NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|194474064|ref|NP_001124038|]
View 

protein phosphatase 1 regulatory subunit 16A [Rattus norvegicus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins 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

Gene Ontology:  GO:0005515
PubMed:  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];
74-328 2.14e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 2.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  74 IALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHL 153
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 154 VELLISRGADLLAVNTDGNMPydlcedeqtldyLETAMANrgitqDSIEEARAvpelcmlndlqnLLHAGANLNDPLDHG 233
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTP------------LHLAAAN-----GNLEIVKL------------LLEAGADVNARDNDG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 234 ATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLD---VCGDEE 310
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAAL 266

                        250
                 ....*....|....*...
gi 194474064 311 VRAKLLELKHKQDALLRA 328
Cdd:COG0666  267 IVKLLLLALLLLAAALLD 284
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-328 2.14e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 2.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  74 IALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHL 153
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 154 VELLISRGADLLAVNTDGNMPydlcedeqtldyLETAMANrgitqDSIEEARAvpelcmlndlqnLLHAGANLNDPLDHG 233
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTP------------LHLAAAN-----GNLEIVKL------------LLEAGADVNARDNDG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 234 ATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLD---VCGDEE 310
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAAL 266

                        250
                 ....*....|....*...
gi 194474064 311 VRAKLLELKHKQDALLRA 328
Cdd:COG0666  267 IVKLLLLALLLLAAALLD 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-168 5.43e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 5.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064   76 LLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEaGADVNARDSEcWTPLHAAATCGHLHLVE 155
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 194474064  156 LLISRGADLLAVN 168
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-303 3.66e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.00  E-value: 3.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  77 LEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCC---IDDFQEMVQQLLEAGADVNARDSECWTPLH---------- 143
Cdd:PHA03095  19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHlylynattld 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 144 -------------AAATCG----HLHL---------VELLISRGADLLAVNTDGNMPYDL------CEDEqTLDYLETAM 191
Cdd:PHA03095  99 vikllikagadvnAKDKVGrtplHVYLsgfninpkvIRLLLRKGADVNALDLYGMTPLAVllksrnANVE-LLRLLIDAG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 192 ANRgITQDSI---------EEARAVPELcmlndLQNLLHAGANLNDPLDHGATLLHIAAAnGFSEVATL---LLEQGASL 259
Cdd:PHA03095 178 ADV-YAVDDRfrsllhhhlQSFKPRARI-----VRELIRAGCDPAATDMLGNTPLHSMAT-GSSCKRSLvlpLLIAGISI 250

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 194474064 260 SAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPL 303
Cdd:PHA03095 251 NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 77-174 1.31e-07

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: 54.25  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  77 LEAAARNDLEEVRQFLTSGVsPNLANE-------DGLTALHQCCIDDFQEMVQQLLEAGADV-NAR----------DSEC 138
Cdd:cd22192   55 LHVAALYDNLEAAVVLMEAA-PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVvSPRatgtffrpgpKNLI 133

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 194474064 139 W---TPLHAAATCGHLHLVELLISRGADLLAVNTDGNMP 174
Cdd:cd22192  134 YygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 75-319 8.71e-06

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: 48.54  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064   75 ALLEAAARNDLEEVRQFLtsgvsPNLANE--DGLTALHQCCID--DFQEMVQQLLEAGAD-------VNARDSECW---- 139
Cdd:TIGR00870  55 ALFVAAIENENLELTELL-----LNLSCRgaVGDTLLHAISLEyvDAVEAILLHLLAAFRksgplelANDQYTSEFtpgi 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  140 TPLHAAATCGHLHLVELLISRGADLlavntdgnmpydlcedeqtldyletamanrgitqdsieEARAVPELCMLNDLQNL 219
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASV--------------------------------------PARACGDFFVKSQGVDS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  220 LHaganlndpldHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAA----------------------YWG 277
Cdd:TIGR00870 172 FY----------HGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelscqmynfalsLLD 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 194474064  278 QV-HLVELLVAhgadLNGKslvDETPLDVCGDEEvRAKLLELK 319
Cdd:TIGR00870 242 KLrDSKELEVI----LNHQ---GLTPLKLAAKEG-RIVLFRLK 276
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 265-293 5.94e-05

