NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157823075|ref|NP_001101627|]
View 

protein fem-1 homolog B [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-256 1.14e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 1.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075   4 LAGYVYKAASEGKVLTLAALLLNRSESDIRYLLG---YVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYrvqtqqtgtVR 80
Cdd:COG0666   42 LALLALALADALGALLLLAAALAGDLLVALLLLAagaDINAKDDGGNTLLHAAARNGDLEIVKLLLEAG---------AD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  81 FDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMI 160
Cdd:COG0666  113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 161 AAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL 239
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLnAKDKDGLTALLLAAAAGAALIVKLLL 272

                        250
                 ....*....|....*..
gi 157823075 240 SHADCDRRSRIEALELL 256
Cdd:COG0666  273 LALLLLAAALLDLLTLL 289
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
477-577 6.86e-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: 6.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 477 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 556
Cdd:COG0666  113 VNARDKDGETPLHLAAYNG---------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL--------EIV 169

                         90       100
                 ....*....|....*....|.
gi 157823075 557 ISLVEAGAHTDMTNKQNKTPL 577
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPL 190
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-256 1.14e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 1.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075   4 LAGYVYKAASEGKVLTLAALLLNRSESDIRYLLG---YVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYrvqtqqtgtVR 80
Cdd:COG0666   42 LALLALALADALGALLLLAAALAGDLLVALLLLAagaDINAKDDGGNTLLHAAARNGDLEIVKLLLEAG---------AD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  81 FDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMI 160
Cdd:COG0666  113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 161 AAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL 239
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLnAKDKDGLTALLLAAAAGAALIVKLLL 272

                        250
                 ....*....|....*..
gi 157823075 240 SHADCDRRSRIEALELL 256
Cdd:COG0666  273 LALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
158-247 4.75e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 4.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  158 LMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKwRAAIVVNGHGMTPLKVAAESCKADVVEL 237
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 157823075  238 LLSH-ADCDRR 247
Cdd:pfam12796  80 LLEKgADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 47-243 1.82e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  47 STPLIIAARNGHA-----KVVRLLLEHyrvqtqqtgTVRFDGYVIDGATALWCAAGA--GHFEVVKLLVSHGANVNHTTV 119
Cdd:PHA03100  69 STPLHYLSNIKYNltdvkEIVKLLLEY---------GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 120 TNSTPLRAA--CFDGRLDIVKYLVENNANISIANKydntclmiaaykghtdvVRYLLEQRADPNAKAHCGATALHFAAEA 197
Cdd:PHA03100 140 DGENLLHLYleSNKIDLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYN 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157823075 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 3.89e-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: 56.17  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  38 YVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYRVQTQQTGTVrfdgyvidGATALWCAAGAGHFEVVKLLVSHGANVNHT 117
Cdd:cd22192    9 HLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGAL--------GETALHVAALYDNLEAAVVLMEAAPELVNE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 118 TVTNS-----TPLRAACFDGRLDIVKYLVENNANISIAN--------KYDNTC------LMIAAYKGHTDVVRYLLEQRA 178
Cdd:cd22192   81 PMTSDlyqgeTALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpGPKNLIyygehpLSFAACVGNEEIVRLLIEHGA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823075 179 DPNAKAHCGATALH---------FAAEAghIDIV----KELIKWRAAIVVNGHGMTPLKVAA 227
Cdd:cd22192  161 DIRAQDSLGNTVLHilvlqpnktFACQM--YDLIlsydKEDDLQPLDLVPNNQGLTPFKLAA 220
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-577 6.86e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 6.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 477 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 556
Cdd:COG0666  113 VNARDKDGETPLHLAAYNG---------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL--------EIV 169

