-183 1.16e-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: 39.58  E-value: 1.16e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 7657265    155 NTCLMIAAYK-GHTDVVRYLLEQRADPNAK 183
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 153-182 2.61e-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: 38.34  E-value: 2.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 7657265     153 YDNTCLMIAAYKGHTDVVRYLLEQRADPNA 182
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-179 3.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.51  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    48 TPLIIAARNGHAKVVRLLLEH---YRVQTQQTGTVRFdgyvidgatalWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTP 124
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLDYgadIEALSQKIGTALH-----------FALCGTNPYMSVKTLIDRGANVNSKNKDLSTP 445

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 7657265   125 LRAACFDG-RLDIVKYLVENNANISIANKYDNTCLMIAAykGHTDVVRYLLEQRAD 179
Cdd:PHA02876 446 LHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAE 499
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 87-115 4.14e-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: 37.95  E-value: 4.14e-04
                           10        20
                   ....*....|....*....|....*....
gi 7657265      87 DGATALWCAAGAGHFEVVKLLVSHGANVN 115
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-579 4.49e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 42.63  E-value: 4.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  477 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRpisdfltlHSII 556
Cdd:COG0666 179 VNARDNDGETPLHLAAENG---------------HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGN--------LEIV 235

                        90       100
                ....*....|....*....|...
gi 7657265  557 ISLVEAGAHTDMTNKQNKTPLDK 579
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLL 258
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 134-240 6.59e-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: 42.82  E-value: 6.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  134 LDIVKYLVENNANISI---------ANKYD-----NTCLMIAAYKGHTDVVRYLLEQRADPNAKAHC-GATALHFAAEAG 198
Cdd:cd22194 154 GDIVKLLIAKGADVNAhakgvffnpKYKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDITSQDSrGNTVLHALVTVA 233

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7657265  199 -----HIDIVKELI--------KWRAAIVVNGHGMTPLKVAAESCKADVVELLLS 240
Cdd:cd22194 234 edsktQNDFVKRMYdmillkseNKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 134-239 6.71e-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: 6.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  134 LDIVKYLVENNANISIA------NKYDNTC-------LMIAAYKGHTDVVRYLLEQRADP---NAKAHCGATALH---FA 194
Cdd:cd22197 107 LQCVKLLVENGADVHARacgrffQKKQGTCfyfgelpLSLAACTKQWDVVNYLLENPHQPaslQAQDSLGNTVLHalvMI 186

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7657265  195 AE------AGHIDIVKELIKWRAAI--------VVNGHGMTPLKVAAESCKADVVELLL 239
Cdd:cd22197 187 ADnspensALVIKMYDGLLQAGARLcptvqleeISNHEGLTPLKLAAKEGKIEIFRHIL 245
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 20-249 7.59e-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: 42.56  E-value: 7.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   20 LAALLLNRSESDiRYLLGYVSQQGGQRSTPLIIAARNGHAKV---VRLLLEHYRvQTQQTGTVRFDGYV---IDGATALW 93
Cdd:cd21882   1 LEELLGLLECLR-WYLTDSAYQRGATGKTCLHKAALNLNDGVneaIMLLLEAAP-DSGNPKELVNAPCTdefYQGQTALH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   94 CAAGAGHFEVVKLLVSHGANVnHTTVTNST--------------PLRAACFDGRLDIVKYLVENNANISIANKYDNTclm 159
Cdd:cd21882  79 IAIENRNLNLVRLLVENGADV-SARATGRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQDSL--- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  160 iaaykGHTdVVRYLLEQradPNAKAHCGATALHFAAE----AGHIDIVKELikwraAIVVNGHGMTPLKVAAESCKADVV 235
Cdd:cd21882 155 -----GNT-VLHALVLQ---ADNTPENSAFVCQMYNLllsyGAHLDPTQQL-----EEIPNHQGLTPLKLAAVEGKIVMF 220

                       250
                ....*....|....*..
gi 7657265  236 ELLLS---HADCDRRSR 249
Cdd:cd21882 221 QHILQrefSGPYQPLSR 237
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 46-163 1.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    46 RSTPLIIAARNGHAKVVRLLLEHyrvqtqQTGTVRFDGYvidGATALWCAAGAGHFEVVKLLVSHGANVNHttVTNSTPL 125
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIELLIDH------KACLDIEDCC---GCTPLIIAMAKGDIAICKMLLDSGANIDY--FGKNGCV 203

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 7657265   126 RAACF---DGRLDIVKYLVENNA--NI--SIANKYDNTCLMIAAY 163
Cdd:PHA02875 204 AALCYaieNNKIDIVRLFIKRGAdcNImfMIEGEECTILDMICNM 248
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 475-580 1.62e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.10  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   475 IHLDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNrpisdfltLHS 554
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKG---------------DLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN--------FFD 171