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: 40.26  E-value: 5.94e-05
                           10        20
                   ....*....|....*....|....*....
gi 194474064   265 DGWEPLHAAAYWGQVHLVELLVAHGADLN 293
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-328 2.14e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 2.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  74 IALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHL 153
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 154 VELLISRGADLLAVNTDGNMPydlcedeqtldyLETAMANrgitqDSIEEARAvpelcmlndlqnLLHAGANLNDPLDHG 233
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTP------------LHLAAAN-----GNLEIVKL------------LLEAGADVNARDNDG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 234 ATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLD---VCGDEE 310
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAAL 266

                        250
                 ....*....|....*...
gi 194474064 311 VRAKLLELKHKQDALLRA 328
Cdd:COG0666  267 IVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-303 3.34e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 3.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  75 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHLV 154
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 155 ELLISRGADLLAVNTDGNMPydlcedeqtldyLETAMANrgitqDSIEEARAvpelcmlndlqnLLHAGANLNDPLDHGA 234
Cdd:COG0666  170 KLLLEAGADVNARDNDGETP------------LHLAAEN-----GHLEIVKL------------LLEAGADVNAKDNDGK 220

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194474064 235 TLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPL 303
Cdd:COG0666  221 TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-328 7.08e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 7.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  75 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHLV 154
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 155 ELLISRGADLLAVNTDGNMPydlcedeqtldyLETAMANrgitqDSIEEARAvpelcmlndlqnLLHAGANLNDPLDHGA 234
Cdd:COG0666  104 KLLLEAGADVNARDKDGETP------------LHLAAYN-----GNLEIVKL------------LLEAGADVNAQDNDGN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 235 TLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLDV---CGDEEV 311
Cdd:COG0666  155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLaaeNGNLEI 234

                        250
                 ....*....|....*..
gi 194474064 312 RAKLLELKHKQDALLRA 328
Cdd:COG0666  235 VKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
151-323 1.90e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 1.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 151 LHLVELLISRGADLLAVNTDGNMPYDLCEDEQTLDYLETAMANRGITQDSIEEARAVPELCMLNDLQNLLHAGANLNDPL 230
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 231 DHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLDV---CG 307
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNG 164

                        170
                 ....*....|....*.
gi 194474064 308 DEEVrAKLLeLKHKQD 323
Cdd:COG0666  165 NLEI-VKLL-LEAGAD 178
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-168 5.43e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 5.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064   76 LLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEaGADVNARDSEcWTPLHAAATCGHLHLVE 155
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 194474064  156 LLISRGADLLAVN 168
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-303 3.66e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.00  E-value: 3.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  77 LEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCC---IDDFQEMVQQLLEAGADVNARDSECWTPLH---------- 143
Cdd:PHA03095  19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHlylynattld 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 144 -------------AAATCG----HLHL---------VELLISRGADLLAVNTDGNMPYDL------CEDEqTLDYLETAM 191
Cdd:PHA03095  99 vikllikagadvnAKDKVGrtplHVYLsgfninpkvIRLLLRKGADVNALDLYGMTPLAVllksrnANVE-LLRLLIDAG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 192 ANRgITQDSI---------EEARAVPELcmlndLQNLLHAGANLNDPLDHGATLLHIAAAnGFSEVATL---LLEQGASL 259
Cdd:PHA03095 178 ADV-YAVDDRfrsllhhhlQSFKPRARI-----VRELIRAGCDPAATDMLGNTPLHSMAT-GSSCKRSLvlpLLIAGISI 250

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 194474064 260 SAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPL 303
Cdd:PHA03095 251 NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 120-303 2.58e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 85.12  E-value: 2.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 120 MVQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNTDGNMPYDLCEDEQTLDYLETAMANRG-ITQ 198
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSnINK 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 199 DSIEEARAVPElcmlNDLQN---LLHAGANLNDPLDHGATLLHIAA-ANGFSEVATLLLEQGASLSAKDHDGWEPLHAAA 274
Cdd:PHA02876 240 NDLSLLKAIRN----EDLETsllLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                        170       180       190
                 ....*....|....*....|....*....|
gi 194474064 275 YWG-QVHLVELLVAHGADLNGKSLVDETPL 303
Cdd:PHA02876 316 KNGyDTENIRTLIMLGADVNAADRLYITPL 345
Ank_2 pfam12796
Ankyrin repeats (3 copies);
216-293 1.82e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 1.82e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194474064  216 LQNLLHAGANLNDPLDHGATLLHIAAANGFSEVATLLLEQGASlsAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLN 293
Cdd:pfam12796  13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-263 1.82e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  109 LHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELLISrgadllavntdgnmpydlcedeqtldyle 188
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------- 51

