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Conserved domains on  [gi|2462621386|ref|XP_054217364|]
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protein phosphatase 1 regulatory subunit 16A isoform X1 [Homo sapiens]

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

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-401 1.19e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 1.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 152 AMVHRELWEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLI 231
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 232 ASGANLLAVNTDGNMPydlcddeqtldcLETAmadrgITQDSIEAARavpelrMLddirsrLQAGADLHAPLDHGATLLH 311
Cdd:COG0666   141 EAGADVNAQDNDGNTP------------LHLA-----AANGNLEIVK------LL------LEAGADVNARDNDGETPLH 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 312 VAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLD---VCGDEEVRAKL 388
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAALIVKLL 271

                         250
                  ....*....|...
gi 2462621386 389 LELKHKHDALLRA 401
Cdd:COG0666   272 LLALLLLAAALLD 284
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-401 1.19e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 1.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 152 AMVHRELWEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLI 231
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 232 ASGANLLAVNTDGNMPydlcddeqtldcLETAmadrgITQDSIEAARavpelrMLddirsrLQAGADLHAPLDHGATLLH 311
Cdd:COG0666   141 EAGADVNAQDNDGNTP------------LHLA-----AANGNLEIVK------LL------LEAGADVNARDNDGETPLH 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 312 VAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLD---VCGDEEVRAKL 388
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAALIVKLL 271

                         250
                  ....*....|...
gi 2462621386 389 LELKHKHDALLRA 401
Cdd:COG0666   272 LLALLLLAAALLD 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 161-401 3.38e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.69  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 161 VRQFLGSGVSPDLANEDGLTALHQC-CIDDFREMVQQLLEAGANINACDSECWTPLHAAAT--CGHLHLVELLIASGANL 237
Cdd:PHA03095   66 VRLLLEAGADVNAPERCGFTPLHLYlYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 238 LAVNTDGNMPYDL------CDDEqTLDCLETAMADRgITQDSI---------EAARAVPELrmlddIRSRLQAGADLHAP 302
Cdd:PHA03095  146 NALDLYGMTPLAVllksrnANVE-LLRLLIDAGADV-YAVDDRfrsllhhhlQSFKPRARI-----VRELIRAGCDPAAT 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 303 LDHGATLLHVAAANGFSEAAAL--LLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLdvcg 380
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL---- 294

                         250       260
                  ....*....|....*....|.
gi 2462621386 381 deevrakLLELKHKHDALLRA 401
Cdd:PHA03095  295 -------SLMVRNNNGRAVRA 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
161-241 2.57e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 161 VRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEaGANINACDSEcWTPLHAAATCGHLHLVELLIASGANLLAV 240
Cdd:pfam12796  13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVK 90


                  .
gi 2462621386 241 N 241
Cdd:pfam12796  91 D 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 338-367 2.18e-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: 38.72  E-value: 2.18e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462621386  338 DGWEPLHAAAYWGQVPLVELLVAHGADLNA 367
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 160-270 2.99e-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: 43.85  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 160 EVRQFLGSGVsPDLANE-------DGLTALHQCCIDDFREMVQQLLEAGANIN---AC--------DSECW---TPLHAA 218
Cdd:cd22192    65 EAAVVLMEAA-PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVsprATgtffrpgpKNLIYygeHPLSFA 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462621386 219 ATCGHLHLVELLIASGANLLAVNTDGNMP----------------YDLC---DDEQTLDCLETAMADRGIT 270
Cdd:cd22192   144 ACVGNEEIVRLLIEHGADIRAQDSLGNTVlhilvlqpnktfacqmYDLIlsyDKEDDLQPLDLVPNNQGLT 214
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-401 1.19e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 1.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 152 AMVHRELWEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLI 231
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 232 ASGANLLAVNTDGNMPydlcddeqtldcLETAmadrgITQDSIEAARavpelrMLddirsrLQAGADLHAPLDHGATLLH 311
Cdd:COG0666   141 EAGADVNAQDNDGNTP------------LHLA-----AANGNLEIVK------LL------LEAGADVNARDNDGETPLH 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 312 VAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLD---VCGDEEVRAKL 388
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLlaaAAGAALIVKLL 271

                         250
                  ....*....|...
gi 2462621386 389 LELKHKHDALLRA 401
Cdd:COG0666   272 LLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
161-376 2.13e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 2.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 161 VRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAV 240
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 241 NTDGNMPYDLCddeqtldcletamadrgITQDSIEAARavpelrMLddirsrLQAGADLHAPLDHGATLLHVAAANGFSE 320
Cdd:COG0666   183 DNDGETPLHLA-----------------AENGHLEIVK------LL------LEAGADVNAKDNDGKTALDLAAENGNLE 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462621386 321 AAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPL 376
Cdd:COG0666   234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
224-394 1.27e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.32  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 224 LHLVELLIASGANLLAVNTDGNMPYDLCDDEQTLDCLETAMADRGITQDSIEAARAVPELRMLDDIRSRLQAGADLHAPL 303
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 304 DHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDV---CG 380
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNG 164

                         170
                  ....*....|....
gi 2462621386 381 DEEVrAKLLeLKHK 394
Cdd:COG0666   165 NLEI-VKLL-LEAG 176
PHA03095 PHA03095
ankyrin-like protein; Provisional
 161-401 3.38e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.69  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 161 VRQFLGSGVSPDLANEDGLTALHQC-CIDDFREMVQQLLEAGANINACDSECWTPLHAAAT--CGHLHLVELLIASGANL 237
Cdd:PHA03095   66 VRLLLEAGADVNAPERCGFTPLHLYlYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 238 LAVNTDGNMPYDL------CDDEqTLDCLETAMADRgITQDSI---------EAARAVPELrmlddIRSRLQAGADLHAP 302
Cdd:PHA03095  146 NALDLYGMTPLAVllksrnANVE-LLRLLIDAGADV-YAVDDRfrsllhhhlQSFKPRARI-----VRELIRAGCDPAAT 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 303 LDHGATLLHVAAANGFSEAAAL--LLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLdvcg 380
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL---- 294

                         250       260
                  ....*....|....*....|.
gi 2462621386 381 deevrakLLELKHKHDALLRA 401
Cdd:PHA03095  295 -------SLMVRNNNGRAVRA 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
161-241 2.57e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 161 VRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEaGANINACDSEcWTPLHAAATCGHLHLVELLIASGANLLAV 240
Cdd:pfam12796  13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVK 90


                  .
gi 2462621386 241 N 241
Cdd:pfam12796  91 D 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
293-368 9.21e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 9.21e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462621386 293 LQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHrASLSAKDqDGWEPLHAAAYWGQVPLVELLVAHGADLNAK 368
Cdd:pfam12796  17 LENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 188-376 6.73e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.63  E-value: 6.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 188 DDFReMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPYDLCDDEQTLDCLETAMADR 267
Cdd:PHA02876  156 DELL-IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 268 G-ITQDSIEAARAVPElrmlDDIRSRL---QAGADLHAPLDHGATLLHVAA-ANGFSEAAALLLEHRASLSAKDQDGWEP 342
Cdd:PHA02876  235 SnINKNDLSLLKAIRN----EDLETSLllyDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETP 310

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462621386 343 LHAAAYWG-QVPLVELLVAHGADLNAKSLMDETPL 376
Cdd:PHA02876  311 LYLMAKNGyDTENIRTLIMLGADVNAADRLYITPL 345
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 192-376 1.15e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.38  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 192 EMVQQLLEAGAN-INACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTdgNMPYDLCDDEQT-LDCLETAMADRGI 269
Cdd:PHA02874   15 EAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINT--KIPHPLLTAIKIgAHDIIKLLIDNGV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 270 TQDSIeaarAVPELRMlDDIRSRLQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYW 349
Cdd:PHA02874   93 DTSIL----PIPCIEK-DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167