                         90       100
                 ....*....|....*....|....*.
gi 7657265   555 IIISLVEAGAHTDMTNKQNKTPLDKS 580
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNA 197
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 134-240 1.68e-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: 1.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265  134 LDIVKYLVENNANISIA-------NKYDNTC-------LMIAAYKGHTDVVRYLLE---QRADPNAKAHCGATALHFAAE 196
Cdd:cd22193  89 GDIVALLVENGADVHAHakgrffqPKYQGEGfyfgelpLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVT 168

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657265  197 AG-----HIDIVKEL--------IKWRAAI----VVNGHGMTPLKVAAESCKADVVELLLS 240
Cdd:cd22193 169 VAdntkeNTKFVTRMydmilirgAKLCPTVeleeIRNNDGLTPLQLAAKMGKIEILKYILQ 229
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 88-208 1.80e-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: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   88 GATALWCAAGAGHFEVVKLLVSHGANVN----------HTTVT---NSTPLRAACFDGRLDIVKYLVENNANISIANKYD 154
Cdd:cd22197  94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQD 173

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657265  155 ---NTCL----MIA-AYKGHTDVVRYLLEQ------RADPNAKA-----HCGATALHFAAEAGHIDIVKELIK 208
Cdd:cd22197 174 slgNTVLhalvMIAdNSPENSALVIKMYDGllqagaRLCPTVQLeeisnHEGLTPLKLAAKEGKIEIFRHILQ 246
PHA03095 PHA03095
ankyrin-like protein; Provisional
 516-585 1.81e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   516 KLLLDCGAEVNAVDNEGNSALHIIVQYNRPISdfltlhSIIISLVEAGAHTDMTNKQNKTPLDKSTTGVS 585
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLHHHLQSFKPRA------RIVRELIRAGCDPAATDMLGNTPLHSMATGSS 234
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 87-116 2.58e-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: 35.70  E-value: 2.58e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 7657265     87 DGATALWCAAGAGHFEVVKLLVSHGANVNH 116
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 465-552 3.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.42  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   465 CKINKQIYNLIHLDPRTREGFTLLHLAVNSNTPvdDFhtndvcsfpnalvTKLLLDCGAEVNAVDNEGNSALHIIVQYNr 544
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNP--EF-------------VKYLLDLGANPNLVNKYGDTPLHIAILNN- 236


                 ....*...
gi 7657265   545 pISDFLTL 552
Cdd:PHA03100 237 -NKEIFKL 243
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 153-182 3.33e-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: 35.31  E-value: 3.33e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 7657265    153 YDNTCLMIAAYKGHTDVVRYLLEQRADPNA 182
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 103-239 3.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   103 VVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYL--------- 173
Cdd:PHA02874  17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsi 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   174 --------------LEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELL 238
Cdd:PHA02874  97 lpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVnIEDDNGCYPIHIAIKHNFFDIIKLL 176


                 .
gi 7657265   239 L 239
Cdd:PHA02874 177 L 177
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 134-216 3.71e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   134 LDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI 213
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237


                 ...
gi 7657265   214 VVN 216
Cdd:PHA02876 238 NKN 240
Ank_5 pfam13857
Ankyrin repeats (many copies);
107-161 5.62e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 5.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 7657265    107 LVSHG-ANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIA 161
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 102-225 5.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265   102 EVVKLLVSHGANVNHTTVTNsTPLRAACFDGRLD------IVKYLVENNANI---SIANKYDNTCLMIAAYKGHTDVVRY 172
Cdd:PHA02989  51 KIVKLLIDNGADVNYKGYIE-TPLCAVLRNREITsnkikkIVKLLLKFGADInlkTFNGVSPIVCFIYNSNINNCDMLRF 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 7657265   173 LLEQRADPNA-KAHCGATALHFAAEAGHI--DIVKELIKWRAAIV--VNGHGMTPLKV 225
Cdd:PHA02989 130 LLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFGVNLFekTSLYGLTPMNI 187
Ank_5 pfam13857
Ankyrin repeats (many copies);
518-578 5.96e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 5.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657265    518 LLDCG-AEVNAVDNEGNSALHIIVQYNRPIsdfltlhsIIISLVEAGAHTDMTNKQNKTPLD 578
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALE--------IVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 54-140 9.24e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 9.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657265    54 ARNGHAKVVRLLLehyrvqtqqTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGR 133
Cdd:PTZ00322  90 AASGDAVGARILL---------TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160


                 ....*..
gi 7657265   134 LDIVKYL 140
Cdd:PTZ00322 161 REVVQLL 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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