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194474064  189 tamanrgitqdsieearavpelcmlndlqnllHAGANLNdplDHGATLLHIAAANGFSEVATLLLEQGASLSAKD 263
Cdd:pfam12796  52 --------------------------------HADVNLK---DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 74-303 3.01e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 3.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  74 IALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCC-IDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGH-L 151
Cdd:PHA02876 242 LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdT 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 152 HLVELLISRGADLLAVNTDGNMPYdlcEDEQTLD-YLETAM----------ANRGITQDSIEEARAVPELCMLNdlqNLL 220
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLYITPL---HQASTLDrNKDIVItllelganvnARDYCDKTPIHYAAVRNNVVIIN---TLL 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 221 HAGANLNDPLDHGATLLHIA--AANGFSEVATLLlEQGASLSAKDHDGWEPLHAAAYWG-QVHLVELLVAHGADLNGKSL 297
Cdd:PHA02876 396 DYGADIEALSQKIGTALHFAlcGTNPYMSVKTLI-DRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINI 474


                 ....*.
gi 194474064 298 VDETPL 303
Cdd:PHA02876 475 QNQYPL 480
Ank_2 pfam12796
Ankyrin repeats (3 copies);
237-323 4.46e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  237 LHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHgADLNGKSLvDETPLDVC---GDEEVrA 313
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAarsGHLEI-V 77

                          90
                  ....*....|
gi 194474064  314 KLLeLKHKQD 323
Cdd:pfam12796  78 KLL-LEKGAD 86
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 84-303 1.54e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.61  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  84 DLEEVRQFL-TSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELLISRGA 162
Cdd:PHA02874  13 DIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 163 DLLAvntdgnMPYDLCEDEQTLDYLETAManrgitQDSIEEARAVPELCML---NDLQN---LLHAGANLNDPLDHGATL 236
Cdd:PHA02874  93 DTSI------LPIPCIEKDMIKTILDCGI------DVNIKDAELKTFLHYAikkGDLESikmLFEYGADVNIEDDNGCYP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194474064 237 LHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPL 303
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-303 2.16e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  92 LTSGVSPNLANEDGLTALHQCC-----IDDFQEMVQQLLEAGADVNARDSECWTPLHAAATC--GHLHLVELLISRGADL 164
Cdd:PHA03100  55 LDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANV 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 165 LAVNTDGNMPYDLcedeqtldYLEtamanrGITQDsieearavpelcmLNDLQNLLHAGANLNdpldhgatllhiaAANg 244
Cdd:PHA03100 135 NIKNSDGENLLHL--------YLE------SNKID-------------LKILKLLIDKGVDIN-------------AKN- 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194474064 245 fseVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPL 303
Cdd:PHA03100 174 ---RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 86-305 1.59e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.14  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  86 EEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLL 165
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 166 AVNTDGNMPydLCEDEQTLDYletamanrgitqdsieearavpelcmlNDLQNLLHAGANLNDPLDHGATLLHIAAANGF 245
Cdd:PHA02874 185 VKDNNGESP--LHNAAEYGDY---------------------------ACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194474064 246 SEVAtlLLEQGASLSAKDHDGWEPLH-AAAYWGQVHLVELLVAHGADLNGKSLVDETPLDV 305
Cdd:PHA02874 236 SAIE--LLINNASINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDT 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
105-158 2.70e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 2.70e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194474064  105 GLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELLI 158
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 120-365 3.12e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.04  E-value: 3.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 120 MVQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNTDGNmpydlcedeqtldyleTAMANRGITQD 199
Cdd:PLN03192 540 LLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN----------------TALWNAISAKH 603

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 200 sieearavpelcmlNDLQNLLHAGANLNDPlDHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQV 279
Cdd:PLN03192 604 --------------HKIFRILYHFASISDP-HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHV 668

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 280 HLVELLVAHGADLNGKSLVDE-TPLDVcgdEEVRAKlLELKHK------QDALLRAQGRQRSLLRRRTSSAGSRGKVVRR 352
Cdd:PLN03192 669 DMVRLLIMNGADVDKANTDDDfSPTEL---RELLQK-RELGHSitivdsVPADEPDLGRDGGSRPGRLQGTSSDNQCRPR 744