                         90       100
                 ....*....|....*....|.
gi 157823075 557 ISLVEAGAHTDMTNKQNKTPL 577
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPL 190
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 11-239 9.40e-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: 9.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075   11 AASEGKVLTLAALLLNRSEsdirylLGYVSQQggqrstpLIIAARNGHAKVVRLLLEHYRVQTQQTGTVRfdgYVID--- 87
Cdd:TIGR00870  59 AAIENENLELTELLLNLSC------RGAVGDT-------LLHAISLEYVDAVEAILLHLLAAFRKSGPLE---LANDqyt 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075   88 -----GATALWCAAGAGHFEVVKLLVSHGANVN------------HTTVTNSTPLR---AACFdGRLDIVKYLVENNANI 147
Cdd:TIGR00870 123 seftpGITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFYHGESPlnaAACL-GSPSIVALLSEDPADI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  148 SIANKYDNTCLMIAAYKGhtdvvryllEQRADPNAKA-HCGATALHFAAeagHIDIVKELikwraAIVVNGHGMTPLKVA 226
Cdd:TIGR00870 202 LTADSLGNTLLHLLVMEN---------EFKAEYEELScQMYNFALSLLD---KLRDSKEL-----EVILNHQGLTPLKLA 264

                         250
                  ....*....|...
gi 157823075  227 AESCKADVVELLL 239
Cdd:TIGR00870 265 AKEGRIVLFRLKL 277
PHA03095 PHA03095
ankyrin-like protein; Provisional
 475-613 3.21e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 475 IHLDPRTREGFTLLHLAVNSNTPVDdfhtndvcsfpnalVTKLLLDCGAEVNAVDNEGNSALHIivqYnrpISDFLTLHS 554
Cdd:PHA03095  74 ADVNAPERCGFTPLHLYLYNATTLD--------------VIKLLIKAGADVNAKDKVGRTPLHV---Y---LSGFNINPK 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823075 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 2.56e-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: 2.56e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 157823075   153 YDNTCLMIAAYKGHTDVVRYLLEQRADPNA 182
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
518-578 6.33e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 6.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823075  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 1.14e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 1.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075   4 LAGYVYKAASEGKVLTLAALLLNRSESDIRYLLG---YVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYrvqtqqtgtVR 80
Cdd:COG0666   42 LALLALALADALGALLLLAAALAGDLLVALLLLAagaDINAKDDGGNTLLHAAARNGDLEIVKLLLEAG---------AD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  81 FDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMI 160
Cdd:COG0666  113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 161 AAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL 239
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLnAKDKDGLTALLLAAAAGAALIVKLLL 272

                        250
                 ....*....|....*..
gi 157823075 240 SHADCDRRSRIEALELL 256
Cdd:COG0666  273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
48-271 1.86e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 1.86e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  48 TPLIIAARNGHAKVVRLLLEHYRVQTQQTgtvrfdgyvIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRA 127
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKD---------DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 128 ACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELI 207
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823075 208 KWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-ADCDRRSRIEALELLGASFANDRENYDIMK 271
Cdd:COG0666  207 EAGADVnAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-265 1.68e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 1.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  95 AAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLL 174
Cdd:COG0666   28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 175 EQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-ADCDRRSRIEA 252
Cdd:COG0666  108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAgADVNARDNDGE 187

                        170
                 ....*....|...
gi 157823075 253 LELLGASFANDRE 265
Cdd:COG0666  188 TPLHLAAENGHLE 200
Ank_2 pfam12796
Ankyrin repeats (3 copies);
158-247 4.75e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 4.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  158 LMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKwRAAIVVNGHGMTPLKVAAESCKADVVEL 237
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 157823075  238 LLSH-ADCDRR 247
Cdd:pfam12796  80 LLEKgADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-216 7.00e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 7.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  125 LRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQrADPNAKAHcGATALHFAAEAGHIDIVK 204
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 157823075  205 ELIKWRAAIVVN 216
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
92-183 1.27e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075   92 LWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVEnNANISIANkYDNTCLMIAAYKGHTDVVR 171
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 157823075  172 YLLEQRADPNAK 183
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 47-243 1.82e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  47 STPLIIAARNGHA-----KVVRLLLEHyrvqtqqtgTVRFDGYVIDGATALWCAAGA--GHFEVVKLLVSHGANVNHTTV 119
Cdd:PHA03100  69 STPLHYLSNIKYNltdvkEIVKLLLEY---------GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 120 TNSTPLRAA--CFDGRLDIVKYLVENNANISIANKydntclmiaaykghtdvVRYLLEQRADPNAKAHCGATALHFAAEA 197
Cdd:PHA03100 140 DGENLLHLYleSNKIDLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYN 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157823075 198 GHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSHAD 243
Cdd:PHA03100 203 NNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-151 1.13e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075   50 LIIAARNGHAKVVRLLLEHyrvqtqqtgTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHgANVNHTTvTNSTPLRAAC 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN---------GADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAA 69