                         170       180
                  ....*....|....*....|....*..
gi 2462621386 350 GQVPLVELLVAHGADLNAKSLMDETPL 376
Cdd:PHA02874  168 NFFDIIKLLLEKGAYANVKDNNGESPL 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-396 9.81e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 9.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 310 LHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHgADLNAKSlMDETPLDVC---GDEEVrA 386
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAarsGHLEI-V 77

                          90
                  ....*....|
gi 2462621386 387 KLLeLKHKHD 396
Cdd:pfam12796  78 KLL-LEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
182-336 1.11e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 182 LHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIAsganllavNTDGNMPydlcddeqtldcle 261
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--------HADVNLK-------------- 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462621386 262 tamadrgitqdsieaaravpelrmlddirsrlqagadlhaplDHGATLLHVAAANGFSEAAALLLEHRASLSAKD 336
Cdd:pfam12796  59 ------------------------------------------DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 187-376 4.90e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 187 IDDFREMVQQLLEAGANINACDSECWTPLHAAATC--GHLHLVELLIASGANLLAVNTDGNMPYdlcddeqtldcletAM 264
Cdd:PHA03100   82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL--------------HL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 265 ADRGITQDSieaaravpelrmldDIRSRLqagadlhapLDHGAtllHVAAANGFSeaaaLLLEHRASLSAKDQDGWEPLH 344
Cdd:PHA03100  148 YLESNKIDL--------------KILKLL---------IDKGV---DINAKNRVN----YLLSYGVPINIKDVYGFTPLH 197

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462621386 345 AAAYWGQVPLVELLVAHGADLNAKSLMDETPL 376
Cdd:PHA03100  198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
178-231 4.10e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 4.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462621386 178 GLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLI 231
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 286-401 2.79e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 2.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 286 LDDIRSRLQAGADLHAPLDHGATLLHVAAANGFS---EAAALLLEHRASLSAKDQDGWEPLHAAAYWGQV-PLVELLVAH 361
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462621386 362 GADLNAKSLMDETPLDVC-GDEEVRAKLLELkhkhdaLLRA 401
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYlSGFNINPKVIRL------LLRK 141
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 182-390 2.82e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 182 LHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIAS------GANLLAVNTDGN---------M 246
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvFYTLVAIKDAFNnrnveifkiI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 247 PYDLCDDEQTLDCLETAMADRgitQDSIEAaravpelrmlDDIRSRLQAGADLHAPLDH-GATLLHVAAANGFSEAAALL 325
Cdd:PHA02878  121 LTNRYKNIQTIDLVYIDKKSK---DDIIEA----------EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELL 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462621386 326 LEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDV----CGDEEVRAKLLE 390
Cdd:PHA02878  188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIsvgyCKDYDILKLLLE 256
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 152-366 9.86e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 9.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 152 AMVHRELWEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGA--NINACDSEcwTPLHAAATCGHLHLVEL 229
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDAVEEGDVKAVEE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 230 LIASGANLLAV-NTDGNMPYDLCDDEQTLDCLETAMAdrgitqdsieaaravpelrmlddirsrlqAGADLHAPLDHGAT 308
Cdd:PHA02875   87 LLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIA-----------------------------RGADPDIPNTDKFS 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462621386 309 LLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLN 366
Cdd:PHA02875  138 PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 161-378 3.12e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 161 VRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAV 240
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 241 NTDGNMPYDLCDDEQTLDCletamadrgitqdsieaaravpelrmlddIRSRLQAGADLHAPLDHGATLLHVAAAngFSE 320
Cdd:PHA02874  187 DNNGESPLHNAAEYGDYAC-----------------------------IKLLIDHGNHIMNKCKNGFTPLHNAII--HNR 235