                        250
                 ....*....|...
gi 194474064 353 VSLTHRTNLYRKE 365
Cdd:PLN03192 745 VSIYKGHPLLRNE 757
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 121-209 9.87e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 9.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 121 VQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNTDGNMPYDLCEDEQTLDYLETAManRGITQDS 200
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS--RHSQCHF 175


                 ....*....
gi 194474064 201 IEEARAVPE 209
Cdd:PTZ00322 176 ELGANAKPD 184
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 81-292 1.49e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  81 ARN--DLEEVRQFLTSGVSPNLANEDGLTALHQC-CIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELL 157
Cdd:PHA02876 315 AKNgyDTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 158 ISRGADLLAVNtdgnmpydlcedEQTLDYLETAmanrgitqdsieearavpeLCMLN---DLQNLLHAGANLNDPLDHGA 234
Cdd:PHA02876 395 LDYGADIEALS------------QKIGTALHFA-------------------LCGTNpymSVKTLIDRGANVNSKNKDLS 443

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 235 TLLHIAAANGFS-EVATLLLEQGASLSAKDHDGWEPLHAA-AYWGqvhLVELLVAHGADL 292
Cdd:PHA02876 444 TPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAlEYHG---IVNILLHYGAEL 500
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 119-305 1.80e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 119 EMVQQLLEAGADVNARDSECW-TPLHAAATCGHLHLVELLISRGADLLAVNTDGNMPydlcedeqtldyLETAMANRgit 197
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP------------LHHAVKHY--- 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 198 QDSIEEAravpelcmlndlqnLLHAGANLNDPLDHGATLLHIAAANGFS-EVATLLLEQGASLSAKDH-DGWEPLHAAAY 275
Cdd:PHA02878 213 NKPIVHI--------------LLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278

                        170       180       190
                 ....*....|....*....|....*....|
gi 194474064 276 WGQVhlVELLVAHGADLNGKSLVDETPLDV 305
Cdd:PHA02878 279 SERK--LKLLLEYGADINSLNSYKLTPLSS 306
PHA03095 PHA03095
ankyrin-like protein; Provisional
 213-328 6.18e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 6.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 213 LNDLQNLLHAGANLNDPLDHGATLLHIAAANGFS---EVATLLLEQGASLSAKDHDGWEPLHAAAYWGQV-HLVELLVAH 288
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 194474064 289 GADLNGKSLVDETPLDVC-GDEEVRAKLLELkhkqdaLLRA 328
Cdd:PHA03095 107 GADVNAKDKVGRTPLHVYlSGFNINPKVIRL------LLRK 141
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 74-293 6.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 6.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  74 IALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHL 153
Cdd:PHA02875   4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 154 VELLISRGADLLAV-NTDGNMPYDLCEDEQTLDYLETamanrgitqdsieearavpelcmlndlqnLLHAGANLNDPLDH 232
Cdd:PHA02875  84 VEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKL-----------------------------LIARGADPDIPNTD 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194474064 233 GATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLN 293
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 197-288 6.37e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 6.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 197 TQDSIEEARA---VPELCMLN------DLQNLLHAGANLNDPLDHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGW 267
Cdd:PTZ00322  70 TEEVIDPVVAhmlTVELCQLAasgdavGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK 149

                         90       100
                 ....*....|....*....|.
gi 194474064 268 EPLHAAAYWGQVHLVELLVAH 288
Cdd:PTZ00322 150 TPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
235-286 8.19e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 8.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 194474064  235 TLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLV 286
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 109-317 3.33e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.04  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 109 LHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAatCGH---LHLVELLISR-----GADLLAVNTDGN-------- 172
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHII--CKEpnkLGMKEMIRSInkcsvFYTLVAIKDAFNnrnveifk 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 173 -MPYDLCEDEQTLDYLETamanRGITQDSIEEARAVpelcmlndlQNLLHAGANLNDPLDH-GATLLHIAAANGFSEVAT 250
Cdd:PHA02878 119 iILTNRYKNIQTIDLVYI----DKKSKDDIIEAEIT---------KLLLSYGADINMKDRHkGNTALHYATENKDQRLTE 185

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194474064 251 LLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLDV----CGDEEVRAKLLE 317
Cdd:PHA02878 186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIsvgyCKDYDILKLLLE 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 73-159 6.00e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 6.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  73 SIALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLH 152
Cdd:PTZ00322  83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162