                          90       100
                  ....*....|....*....|..
gi 157823075  130 FDGRLDIVKYLVENNANISIAN 151
Cdd:pfam12796  70 RSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-265 6.62e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.68  E-value: 6.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 101 FEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADP 180
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 181 NAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-ADCDRRSRIEALELLGA 258
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDNDGNTPLHLA 160


                 ....*..
gi 157823075 259 SFANDRE 265
Cdd:COG0666  161 AANGNLE 167
Ank_2 pfam12796
Ankyrin repeats (3 copies);
11-117 8.15e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 8.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075   11 AASEGKVLTLAALLLNRSESDIRYLLGYvsqqggqrsTPLIIAARNGHAKVVRLLLEHYRVQTQQtgtvrfdgyviDGAT 90
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGR---------TALHLAAKNGHLEIVKLLLEHADVNLKD-----------NGRT 63

                          90       100
                  ....*....|....*....|....*..
gi 157823075   91 ALWCAAGAGHFEVVKLLVSHGANVNHT 117
Cdd:pfam12796  64 ALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 59-226 1.93e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 1.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  59 AKVVRLLLEH---YRVQTQQTGTvrfdgyvidgaTALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLD 135
Cdd:PHA02878 147 AEITKLLLSYgadINMKDRHKGN-----------TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKP 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 136 IVKYLVENNANISIANKYDNTCLMIA-AYKGHTDVVRYLLEQRADPNAKAHC-GATALHFAAEAGhiDIVKELIKWRAAI 213
Cdd:PHA02878 216 IVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSE--RKLKLLLEYGADI 293

                        170
                 ....*....|....
gi 157823075 214 -VVNGHGMTPLKVA 226
Cdd:PHA02878 294 nSLNSYKLTPLSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 102-249 1.45e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.05  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 102 EVVKLLVSHGANVNHTTVTNSTPLRA-ACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAyKG---HTDVVRYLLEQR 177
Cdd:PHA03095  64 DIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYL-SGfniNPKVIRLLLRKG 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823075 178 ADPNAKAHCGATALHFAAEAGHIDI--VKELIKWRAAIV-VNGHGMTPLKVAAESCK--ADVVELLLShADCDRRSR 249
Cdd:PHA03095 143 ADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYaVDDRFRSLLHHHLQSFKprARIVRELIR-AGCDPAAT 218
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-239 3.44e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 3.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 102 EVVKLLVSHGANVNHTTVTNSTPL-----RAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYK--GHTDVVRYLL 174
Cdd:PHA03100  49 DVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 175 EQRADPNAKAHCGATALHFAAEAGHID--IVKELIKWRAAI-----------------VVNGHGMTPLKVAAESCKADVV 235
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDInaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFV 208


                 ....
gi 157823075 236 ELLL 239
Cdd:PHA03100 209 KYLL 212
Ank_4 pfam13637
Ankyrin repeats (many copies);
155-207 6.45e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 6.45e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157823075  155 NTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELI 207
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 49-241 1.07e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.30  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  49 PLIIAARNGHAKVVRLLL--------------EHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANV 114
Cdd:PHA02874  71 PLLTAIKIGAHDIIKLLIdngvdtsilpipciEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADV 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 115 NHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFA 194
Cdd:PHA02874 151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157823075 195 AEAGHiDIVKELIKWRAAIVVNGHGMTPLKVAAE-SCKADVVELLLSH 241
Cdd:PHA02874 231 IIHNR-SAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYH 277
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 85-243 1.36e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  85 VIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISI--------------- 149
Cdd:PHA02874  32 VDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpipciekdmiktil 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 150 --------ANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRA-AIVVNGHGM 220
Cdd:PHA02874 112 dcgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyANVKDNNGE 191