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462621386 321 AAALLLEHRASLSAKDQDGWEPLH-AAAYWGQVPLVELLVAHGADLNAKSLMDETPLDV 378
Cdd:PHA02874  236 SAIELLINNASINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDT 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-359 3.46e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 3.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462621386 308 TLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLV 359
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 286-378 4.07e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 4.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 286 LDDIRSRLQAGADLHAPLDHGATLLHVAAANGFSEA-AALLLEHRASLSAKDQDGWEPLHA--AAYWGQVPLVELLVAHG 362
Cdd:PHA03095   63 KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKG 142

                          90
                  ....*....|....*.
gi 2462621386 363 ADLNAKSLMDETPLDV 378
Cdd:PHA03095  143 ADVNALDLYGMTPLAV 158
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 192-378 8.83e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 8.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 192 EMVQQLLEAGANINACDSECW-TPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPydlcddeqtldcLETAMADRgiT 270
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP------------LHHAVKHY--N 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 271 QDSIEAAravpelrmlddirsrLQAGADLHAPLDHGATLLHVAAANGFS-EAAALLLEHRASLSAKDQ-DGWEPLHAAAY 348
Cdd:PHA02878  214 KPIVHIL---------------LENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462621386 349 WGQVplVELLVAHGADLNAKSLMDETPLDV 378
Cdd:PHA02878  279 SERK--LKLLLEYGADINSLNSYKLTPLSS 306
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 194-282 2.80e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 194 VQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPYDLCDDEQTLDCLETAMadRGITQDS 273
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS--RHSQCHF 175


                  ....*....
gi 2462621386 274 IEAARAVPE 282
Cdd:PTZ00322  176 ELGANAKPD 184
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 191-376 3.19e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 191 REMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPYDLCDDEQTLDCletamadrgit 270
Cdd:PHA02874  104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI----------- 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 271 qdsieaaravpelrmlddIRSRLQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWG 350
Cdd:PHA02874  173 ------------------IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN 234

                         170       180
                  ....*....|....*....|....*.
gi 2462621386 351 QvPLVELLVaHGADLNAKSLMDETPL 376
Cdd:PHA02874  235 R-SAIELLI-NNASINDQDIDGSTPL 258
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 160-236 1.17e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.20  E-value: 1.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462621386 160 EVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGAN 236
Cdd:PHA03100  174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 193-438 1.36e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 193 MVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNmpydlcddeqtldcleTAMadrgitQD 272
Cdd:PLN03192  540 LLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN----------------TAL------WN 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 273 SIEAARavpelRMLDDIRSRLQAGADLHApldhGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQV 352
Cdd:PLN03192  598 AISAKH-----HKIFRILYHFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHV 668

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 353 PLVELLVAHGADLNAKSLMDE-TPLDVcgdEEVRAKlLELKHK------HDALLRAQSRQRSLLRRRTSSAGSRGKVVRR 425
Cdd:PLN03192  669 DMVRLLIMNGADVDKANTDDDfSPTEL---RELLQK-RELGHSitivdsVPADEPDLGRDGGSRPGRLQGTSSDNQCRPR 744

                         250
                  ....*....|...
gi 2462621386 426 VSLTQRTDLYRKQ 438
Cdd:PLN03192  745 VSIYKGHPLLRNE 757
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 161-376 1.50e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 161 VRQFLGSGVSPDLANEDGLTALHQCCIDDF-REMVQQLLEAGANINACDSECWTPLHAAATCG-HLHLVELLIASGANLL 238
Cdd:PHA02876  290 VPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 239 AvntdgnmpYDLCDdeqtldclETAMADRGITQDSIeaaravpelrmldDIRSRLQAGADLHAPLDHGATLLHVA--AAN 316
Cdd:PHA02876  370 A--------RDYCD--------KTPIHYAAVRNNVV-------------IINTLLDYGADIEALSQKIGTALHFAlcGTN 420

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462621386 317 GFSeAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVP-LVELLVAHGADLNAKSLMDETPL 376
Cdd:PHA02876  421 PYM-SVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPL 480
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 289-373 2.03e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 289 IRSRLQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGA---DL 365
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQchfEL 177