                 ....*..
gi 194474064 153 LVELLIS 159
Cdd:PTZ00322 163 VVQLLSR 169
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 77-174 1.31e-07

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: 54.25  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  77 LEAAARNDLEEVRQFLTSGVsPNLANE-------DGLTALHQCCIDDFQEMVQQLLEAGADV-NAR----------DSEC 138
Cdd:cd22192   55 LHVAALYDNLEAAVVLMEAA-PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVvSPRatgtffrpgpKNLI 133

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 194474064 139 W---TPLHAAATCGHLHLVELLISRGADLLAVNTDGNMP 174
Cdd:cd22192  134 YygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
PHA03095 PHA03095
ankyrin-like protein; Provisional
 219-305 1.52e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 219 LLHAGANLNDPLDHGATLLHIAAANGFSE-VATLLLEQGASLSAKDHDGWEPLHaaaywgqVHL---------VELLVAH 288
Cdd:PHA03095  69 LLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLH-------VYLsgfninpkvIRLLLRK 141

                         90
                 ....*....|....*..
gi 194474064 289 GADLNGKSLVDETPLDV 305
Cdd:PHA03095 142 GADVNALDLYGMTPLAV 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
124-178 1.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 194474064  124 LLEAG-ADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNTDGNMPYDLC 178
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 83-163 2.61e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  83 NDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELLISRGA 162
Cdd:PHA03100 170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                 .
gi 194474064 163 D 163
Cdd:PHA03100 250 S 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-271 2.61e-07

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: 53.48  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  73 SIALLEAAARNDLEEVRQFLTS-GVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGAD-VN-ARDSECW---TPLHAAA 146
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 147 TCGHLHLVELLISRGADllaVNTdgnmpydlcedeqtldyletamanrgitqdsieeARAVpELCMLNDLQNLLHAGanl 226
Cdd:cd22192   98 VNQNLNLVRELIARGAD---VVS----------------------------------PRAT-GTFFRPGPKNLIYYG--- 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 194474064 227 ndplDHgatLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLH 271
Cdd:cd22192  137 ----EH---PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 76-257 1.26e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  76 LLEAAARNDLEEVRQFLTSGVSPN-LANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAAATCGHLHLV 154
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 155 ELLISRGADLLAVNTDGNMPydlcedeqtldyLETAMANRGItqdsieearavpELCMLndlqnLLHAGANLNDPLDHG- 233
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTP------------LIIAMAKGDI------------AICKM-----LLDSGANIDYFGKNGc 202

                        170       180
                 ....*....|....*....|....
gi 194474064 234 ATLLHIAAANGFSEVATLLLEQGA 257
Cdd:PHA02875 203 VAALCYAIENNKIDIVRLFIKRGA 226
PHA02946 PHA02946
ankyin-like protein; Provisional
 112-303 1.53e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.44  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 112 CCIDDFQE-MVQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNTDGNMP--YDLCEDEQTLDYLE 188
Cdd:PHA02946  45 CGIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlyYLSGTDDEVIERIN 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 189 TAMANRGITQDSIEEARAVPELCMLND----LQNLLHAG--ANLNDPLDHGATLLHIAAANGFSEVATLLLEQGASLSAK 262
Cdd:PHA02946 125 LLVQYGAKINNSVDEEGCGPLLACTDPservFKKIMSIGfeARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKP 204

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 194474064 263 DHDGWEPLH--AAAYWGQVHLVELLVAhGADLNGKSLVDETPL 303
Cdd:PHA02946 205 DHDGNTPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPL 246
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-303 2.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  63 KPQKQVHFPPSIAllEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPL 142
Cdd:PHA02876 138 KINESIEYMKLIK--ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVL 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 143 HAAATCGHLHLVELLISRGA-----DLLAVNTDGNmpydlcEDeqtldyLETAMA--NRGITQDSIEE--------ARAV 207
Cdd:PHA02876 216 ECAVDSKNIDTIKAIIDNRSninknDLSLLKAIRN------ED------LETSLLlyDAGFSVNSIDDckntplhhASQA 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 208 PELCMLndLQNLLHAGANLNDPLDHGATLLHIAAANGF-SEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVH-LVELL 285
Cdd:PHA02876 284 PSLSRL--VPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITL 361