                        170       180
                 ....*....|....*....|...
gi 157823075 221 TPLKVAAESCKADVVELLLSHAD 243
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGN 214
PHA03095 PHA03095
ankyrin-like protein; Provisional
 101-366 1.43e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 101 FEVVKLLVSHGANVNHTTVTNSTPL----RAACFDgRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHT-DVVRYLLE 175
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLhlylHYSSEK-VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 176 QRADPNAKAHCGATALH--FAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVaaesckadvvelLLSHADCDrrsrIEA 252
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVnALDLYGMTPLAV------------LLKSRNAN----VEL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 253 LELLGASFANDRENYDIMKT-YHYlylaMLERFQDGDNILEKEVLPPIHAYGNRTECRNPQELEAIRQDRDALHMEGLIv 331
Cdd:PHA03095 170 LRLLIDAGADVYAVDDRFRSlLHH----HLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLL- 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 157823075 332 rerilgADNIDVS------HPIIYRGAVYADNMEFEQCIKL 366
Cdd:PHA03095 245 ------IAGISINarnrygQTPLHYAAVFNNPRACRRLIAL 279
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-208 3.02e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 3.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  48 TPLIIAARNGHAKVVRLLLEhyrvqtqqTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRA 127
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLD--------LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 128 ACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCG-ATALHFAAEAGHIDIVKEL 206
Cdd:PHA02875 142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLF 221


                 ..
gi 157823075 207 IK 208
Cdd:PHA02875 222 IK 223
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 157823075  85 VIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANIS-IANKYDNTCLMIAAY 163
Cdd:PHA02875  32 IYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATI 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 164 KGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL-SH 241
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLdIEDCCGCTPLIIAMAKGDIAICKMLLdSG 191

                        170       180
                 ....*....|....*....|...
gi 157823075 242 ADCDRRSRIEALELLGASFANDR 264
Cdd:PHA02875 192 ANIDYFGKNGCVAALCYAIENNK 214
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-174 1.64e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 1.64e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157823075  121 NSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLL 174
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-242 1.93e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  86 IDGATALWCAAGAGH-FEVVKLLVSHGANVNHTTVTNSTPL-RAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAY 163
Cdd:PHA02876 305 IKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLhQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAV 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 164 KGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDI-VKELIKwRAAIV--VNGHGMTPLKVAAE-SCKADVVELLL 239
Cdd:PHA02876 385 RNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLID-RGANVnsKNKDLSTPLHYACKkNCKLDVIEMLL 463


                 ...
gi 157823075 240 SHA 242
Cdd:PHA02876 464 DNG 466
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 162-245 4.52e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 162 AYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRA-AIVVNGHGMTPLKVAAESCKADVVELLLS 240
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAdPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                 ....*
gi 157823075 241 HADCD 245
Cdd:PTZ00322 170 HSQCH 174
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 12-182 1.25e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  12 ASEGKVLTLAALLLNRSesdiryllGYVSQQGGQRSTPLIIAARN--GHAKVVRLLLEHyrvqTQQTGTVRFDGYvidga 89
Cdd:PHA03100  80 YNLTDVKEIVKLLLEYG--------ANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN----GANVNIKNSDGE----- 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  90 TALWCAAGAGH--FEVVKLLVSHGANVNHTTVTN----------------STPLRAACFDGRLDIVKYLVENNANISIAN 151
Cdd:PHA03100 143 NLLHLYLESNKidLKILKLLIDKGVDINAKNRVNyllsygvpinikdvygFTPLHYAVYNNNPEFVKYLLDLGANPNLVN 222

                        170       180       190
                 ....*....|....*....|....*....|.
gi 157823075 152 KYDNTCLMIAAYKGHTDVVRYLLEQRADPNA 182
Cdd:PHA03100 223 KYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 88-207 1.03e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  88 GATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNaniSIANKY---DNTCLmiAAYK 164
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFA---SISDPHaagDLLCT--AAKR 632