                  ....*...
gi 2462621386 366 NAKSLMDE 373
Cdd:PTZ00322  178 GANAKPDS 185
Ank_5 pfam13857
Ankyrin repeats (many copies);
197-251 1.11e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462621386 197 LLEAG-ANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPYDLC 251
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 175-391 2.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 175 NEDGLTALHQCCIDDFrEMVQQLLEAGANINACDSECWTPLHAAATCGHL-HLVELLIASGANLLAVNTDGNMPYDLCD- 252
Cdd:PHA02876  238 NKNDLSLLKAIRNEDL-ETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAk 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 253 ---DEQTLDCLETAMADRGITqDSIEAA---RAVPELRMLDDIRSRLQAGADLHAPLDHGATLLHVAAANGFSEAAALLL 326
Cdd:PHA02876  317 ngyDTENIRTLIMLGADVNAA-DRLYITplhQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462621386 327 EHRASLSAKDQDGWEPLHAAAYwGQVPL--VELLVAHGADLNAKSLMDETPLDVCGDEEVRAKLLEL 391
Cdd:PHA02876  396 DYGADIEALSQKIGTALHFALC-GTNPYmsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEM 461
Ank_5 pfam13857
Ankyrin repeats (many copies);
325-379 2.29e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462621386 325 LLEHR-ASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDVC 379
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 314-385 2.57e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462621386 314 AANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDVCGDEEVR 385
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 157-376 3.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 157 ELWEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGAN 236
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 237 llaVNTDGNMPYDLCDDEQtldcLETAMA--DRGITQDSIEA--------ARAVPELRMLddIRSRLQAGADLHAPLDHG 306
Cdd:PHA02876  237 ---INKNDLSLLKAIRNED----LETSLLlyDAGFSVNSIDDckntplhhASQAPSLSRL--VPKLLERGADVNAKNIKG 307

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462621386 307 ATLLHVAAANGF-SEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQ-----VPLVELlvahGADLNAKSLMDETPL 376
Cdd:PHA02876  308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRnkdivITLLEL----GANVNARDYCDKTPI 379
Ank_4 pfam13637
Ankyrin repeats (many copies);
339-389 4.05e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462621386 339 GWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDVC---GDEEVrAKLL 389
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasnGNVEV-LKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-247 4.21e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 175 NEDGLTALHQ---CCIDDFrEMVQQLLEAGANINACDS---------------EC-WTPLHAAATCGHLHLVELLIASGA 235
Cdd:PHA03100  138 NSDGENLLHLyleSNKIDL-KILKLLIDKGVDINAKNRvnyllsygvpinikdVYgFTPLHYAVYNNNPEFVKYLLDLGA 216

                          90
                  ....*....|..
gi 2462621386 236 NLLAVNTDGNMP 247
Cdd:PHA03100  217 NPNLVNKYGDTP 228
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 152-377 4.34e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 152 AMVHRELWEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLI 231
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 232 ASGANLLAVNTDGNMPydlcddeqtldcLETAMadrgitqdsIEAARAVPELrmlddIRSRLQAGADLhapldHGATLLH 311
Cdd:PHA02874  211 DHGNHIMNKCKNGFTP------------LHNAI---------IHNRSAIELL-----INNASINDQDI-----DGSTPLH 259