                        250
                 ....*....|....*...
gi 194474064 286 VAHGADLNGKSLVDETPL 303
Cdd:PHA02876 362 LELGANVNARDYCDKTPI 379
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 241-312 5.62e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 5.62e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194474064 241 AANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLDVCGDEEVR 312
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 75-319 8.71e-06

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: 48.54  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064   75 ALLEAAARNDLEEVRQFLtsgvsPNLANE--DGLTALHQCCID--DFQEMVQQLLEAGAD-------VNARDSECW---- 139
Cdd:TIGR00870  55 ALFVAAIENENLELTELL-----LNLSCRgaVGDTLLHAISLEyvDAVEAILLHLLAAFRksgplelANDQYTSEFtpgi 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  140 TPLHAAATCGHLHLVELLISRGADLlavntdgnmpydlcedeqtldyletamanrgitqdsieEARAVPELCMLNDLQNL 219
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASV--------------------------------------PARACGDFFVKSQGVDS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  220 LHaganlndpldHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAA----------------------YWG 277
Cdd:TIGR00870 172 FY----------HGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelscqmynfalsLLD 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 194474064  278 QV-HLVELLVAhgadLNGKslvDETPLDVCGDEEvRAKLLELK 319
Cdd:TIGR00870 242 KLrDSKELEVI----LNHQ---GLTPLKLAAKEG-RIVLFRLK 276
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-168 1.38e-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: 41.89  E-value: 1.38e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 194474064  139 WTPLHAAAT-CGHLHLVELLISRGADLLAVN 168
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 248-304 3.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 3.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194474064 248 VATLLLEQGASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLD 304
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 82-174 5.61e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.43  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  82 RNDLEEVRQFLTSGVSPNLANEDGLTALHQ---CCIDDFqEMVQQLLEAGAD----------------VNARDSECWTPL 142
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLyleSNKIDL-KILKLLIDKGVDinaknrvnyllsygvpINIKDVYGFTPL 196

                         90       100       110
                 ....*....|....*....|....*....|..
gi 194474064 143 HAAATCGHLHLVELLISRGADLLAVNTDGNMP 174
Cdd:PHA03100 197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
Ank_5 pfam13857
Ankyrin repeats (many copies);
96-145 5.92e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 5.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 194474064   96 VSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLHAA 145
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 265-293 5.94e-05

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: 40.26  E-value: 5.94e-05
                           10        20
                   ....*....|....*....|....*....
gi 194474064   265 DGWEPLHAAAYWGQVHLVELLVAHGADLN 293
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 139-164 6.95e-05

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: 39.88  E-value: 6.95e-05
                           10        20
                   ....*....|....*....|....*.
gi 194474064   139 WTPLHAAATCGHLHLVELLISRGADL 164
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 104-135 9.80e-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: 39.58  E-value: 9.80e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 194474064  104 DGLTALHQCCID-DFQEMVQQLLEAGADVNARD 135
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 119-173 2.02e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 2.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 194474064 119 EMVQQLLEAGADVNARDSECWTPLHAAATCGHLHLVELLISRGADLLAVNTDGNM 173
Cdd:PLN03192 636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
Ank_4 pfam13637
Ankyrin repeats (many copies);
266-316 2.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 2.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194474064  266 GWEPLHAAAYWGQVHLVELLVAHGADLNGKSLVDETPLDVC---GDEEVrAKLL 316
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasnGNVEV-LKLL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-166 3.80e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 3.80e-04
                          10        20
                  ....*....|....*....|....*...
gi 194474064  139 WTPLHAAATCGHLHLVELLISRGADLLA 166
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 232-291 4.07e-04

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: 43.08  E-value: 4.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194474064 232 HGATLLHIAAANGFSEVATLLLEQGASL-----SAKDHDGWEPLHAAAYWGQVHLVELLVAHGAD 291
Cdd:cd22192   50 LGETALHVAALYDNLEAAVVLMEAAPELvnepmTSDLYQGETALHIAVVNQNLNLVRELIARGAD 114
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 76-133 4.53e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 4.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 194474064  76 LLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNA 133
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 265-293 5.37e-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: 37.65  E-value: 5.37e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 194474064  265 DGWEPLHAAAY-WGQVHLVELLVAHGADLN 293
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVN 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 73-169 5.76e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  73 SIALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNARDSECWTPLH-AAATCGHL 151
Cdd:PHA02878 169 NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDY 248

                         90
                 ....*....|....*...
gi 194474064 152 HLVELLISRGADLLAVNT 169
Cdd:PHA02878 249 DILKLLLEHGVDVNAKSY 266
Ank_4 pfam13637
Ankyrin repeats (many copies);
138-187 6.93e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 6.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 194474064  138 CWTPLHAAATCGHLHLVELLISRGADLLAVNTDGNMPYDLC---EDEQTLDYL 187
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasnGNVEVLKLL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 265-293 7.79e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 7.79e-04
                          10        20
                  ....*....|....*....|....*....
gi 194474064  265 DGWEPLHAAAYWGQVHLVELLVAHGADLN 293
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02946 PHA02946
ankyin-like protein; Provisional
 216-318 7.97e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.96  E-value: 7.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 216 LQNLLHAGANLNDPLDHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAAAYWGQ--VHLVELLVAHGADLN 293
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIN 134

                         90       100       110
                 ....*....|....*....|....*....|
gi 194474064 294 GKslVDET---PLDVCGD--EEVRAKLLEL 318
Cdd:PHA02946 135 NS--VDEEgcgPLLACTDpsERVFKKIMSI 162
Ank_5 pfam13857
Ankyrin repeats (many copies);
219-273 1.12e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 194474064  219 LLHAG-ANLNDPLDHGATLLHIAAANGFSEVATLLLEQGASLSAKDHDGWEPLHAA 273
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 75-133 1.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194474064  75 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLLEAGADVNA 133
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 232-264 1.65e-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. 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: 36.11  E-value: 1.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 194474064  232 HGATLLHIAAA-NGFSEVATLLLEQGASLSAKDH 264
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
75-125 1.75e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 194474064   75 ALLEAAARNDLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDFQEMVQQLL 125
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 219-290 2.54e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 39.03  E-value: 2.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194474064 219 LLHAGANLND-PLDHGATLLHIAAANGFSEVATLLLEQ-GASLSAKDHDGWEPLHAAAYWGQVHLVELLVAHGA 290
Cdd:PHA02743  79 LVNMGADINArELGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
PHA02741 PHA02741
hypothetical protein; Provisional
 119-182 4.14e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 4.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194474064 119 EMVQQLLEAGADVNARDS-ECWTPLHAAATCGHLHLVELLISR-GADLLAVNTDGNMPYDLCEDEQ 182
Cdd:PHA02741  78 EIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDNE 143
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 104-133 4.39e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 4.39e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 194474064   104 DGLTALHQCCIDDFQEMVQQLLEAGADVNA 133
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
203-253 4.93e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 4.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194474064  203 EARAVPELCMLNDLQN---LLHAGANLNDPLDHGATLLHIAAANGFSEVATLLL 253
Cdd:pfam13637   1 ELTALHAAAASGHLELlrlLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 232-261 5.00e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 5.00e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 194474064  232 HGATLLHIAAANGFSEVATLLLEQGASLSA 261
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 222-299 5.37e-03

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: 39.48  E-value: 5.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 222 AGANLNDPLDHGATLLHIAAANGFSEVATLLLEQGASLSAKD-------------HDGWEPLHAAAYWGQVHLVELLVAH 288
Cdd:cd21882   62 VNAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLEN 141

                         90
                 ....*....|.
gi 194474064 289 GADLNGKSLVD 299
Cdd:cd21882  142 GAQPAALEAQD 152
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 102-196 7.62e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.16  E-value: 7.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064 102 NEDGLTALHQCC---IDDFQEMVQQLLEAGADVNARDSECW-TPLHAAATCGHLHLVELLISR-GADLLAVNTDGNMPYD 176
Cdd:PHA02736  52 NRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERVFGnTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYY 131

                         90       100
                 ....*....|....*....|...
gi 194474064 177 L---CEDEQTLDYLETAMANRGI 196
Cdd:PHA02736 132 VaceRHDAKMMNILRAKGAQCKV 154
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 81-174 8.30e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.12  E-value: 8.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474064  81 ARN-DLEEVRQFLTSGVSPNLANEDGLTALHQCCIDDF--QEMVQQLLEAGADVNARDSECWTPLHAAATCG-------- 149
Cdd:PHA02716 292 ARNiDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildp 371

                         90       100       110
                 ....*....|....*....|....*....|.
gi 194474064 150 ------HLHLVELLISRGADLLAVNTDGNMP 174
Cdd:PHA02716 372 etdndiRLDVIQCLISLGADITAVNCLGYTP 402
 
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