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157823075 165 GHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELI 207
Cdd:PLN03192 633 NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-218 1.21e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.92  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 101 FEVVKLLVSHGANVNHTTVTNSTPLraaC--------FDGRLDIVKYLVENNANISIANKYDNT---CLMIAAYKGHTDV 169
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsnikdYKHMLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEI 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157823075 170 VRYLLEQRADPNAKAHCGATALHFAAEAGH---IDIVKELIKwrAAIVVNGH 218
Cdd:PHA02798 128 LLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLE--KGVDINTH 177
Ank_4 pfam13637
Ankyrin repeats (many copies);
90-141 1.44e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157823075   90 TALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLV 141
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 38-227 3.89e-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: 56.17  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  38 YVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYRVQTQQTGTVrfdgyvidGATALWCAAGAGHFEVVKLLVSHGANVNHT 117
Cdd:cd22192    9 HLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGAL--------GETALHVAALYDNLEAAVVLMEAAPELVNE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 118 TVTNS-----TPLRAACFDGRLDIVKYLVENNANISIAN--------KYDNTC------LMIAAYKGHTDVVRYLLEQRA 178
Cdd:cd22192   81 PMTSDlyqgeTALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpGPKNLIyygehpLSFAACVGNEEIVRLLIEHGA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823075 179 DPNAKAHCGATALH---------FAAEAghIDIV----KELIKWRAAIVVNGHGMTPLKVAA 227
Cdd:cd22192  161 DIRAQDSLGNTVLHilvlqpnktFACQM--YDLIlsydKEDDLQPLDLVPNNQGLTPFKLAA 220
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-577 6.86e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 6.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 477 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 556
Cdd:COG0666  113 VNARDKDGETPLHLAAYNG---------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL--------EIV 169

                         90       100
                 ....*....|....*....|.
gi 157823075 557 ISLVEAGAHTDMTNKQNKTPL 577
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-578 1.14e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 477 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPisdfltlhSII 556
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANG---------------NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL--------EIV 202

                         90       100
                 ....*....|....*....|..
gi 157823075 557 ISLVEAGAHTDMTNKQNKTPLD 578
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALD 224
PHA03095 PHA03095
ankyrin-like protein; Provisional
 102-208 1.26e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.65  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 102 EVVKLLVSHGANVNHTTVTNSTPLRAA---CFDGRLDIVKYLvENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRA 178
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLL-IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281

                         90       100       110
                 ....*....|....*....|....*....|
gi 157823075 179 DPNAKAHCGATALHFAAEAGHIDIVKELIK 208
Cdd:PHA03095 282 DINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-179 2.06e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  48 TPLIIAARNGHAKVVRLLLEHY-RVQTQQtgtvrfdgyvIDGATALWCAAGAGHFEVVKLLVsHGANVNHTTVTNSTpLR 126
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHAcNVHIRD----------ANGNTALWNAISAKHHKIFRILY-HFASISDPHAAGDL-LC 627

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157823075 127 AACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRAD 179
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA03095 PHA03095
ankyrin-like protein; Provisional
 100-227 2.64e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 2.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 100 HFEVVKLLVSHGANVNHTTVTNSTPLraACF----DGRLDIVKYLVENNANISIANKYDNTCLMIAA--YKGHTDVVRYL 173
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPL--AVLlksrNANVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVREL 208