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462621386 312 VAAANGFS-EAAALLLEHRASLSAKDQDGWEPLHAA-AYWGQVPLVELLVAHGADLN-AKSLMDETPLD 377
Cdd:PHA02874  260 HAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAfKYINKDPVIKDIIANAVLIKeADKLKDSDFLE 328
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 212-241 6.41e-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: 40.35  E-value: 6.41e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462621386 212 WTPLHAAAT-CGHLHLVELLIASGANLLAVN 241
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 338-368 1.87e-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: 38.81  E-value: 1.87e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462621386 338 DGWEPLHAAAY-WGQVPLVELLVAHGADLNAK 368
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 338-367 2.18e-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: 38.72  E-value: 2.18e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462621386  338 DGWEPLHAAAYWGQVPLVELLVAHGADLNA 367
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 160-270 2.99e-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: 43.85  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 160 EVRQFLGSGVsPDLANE-------DGLTALHQCCIDDFREMVQQLLEAGANIN---AC--------DSECW---TPLHAA 218
Cdd:cd22192    65 EAAVVLMEAA-PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVsprATgtffrpgpKNLIYygeHPLSFA 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462621386 219 ATCGHLHLVELLIASGANLLAVNTDGNMP----------------YDLC---DDEQTLDCLETAMADRGIT 270
Cdd:cd22192   144 ACVGNEEIVRLLIEHGADIRAQDSLGNTVlhilvlqpnktfacqmYDLIlsyDKEDDLQPLDLVPNNQGLT 214
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 212-237 3.20e-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: 3.20e-04
                           10        20
                   ....*....|....*....|....*.
gi 2462621386  212 WTPLHAAATCGHLHLVELLIASGANL 237
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 338-367 3.31e-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: 38.01  E-value: 3.31e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462621386 338 DGWEPLHAAAYWGQVPLVELLVAHGADLNA 367
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 161-230 3.33e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 3.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 161 VRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELL 230
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 293-364 4.71e-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: 4.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462621386 293 LQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASL------SAKDQdGWEPLHAAAYWGQVPLVELLVAHGAD 364
Cdd:cd22192    38 KCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmtSDLYQ-GETALHIAVVNQNLNLVRELIARGAD 114
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 177-206 5.09e-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: 5.09e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462621386 177 DGLTALHQCCIDDFREMVQQLLEAGANINA 206
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 161-376 5.18e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 161 VRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGH--LHLVELLIASGANL- 237
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIn 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 238 LAVNTDGNMPYDLCDDeqtldcletamadrgitqdsieaaravPELRMLDDIRSrLQAGADLHAPLDHGATLLHVAAANG 317
Cdd:PHA02946  135 NSVDEEGCGPLLACTD---------------------------PSERVFKKIMS-IGFEARIVDKFGKNHIHRHLMSDNP 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462621386 318 FSEAAALLLEHRASLSAKDQDGWEPLH--AAAYWGQVPLVELLVAhGADLNAKSLMDETPL 376
Cdd:PHA02946  187 KASTISWMMKLGISPSKPDHDGNTPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPL 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 177-208 5.79e-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. 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: 5.79e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462621386 177 DGLTALHQCCID-DFREMVQQLLEAGANINACD 208
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
211-247 7.08e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 7.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462621386 211 CWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMP 247
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 322-377 7.83e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 7.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462621386 322 AALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLD 377
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 177-206 9.73e-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: 36.80  E-value: 9.73e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462621386  177 DGLTALHQCCIDDFREMVQQLLEAGANINA 206
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
169-218 1.54e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462621386 169 VSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAA 218
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 212-239 3.33e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 3.33e-03
                          10        20
                  ....*....|....*....|....*...
gi 2462621386 212 WTPLHAAATCGHLHLVELLIASGANLLA 239
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 192-246 3.34e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.62  E-value: 3.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462621386 192 EMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNM 246
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
Ank_5 pfam13857
Ankyrin repeats (many copies);
297-346 3.60e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 3.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462621386 297 ADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAA 346
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 306-390 6.05e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.20  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621386 306 GATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDVC---GDE 382
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAmakGDI 181


                  ....*...
gi 2462621386 383 EVRAKLLE 390
Cdd:PHA02875  182 AICKMLLD 189
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 178-235 6.95e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 39.23  E-value: 6.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462621386 178 GLTALHQCCIDDFREMVQQLLEAGANI--NACDSECW---TPLHAAATCGHLHLVELLIASGA 235
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDLYqgeTALHIAVVNQNLNLVRELIARGA 113
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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