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823075 174 LEQRADPNAKAHCGATALHFAAEAG---HIDIVKELIKWRAAIVVNGHGMTPLKVAA 227
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGISINARNRYGQTPLHYAA 265
Ank_5 pfam13857
Ankyrin repeats (many copies);
140-194 2.85e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 2.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157823075  140 LVEN-NANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFA 194
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 11-239 9.40e-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: 9.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075   11 AASEGKVLTLAALLLNRSEsdirylLGYVSQQggqrstpLIIAARNGHAKVVRLLLEHYRVQTQQTGTVRfdgYVID--- 87
Cdd:TIGR00870  59 AAIENENLELTELLLNLSC------RGAVGDT-------LLHAISLEYVDAVEAILLHLLAAFRKSGPLE---LANDqyt 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075   88 -----GATALWCAAGAGHFEVVKLLVSHGANVN------------HTTVTNSTPLR---AACFdGRLDIVKYLVENNANI 147
Cdd:TIGR00870 123 seftpGITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFYHGESPlnaAACL-GSPSIVALLSEDPADI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  148 SIANKYDNTCLMIAAYKGhtdvvryllEQRADPNAKA-HCGATALHFAAeagHIDIVKELikwraAIVVNGHGMTPLKVA 226
Cdd:TIGR00870 202 LTADSLGNTLLHLLVMEN---------EFKAEYEELScQMYNFALSLLD---KLRDSKEL-----EVILNHQGLTPLKLA 264

                         250
                  ....*....|...
gi 157823075  227 AESCKADVVELLL 239
Cdd:TIGR00870 265 AKEGRIVLFRLKL 277
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 95-264 1.39e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.03  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  95 AAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAAC--------------------------------------------- 129
Cdd:PHA02878  44 AVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikdafnnrnveifkiiltn 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 130 -FDGRLD------------------IVKYLVENNANISIANKY-DNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGAT 189
Cdd:PHA02878 124 rYKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823075 190 ALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKA-DVVELLLSH-ADCDRRSRIEALELLGASFANDR 264
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTdARDKCGNTPLHISVGYCKDyDILKLLLEHgVDVNAKSYILGLTALHSSIKSER 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
467-577 3.44e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.18  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 467 INKQIYNLIHLDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPi 546
Cdd:COG0666   70 ALLLLAAGADINAKDDGGNTLLHAAARNG---------------DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL- 133

                         90       100       110
                 ....*....|....*....|....*....|.
gi 157823075 547 sdfltlhSIIISLVEAGAHTDMTNKQNKTPL 577
Cdd:COG0666  134 -------EIVKLLLEAGADVNAQDNDGNTPL 157
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 104-174 4.80e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 4.80e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823075 104 VKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLL 174
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 89-315 6.10e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  89 ATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTD 168
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 169 VVR--YLLEQRADPnakaHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLLSH-ADC 244
Cdd:PLN03192 606 IFRilYHFASISDP----HAAGDLLCTAAKRNDLTAMKELLKQGLNVdSEDHQGATALQVAMAEDHVDMVRLLIMNgADV 681

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823075 245 DRRSriealellgasfandreNYDIMKTYHylYLAMLERFQDGDNILEKEVLPPIHAYGNRTECRNPQELE 315
Cdd:PLN03192 682 DKAN-----------------TDDDFSPTE--LRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPGRLQ 733
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 87-118 2.48e-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: 2.48e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 157823075   87 DGATALWCAAG-AGHFEVVKLLVSHGANVNHTT 118
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 475-613 3.21e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 475 IHLDPRTREGFTLLHLAVNSNTPVDdfhtndvcsfpnalVTKLLLDCGAEVNAVDNEGNSALHIivqYnrpISDFLTLHS 554
Cdd:PHA03095  74 ADVNAPERCGFTPLHLYLYNATTLD--------------VIKLLIKAGADVNAKDKVGRTPLHV---Y---LSGFNINPK 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823075 555 IIISLVEAGAHTDMTNKQNKTPLDK--STTGVSEILLKtqmkmsLKCLAARAVRANDINYQ 613
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLR------LLIDAGADVYAVDDRFR 188
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 83-153 7.25e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.43  E-value: 7.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823075  83 GYVID-----GATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKY 153
Cdd:PHA03100 182 GVPINikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_5 pfam13857
Ankyrin repeats (many copies);
173-226 7.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 7.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157823075  173 LLEQR-ADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVA 226
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLnLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
189-239 7.91e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 7.91e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157823075  189 TALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELLL 239
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-108 8.48e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 8.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823075   46 RSTPLIIAARNGHAKVVRLLLEHyrvqtqqtgTVRFDGYVIDGATALWCAAGAGHFEVVKLLV 108
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK---------GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-263 9.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 9.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  48 TPLIIAARNGHAKVVRLLLEHyrvqtqqtgTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNhttvTNSTPLRA 127
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSY---------GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 128 ACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGH-TDVVRYLLEQRADPNAKAHCGATALHFAAEAGH-IDIVKE 205
Cdd:PHA02876 247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRT 326

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823075 206 LIKWRAAI-VVNGHGMTPLKVAA--ESCKADVVELLLSHADCDRRSRIEALELLGASFAND 263
Cdd:PHA02876 327 LIMLGADVnAADRLYITPLHQAStlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 155-183 1.20e-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: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 157823075  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 2.56e-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: 2.56e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 157823075   153 YDNTCLMIAAYKGHTDVVRYLLEQRADPNA 182
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-179 3.11e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  48 TPLIIAARNGHAKVVRLLLEH---YRVQTQQTGTVRFdgyvidgatalWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTP 124
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLDYgadIEALSQKIGTALH-----------FALCGTNPYMSVKTLIDRGANVNSKNKDLSTP 445

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157823075 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 4.10e-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: 4.10e-04
                           10        20
                   ....*....|....*....|....*....
gi 157823075    87 DGATALWCAAGAGHFEVVKLLVSHGANVN 115
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-579 4.57e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 42.63  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 477 LDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRpisdfltlHSII 556
Cdd:COG0666  179 VNARDNDGETPLHLAAENG---------------HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGN--------LEIV 235

                         90       100
                 ....*....|....*....|...
gi 157823075 557 ISLVEAGAHTDMTNKQNKTPLDK 579
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLL 258
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 134-240 6.37e-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: 6.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 134 LDIVKYLVENNANISI---------ANKYD-----NTCLMIAAYKGHTDVVRYLLEQRADPNAKAHC-GATALHFAAEAG 198
Cdd:cd22194  154 GDIVKLLIAKGADVNAhakgvffnpKYKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDITSQDSrGNTVLHALVTVA 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157823075 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 157823075 134 LDIVKYLVENNANISIA------NKYDNTC-------LMIAAYKGHTDVVRYLLEQRADP---NAKAHCGATALH---FA 194
Cdd:cd22197  107 LQCVKLLVENGADVHARacgrffQKKQGTCfyfgelpLSLAACTKQWDVVNYLLENPHQPaslQAQDSLGNTVLHalvMI 186

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157823075 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 7.72e-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: 7.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  20 LAALLLNRSESDiRYLLGYVSQQGGQRSTPLIIAARNGHAKV---VRLLLEHYRVQTQQTGTVR---FDGYvIDGATALW 93
Cdd:cd21882    1 LEELLGLLECLR-WYLTDSAYQRGATGKTCLHKAALNLNDGVneaIMLLLEAAPDSGNPKELVNapcTDEF-YQGQTALH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  94 CAAGAGHFEVVKLLVSHGANVnHTTVTNST--------------PLRAACFDGRLDIVKYLVENNANISIANKYDNTclm 159
Cdd:cd21882   79 IAIENRNLNLVRLLVENGADV-SARATGRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQDSL--- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 160 iaaykGHTdVVRYLLEQradPNAKAHCGATALHFAAE----AGHIDIVKELikwraAIVVNGHGMTPLKVAAESCKADVV 235
Cdd:cd21882  155 -----GNT-VLHALVLQ---ADNTPENSAFVCQMYNLllsyGAHLDPTQQL-----EEIPNHQGLTPLKLAAVEGKIVMF 220

                        250
                 ....*....|....*..
gi 157823075 236 ELLLS---HADCDRRSR 249
Cdd:cd21882  221 QHILQrefSGPYQPLSR 237
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 46-163 9.70e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 9.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075  46 RSTPLIIAARNGHAKVVRLLLEHyrvqtqQTGTVRFDGYvidGATALWCAAGAGHFEVVKLLVSHGANVNHttVTNSTPL 125
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIELLIDH------KACLDIEDCC---GCTPLIIAMAKGDIAICKMLLDSGANIDY--FGKNGCV 203

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 157823075 126 RAACF---DGRLDIVKYLVENNA--NI--SIANKYDNTCLMIAAY 163
Cdd:PHA02875 204 AALCYaieNNKIDIVRLFIKRGAdcNImfMIEGEECTILDMICNM 248
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 465-552 1.20e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 465 CRINKQIYNLIHLDPRTREGFTLLHLAVNSNTPvdDFhtndvcsfpnalvTKLLLDCGAEVNAVDNEGNSALHIIVQYNr 544
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNP--EF-------------VKYLLDLGANPNLVNKYGDTPLHIAILNN- 236


                 ....*...
gi 157823075 545 pISDFLTL 552
Cdd:PHA03100 237 -NKEIFKL 243
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 475-580 1.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 475 IHLDPRTREGFTLLHLAVNSNtpvddfhtndvcsfpNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNrpisdfltLHS 554
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKG---------------DLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN--------FFD 171

                         90       100
                 ....*....|....*....|....*.
gi 157823075 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 157823075 134 LDIVKYLVENNANISIA-------NKYDNTC-------LMIAAYKGHTDVVRYLLE---QRADPNAKAHCGATALHFAAE 196
Cdd:cd22193   89 GDIVALLVENGADVHAHakgrffqPKYQGEGfyfgelpLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVT 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823075 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 157823075  88 GATALWCAAGAGHFEVVKLLVSHGANVN----------HTTVT---NSTPLRAACFDGRLDIVKYLVENNANISIANKYD 154
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQD 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823075 155 ---NTCL----MIA-AYKGHTDVVRYLLEQ------RADPNAKA-----HCGATALHFAAEAGHIDIVKELIK 208
Cdd:cd22197  174 slgNTVLhalvMIAdNSPENSALVIKMYDGllqagaRLCPTVQLeeisnHEGLTPLKLAAKEGKIEIFRHILQ 246
PHA03095 PHA03095
ankyrin-like protein; Provisional
 516-585 1.84e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 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 2.63e-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: 2.63e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 157823075   87 DGATALWCAAGAGHFEVVKLLVSHGANVNH 116
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 103-239 3.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 103 VVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYL--------- 173
Cdd:PHA02874  17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsi 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 174 --------------LEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI-VVNGHGMTPLKVAAESCKADVVELL 238
Cdd:PHA02874  97 lpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVnIEDDNGCYPIHIAIKHNFFDIIKLL 176


                 .
gi 157823075 239 L 239
Cdd:PHA02874 177 L 177
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 134-216 3.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 134 LDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAI 213
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237


                 ...
gi 157823075 214 VVN 216
Cdd:PHA02876 238 NKN 240
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 153-182 3.43e-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: 3.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 157823075  153 YDNTCLMIAAYKGHTDVVRYLLEQRADPNA 182
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 102-225 4.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823075 102 EVVKLLVSHGANVNHTTVTNsTPLRAACFDGRLD------IVKYLVENNANI---SIANKYDNTCLMIAAYKGHTDVVRY 172
Cdd:PHA02989  51 KIVKLLIDNGADVNYKGYIE-TPLCAVLRNREITsnkikkIVKLLLKFGADInlkTFNGVSPIVCFIYNSNINNCDMLRF 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157823075 173 LLEQRADPNA-KAHCGATALHFAAEAGHI--DIVKELIKWRAAIV--VNGHGMTPLKV 225
Cdd:PHA02989 130 LLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFGVNLFekTSLYGLTPMNI 187
Ank_5 pfam13857
Ankyrin repeats (many copies);
107-161 6.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 6.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157823075  107 LVSHG-ANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIA 161
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
518-578 6.33e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 6.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823075  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 157823075  54 ARNGHAKVVRLLLehyrvqtqqTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGR 133
Cdd:PTZ00322  90 AASGDAVGARILL---------TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160


                 ....*..
gi 157823075 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH