NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|46519154|ref|NP_078944|]
View 

ankyrin repeat and KH domain-containing protein 1 isoform 3 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13333862)

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

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];
285-572 2.09e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 2.09e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 285 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 364
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 365 NThSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 444
Cdd:COG0666  81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 445 AACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFL 524
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46519154 525 IKAGADIELGC---STPLMEASQEGHLELVKYLLASGANVHATTATGDTAL 572
Cdd:COG0666 239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
144-409 8.61e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 8.61e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 144 ARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMKAENSHNAGQVDTRSLAEACSDGDVNAVRK 223
Cdd:COG0666  26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 224 LLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSA 303
Cdd:COG0666 106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 304 TGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKG 383
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAG 263

                       250       260
                ....*....|....*....|....*.
gi 46519154 384 HLDMVRFLLEAGADQEHKTDEMHTAL 409
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 568-596 1.61e-04

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


:

Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.61e-04
                           10        20
                   ....*....|....*....|....*....
gi 46519154    568 GDTALTYACENGHTDVADVLLQAGADLDK 596
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
285-572 2.09e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 2.09e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 285 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 364
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 365 NThSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 444
Cdd:COG0666  81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 445 AACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFL 524
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46519154 525 IKAGADIELGC---STPLMEASQEGHLELVKYLLASGANVHATTATGDTAL 572
Cdd:COG0666 239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
144-409 8.61e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 8.61e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 144 ARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMKAENSHNAGQVDTRSLAEACSDGDVNAVRK 223
Cdd:COG0666  26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 224 LLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSA 303
Cdd:COG0666 106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 304 TGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKG 383
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAG 263

                       250       260
                ....*....|....*....|....*.
gi 46519154 384 HLDMVRFLLEAGADQEHKTDEMHTAL 409
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 211-531 6.86e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.19  E-value: 6.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  211 EACSDGDVNAVRKLLDEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGNKGDiTPLMA-ASSGGYLD 286
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  287 IVKLLLLHDADVNSQSATGNTALtYACAGGF---VDIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVLLDH 360
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  361 GAGI-----------NTHSNEFKESAltlacykghlDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 427
Cdd:PHA03095 177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  428 GAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINA-------- 499
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETvaatlnta 326

                        330       340       350
                 ....*....|....*....|....*....|...
gi 46519154  500 -QTEETQETALTLACcggfseVADFLIKAGADI 531
Cdd:PHA03095 327 sVAGGDIPSDATRLC------VAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-366 1.68e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   276 LMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANieDHNENGHTPLMEAASAGHVEVAR 355
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 46519154   356 VLLDHGAGINT 366
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-301 7.03e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 7.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   209 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGNkgdiTPLMAASSGGYLDI 287
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNGR----TALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 46519154   288 VKLLLLHDADVNSQ 301
Cdd:pfam12796  77 VKLLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-512 7.34e-12

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: 68.12  E-value: 7.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 340 TPLMEAASAGHVEVARVLLdhgagINTHSNEFK-----ESALTLACYKGHLDMVRFLLEAGAD--QEHKTDEMH---TAL 409
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLL-----KCPSCDLFQrgalgETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTAL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 410 MEACMDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL 475
Cdd:cd22192  94 HIAVVNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 46519154 476 ----MEAAREGHEEMVALLLAQGANINAQTEETQE-----TALTLA 512
Cdd:cd22192 174 hilvLQPNKTFACQMYDLILSYDKEDDLQPLDLVPnnqglTPFKLA 219
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 216-337 1.75e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  216 GDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR--------------GNKGDiTPLM 277
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsygvpinikDVYGF-TPLH 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  278 AASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 337
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 312-465 1.90e-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: 50.85  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   312 ACAGGFVDIVKVLLNEGA--NIEDHNENGHTPLMEAASAG-HVEVARVLLDHGAGINThsnefkESALTLACYKGHLDMV 388
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV------GDTLLHAISLEYVDAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   389 ----RFLLEAGADQ-------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ES 440
Cdd:TIGR00870  98 eailLHLLAAFRKSgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgES 177

                         170       180
                  ....*....|....*....|....*
gi 46519154   441 PLTLAACGGHVELAALLIERGANLE 465
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADIL 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 470-499 2.63e-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: 41.42  E-value: 2.63e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 46519154    470 EGYTPLMEAAREGHEEMVALLLAQGANINA 499
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 568-596 1.61e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.61e-04
                           10        20
                   ....*....|....*....|....*....
gi 46519154    568 GDTALTYACENGHTDVADVLLQAGADLDK 596
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 551-605 1.64e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46519154  551 VKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGAD---LDKqeDMKTILE 605
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADptlLDK--DGKTPLE 153
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 568-596 2.55e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 2.55e-03
                          10        20
                  ....*....|....*....|....*....
gi 46519154   568 GDTALTYACENGHTDVADVLLQAGADLDK 596
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
285-572 2.09e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 2.09e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 285 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 364
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 365 NThSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 444
Cdd:COG0666  81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 445 AACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFL 524
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46519154 525 IKAGADIELGC---STPLMEASQEGHLELVKYLLASGANVHATTATGDTAL 572
Cdd:COG0666 239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-436 1.43e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 1.43e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 155 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMKAENSHNAGQVDTRSLAEACSDGDVNAVRKLLDEGRSVNEH 234
Cdd:COG0666   4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 235 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACA 314
Cdd:COG0666  84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 315 GGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHsNEFKESALTLACYKGHLDMVRFLLEA 394
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 46519154 395 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 436
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
357-617 3.12e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.73  E-value: 3.12e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 357 LLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 436
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 437 SFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGG 516
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANG 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 517 FSEVADFLIKAGADIELGCS---TPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGAD 593
Cdd:COG0666 165 NLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                       250       260
                ....*....|....*....|....
gi 46519154 594 LDKQEDMKTILEGIDPAKHQVRVA 617
Cdd:COG0666 245 LNAKDKDGLTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
144-409 8.61e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 8.61e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 144 ARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMKAENSHNAGQVDTRSLAEACSDGDVNAVRK 223
Cdd:COG0666  26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 224 LLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSA 303
Cdd:COG0666 106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 304 TGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKG 383
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAG 263

                       250       260
                ....*....|....*....|....*.
gi 46519154 384 HLDMVRFLLEAGADQEHKTDEMHTAL 409
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
385-599 1.58e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 1.58e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 385 LDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANL 464
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 465 EEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFLIKAGADIEL---GCSTPLME 541
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAqdnDGNTPLHL 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46519154 542 ASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDKQED 599
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
PHA03095 PHA03095
ankyrin-like protein; Provisional
 211-531 6.86e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.19  E-value: 6.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  211 EACSDGDVNAVRKLLDEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGNKGDiTPLMA-ASSGGYLD 286
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  287 IVKLLLLHDADVNSQSATGNTALtYACAGGF---VDIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVLLDH 360
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  361 GAGI-----------NTHSNEFKESAltlacykghlDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 427
Cdd:PHA03095 177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  428 GAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINA-------- 499
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETvaatlnta 326

                        330       340       350
                 ....*....|....*....|....*....|...
gi 46519154  500 -QTEETQETALTLACcggfseVADFLIKAGADI 531
Cdd:PHA03095 327 sVAGGDIPSDATRLC------VAKVVLRGAFSL 353
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 418-595 7.58e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 107.44  E-value: 7.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  418 VEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-----ELAALLIERGANLEEVNDEGYTPLMEAARE--GHEEMVALL 490
Cdd:PHA03100  48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  491 LAQGANINAQTEeTQETALTLA--CCGGFSEVADFLIKAGADI----------ELGC---------STPLMEASQEGHLE 549
Cdd:PHA03100 128 LDNGANVNIKNS-DGENLLHLYleSNKIDLKILKLLIDKGVDInaknrvnyllSYGVpinikdvygFTPLHYAVYNNNPE 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 46519154  550 LVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLD 595
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 197-594 7.95e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 106.30  E-value: 7.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  197 NSHNAGQVDTRSLAEACSDGDV--NAVRKLLDEGRSVNEHTEEGESLLclacsagyyelAQVLLAMHANVedrgNKGDI- 273
Cdd:PHA02876 113 NKHKLDEACIHILKEAISGNDIhyDKINESIEYMKLIKERIQQDELLI-----------AEMLLEGGADV----NAKDIy 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  274 --TPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIedhNENGHTpLMEAASAGHV 351
Cdd:PHA02876 178 ciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI---NKNDLS-LLKAIRNEDL 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  352 EVARVLLDHGAGINThSNEFKESALTLACYKGHLD-MVRFLLEAGADQEHKTDEMHTALMEACMDGH-VEVARLLLDSGA 429
Cdd:PHA02876 254 ETSLLLYDAGFSVNS-IDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGA 332

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  430 QVNMPADSFESPLTLAAC-GGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQeTA 508
Cdd:PHA02876 333 DVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TA 411

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  509 LTLACCGG--FSEVADfLIKAGADIELG---CSTPLMEASQEG-HLELVKYLLASGANVHATTATGDTALTYACenGHTD 582
Cdd:PHA02876 412 LHFALCGTnpYMSVKT-LIDRGANVNSKnkdLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHG 488

                        410
                 ....*....|..
gi 46519154  583 VADVLLQAGADL 594
Cdd:PHA02876 489 IVNILLHYGAEL 500
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 260-499 2.57e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 102.82  E-value: 2.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  260 MHANVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFV-----DIVKVLLNEGANIEDH 334
Cdd:PHA03100  23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  335 NENGHTPLMEAASA--GHVEVARVLLDHGAGINTHSNEFKES-ALTLACYKGHLDMVRFLLEAGADQEHKTDemhtalme 411
Cdd:PHA03100 103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLlHLYLESNKIDLKILKLLIDKGVDINAKNR-------- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  412 acmdghVEvarLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLL 491
Cdd:PHA03100 175 ------VN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245


                 ....*...
gi 46519154  492 AQGANINA 499
Cdd:PHA03100 246 NNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-366 1.68e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   276 LMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANieDHNENGHTPLMEAASAGHVEVAR 355
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 46519154   356 VLLDHGAGINT 366
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
309-401 3.02e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 3.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   309 LTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHgagINTHSNEFKESALTLACYKGHLDMV 388
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 46519154   389 RFLLEAGADQEHK 401
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 318-603 1.19e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  318 VDIVKVLLNEGANIEDHNENGHTPL---MEAASAGHVEVARVLLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEA 394
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  395 GADQEHKTDEMHTALmEACMDG---HVEVARLLLDSGAQVNmpaDSFESPLTLAAC-----GGHVELAALLIERGANLEE 466
Cdd:PHA03095 107 GADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVN---ALDLYGMTPLAVllksrNANVELLRLLIDAGADVYA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  467 VNDEGYTPL---MEAAREgHEEMVALLLAQGANINAqTEETQETALTLACCGGF---SEVADFLIkAGADIE----LGcS 536
Cdd:PHA03095 183 VDDRFRSLLhhhLQSFKP-RARIVRELIRAGCDPAA-TDMLGNTPLHSMATGSSckrSLVLPLLI-AGISINarnrYG-Q 258

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46519154  537 TPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADvllqagADLDKQEDMKTI 603
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR------AALAKNPSAETV 319
Ank_2 pfam12796
Ankyrin repeats (3 copies);
409-500 2.26e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 2.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   409 LMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANleEVNDEGYTPLMEAAREGHEEMVA 488
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 46519154   489 LLLAQGANINAQ 500
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 307-594 1.54e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.48  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  307 TALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGagINThsnefkeSALTLACYKGhlD 386
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDT-------SILPIPCIEK--D 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  387 MVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEE 466
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  467 VNDEGYTPLMEAAREGHEEMVALLLAQGANINAQteetqetaltlaCCGGFsevadflikagadielgcsTPLMEASQeg 546
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK------------CKNGF-------------------TPLHNAII-- 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46519154  547 HLELVKYLLASGANVHATTATGDTALTYA----CEnghTDVADVLLQAGADL 594
Cdd:PHA02874 233 HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADI 281
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 337-593 2.12e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.74  E-value: 2.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  337 NGHTPLMEAASAGHVEVARVLLDHGAGIN-THSNEFkeSALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMD 415
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNfEIYDGI--SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  416 GHVEVARLLLDSGAQVNmpaDSF----ESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLL 491
Cdd:PHA02875  79 GDVKAVEELLDLGKFAD---DVFykdgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  492 AQganinaqteetqetaltlaccggfsevadfliKAGADIELGCS-TPLMEASQEGHLELVKYLLASGANVHATTATGD- 569
Cdd:PHA02875 156 DH--------------------------------KACLDIEDCCGcTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCv 203

                        250       260
                 ....*....|....*....|....
gi 46519154  570 TALTYACENGHTDVADVLLQAGAD 593
Cdd:PHA02875 204 AALCYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
342-432 2.19e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 2.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   342 LMEAASAGHVEVARVLLDHGAGINTHsNEFKESALTLACYKGHLDMVRFLLEaGADQEHKTDEMhTALMEACMDGHVEVA 421
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIV 77

                          90
                  ....*....|.
gi 46519154   422 RLLLDSGAQVN 432
Cdd:pfam12796  78 KLLLEKGADIN 88
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 285-595 3.03e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.97  E-value: 3.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  285 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 364
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  365 NTHsnefkESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGhvEVARL---LLDSGAQVNMPADSFESP 441
Cdd:PHA02876 238 NKN-----DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAP--SLSRLvpkLLERGADVNAKNIKGETP 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  442 LTLAACGGH-VELAALLIERGANLEEVNDEGYTPLMEAAR-EGHEEMVALLLAQGANINAQtEETQETALTLACCGGFSE 519
Cdd:PHA02876 311 LYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNAR-DYCDKTPIHYAAVRNNVV 389

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  520 VADFLIKAGADIE-----LGCSTPLMEASQEGHLElVKYLLASGANVHATTATGDTALTYACENG-HTDVADVLLQAGAD 593
Cdd:PHA02876 390 IINTLLDYGADIEalsqkIGTALHFALCGTNPYMS-VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468


                 ..
gi 46519154  594 LD 595
Cdd:PHA02876 469 VN 470
Ank_2 pfam12796
Ankyrin repeats (3 copies);
475-564 5.54e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 5.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   475 LMEAAREGHEEMVALLLAQGANINAQTEETQeTALTLACCGGFSEVADFLI-KAGADIELGCSTPLMEASQEGHLELVKY 553
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLLeHADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 46519154   554 LLASGANVHAT 564
Cdd:pfam12796  80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
442-533 7.94e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 7.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   442 LTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQgANINAQTEetQETALTLACCGGFSEVA 521
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77

                          90
                  ....*....|..
gi 46519154   522 DFLIKAGADIEL 533
Cdd:pfam12796  78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 217-366 1.04e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 1.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  217 DVNAVRKLLDEGRSVNEHTEEGES-LLCLAC-SAGYYELAQVLLAMHANVEDRGNKGdITPLMAASSGGY--LDIVKLLL 292
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITpLLYAISkKSNSYSIVEYLLDNGANVNIKNSDG-ENLLHLYLESNKidLKILKLLI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  293 LHDADVN----------------SQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARV 356
Cdd:PHA03100 164 DKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                        170
                 ....*....|
gi 46519154  357 LLDHGAGINT 366
Cdd:PHA03100 244 LLNNGPSIKT 253
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 283-533 1.43e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 82.35  E-value: 1.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  283 GYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGAnIEDHNENG-HTPLMEAASAGHVEVARVLLDHG 361
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  362 AGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 441
Cdd:PHA02875  92 KFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  442 LTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHE-EMVALLLAQGANINAQTEETQETALTLA-----CCG 515
Cdd:PHA02875 172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNIMFMIEGEECTILDmicnmCTN 251

                        250
                 ....*....|....*...
gi 46519154  516 GFSEVADFLIkagADIEL 533
Cdd:PHA02875 252 LESEAIDALI---ADIAI 266
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 308-530 1.53e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 82.35  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  308 ALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEFkESALTLACYKGHLDM 387
Cdd:PHA02875   5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  388 VRFLLEAG--ADQEHKTDEMhTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLE 465
Cdd:PHA02875  84 VEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46519154  466 EVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTLACCGGFSEVADFLIKAGAD 530
Cdd:PHA02875 163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 217-413 3.32e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.19  E-value: 3.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  217 DVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDA 296
Cdd:PHA02875  47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  297 DVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEFKESAL 376
Cdd:PHA02875 127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 46519154  377 TLACYKGHLDMVRFLLEAGADQEHKT---DEMHTALMEAC 413
Cdd:PHA02875 207 CYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDMIC 246
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 263-444 5.43e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.84  E-value: 5.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  263 NVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL 342
Cdd:PLN03192 516 NGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  343 MEAASAGHVEVARVLLDHGAGINTHSNefkESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVAR 422
Cdd:PLN03192 596 WNAISAKHHKIFRILYHFASISDPHAA---GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672

                        170       180
                 ....*....|....*....|...
gi 46519154  423 LLLDSGAQVNMPA-DSFESPLTL 444
Cdd:PLN03192 673 LLIMNGADVDKANtDDDFSPTEL 695
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-301 7.03e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 7.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   209 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGNkgdiTPLMAASSGGYLDI 287
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNGR----TALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 46519154   288 VKLLLLHDADVNSQ 301
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
509-597 5.49e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 5.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   509 LTLACCGGFSEVADFLIKAGADIELGCS---TPLMEASQEGHLELVKYLLaSGANVHATTAtGDTALTYACENGHTDVAD 585
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKngrTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 46519154   586 VLLQAGADLDKQ 597
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 275-531 2.70e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 2.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  275 PLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEgaNIEDHNENGHTPLMEAASAGHVEVA 354
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  355 RVLLdhgagINTHSNEfKESALTLACYKGHLD-----MVRFLLEAGADQEHKT-DEMHTALMEACMDGHVEVARLLLDSG 428
Cdd:PHA02878 118 KIIL-----TNRYKNI-QTIDLVYIDKKSKDDiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  429 AQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL-MEAAREGHEEMVALLLAQGANINAQTEETQET 507
Cdd:PHA02878 192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLT 271

                        250       260
                 ....*....|....*....|....
gi 46519154  508 ALTLACCGgfSEVADFLIKAGADI 531
Cdd:PHA02878 272 ALHSSIKS--ERKLKLLLEYGADI 293
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 318-595 3.91e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 3.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  318 VDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLdhgAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGAD 397
Cdd:PHA02878  50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  398 QEHKTDEMHtaLMEACMDGHVE--VARLLLDSGAQVNM-PADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTP 474
Cdd:PHA02878 127 NIQTIDLVY--IDKKSKDDIIEaeITKLLLSYGADINMkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  475 LMEAAREGHEEMVALLLAQGANINAQTEetqetaltlacCGgfsevadflikagadielgcSTPL-MEASQEGHLELVKY 553
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDK-----------CG--------------------NTPLhISVGYCKDYDILKL 253

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 46519154  554 LLASGANVHA-TTATGDTALTYACENghTDVADVLLQAGADLD 595
Cdd:PHA02878 254 LLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADIN 294
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 207-397 5.81e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 5.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  207 RSLAEACSDGDVNAVRKLLdegrsVNEHTEEGESLLCLACSAGY-----YELAQVLLAMHANVEDRGNKGDITPLMAASS 281
Cdd:PHA02878 103 VAIKDAFNNRNVEIFKIIL-----TNRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  282 GGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL-MEAASAGHVEVARVLLDH 360
Cdd:PHA02878 178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 46519154  361 GAGINTHSNEFKESALTLACYKGhlDMVRFLLEAGAD 397
Cdd:PHA02878 258 GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGAD 292
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 418-596 6.61e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 6.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  418 VEVARLLLDSGAQVNMPADSFeSPLTLAACGGHVELAALLieRGANLEEVND-EGYTPLMEAAREGHEEMVALLLAQGAN 496
Cdd:PLN03192 507 LNVGDLLGDNGGEHDDPNMAS-NLLTVASTGNAALLEELL--KAKLDPDIGDsKGRTPLHIAASKGYEDCVLVLLKHACN 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  497 INAQtEETQETALTLACCGGFSEVADFLIK--------AGADIelgcstpLMEASQEGHLELVKYLLASGANVHATTATG 568
Cdd:PLN03192 584 VHIR-DANGNTALWNAISAKHHKIFRILYHfasisdphAAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655

                        170       180
                 ....*....|....*....|....*...
gi 46519154  569 DTALTYACENGHTDVADVLLQAGADLDK 596
Cdd:PLN03192 656 ATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 408-595 6.77e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.79  E-value: 6.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  408 ALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAnLEEVNDEGY-TPLMEAAREGHEEM 486
Cdd:PHA02875   5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  487 VALLLAQGANINAQTEETQETALTLACCGGFSEVADFLIKAGADIELGCS---TPLMEASQEGHLELVKYLLASGANVHA 563
Cdd:PHA02875  84 VEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTdkfSPLHLAVMMGDIKGIELLIDHKACLDI 163

                        170       180       190
                 ....*....|....*....|....*....|..
gi 46519154  564 TTATGDTALTYACENGHTDVADVLLQAGADLD 595
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
539-604 2.97e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 2.97e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46519154   539 LMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQaGADLDKQEDMKTIL 604
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTAL 65
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-512 7.34e-12

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: 68.12  E-value: 7.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 340 TPLMEAASAGHVEVARVLLdhgagINTHSNEFK-----ESALTLACYKGHLDMVRFLLEAGAD--QEHKTDEMH---TAL 409
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLL-----KCPSCDLFQrgalgETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTAL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 410 MEACMDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL 475
Cdd:cd22192  94 HIAVVNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 46519154 476 ----MEAAREGHEEMVALLLAQGANINAQTEETQE-----TALTLA 512
Cdd:cd22192 174 hilvLQPNKTFACQMYDLILSYDKEDDLQPLDLVPnnqglTPFKLA 219
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 209-445 9.81e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 9.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  209 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAG-----------------YYELAQVLLAMH---------- 261
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPnklgmkemirsinkcsvFYTLVAIKDAFNnrnveifkii 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  262 -ANVEDRGNKGDITPLMAASSGGYLD--IVKLLLLHDADVNSQSA-TGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 337
Cdd:PHA02878 121 lTNRYKNIQTIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  338 GHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLAC-YKGHLDMVRFLLEAGADQEHKTDEMH-TALMEACMD 415
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTD-ARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKS 279

                        250       260       270
                 ....*....|....*....|....*....|
gi 46519154  416 GhvEVARLLLDSGAQVNMPADSFESPLTLA 445
Cdd:PHA02878 280 E--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02798 PHA02798
ankyrin-like protein; Provisional
 285-502 5.09e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 65.24  E-value: 5.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  285 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFV---DIVKVLLNEGANIEDHNENGHTPLMEAASAGH---VEVARVLL 358
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  359 DHGAGINTHSNEFKESalTLACY------KGHLDMVRFLLEAG-----ADQEHKTDemhtaLMEACMDghvevarLLLDS 427
Cdd:PHA02798 169 EKGVDINTHNNKEKYD--TLHCYfkynidRIDADILKLFVDNGfiinkENKSHKKK-----FMEYLNS-------LLYDN 234

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46519154  428 GaqvNMPADSFEspltlaacgghvelaalLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTE 502
Cdd:PHA02798 235 K---RFKKNILD-----------------FIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 206-369 7.08e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 7.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  206 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLL-------------------------AM 260
Cdd:PHA02874  36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdmiktildcGI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  261 HANVEDRGNKgdiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHT 340
Cdd:PHA02874 116 DVNIKDAELK---TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                        170       180
                 ....*....|....*....|....*....
gi 46519154  341 PLMEAASAGHVEVARVLLDHGAGINTHSN 369
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKCK 221
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 216-337 1.75e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  216 GDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR--------------GNKGDiTPLM 277
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsygvpinikDVYGF-TPLH 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  278 AASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 337
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 403-594 2.82e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 2.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  403 DEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAnleevnDEGYTPLMEAareg 482
Cdd:PHA02874  33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGV------DTSILPIPCI---- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  483 HEEMVALLLAQGANINAQTEETQeTALTLACCGGFSEVADFLIKAGADIEL----GCsTPLMEASQEGHLELVKYLLASG 558
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIeddnGC-YPIHIAIKHNFFDIIKLLLEKG 180

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 46519154  559 ANVHATTATGDTALTYACENGHTDVADVLLQAGADL 594
Cdd:PHA02874 181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
535-588 3.35e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 3.35e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46519154   535 CSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLL 588
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 204-345 8.75e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 8.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  204 VDTRSLAEACSDGDVnaVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDItPLMAASSGG 283
Cdd:PHA02874  92 VDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY-PIHIAIKHN 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46519154  284 YLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEA 345
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 284-589 4.53e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 58.98  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  284 YLDIVKLLLLHDADVNSQSaTGNTALTYACAGGFV--DIVKVLLNEGANIedhNENGH--TPL------MEAASAGHVEV 353
Cdd:PHA02989  15 DKNALEFLLRTGFDVNEEY-RGNSILLLYLKRKDVkiKIVKLLIDNGADV---NYKGYieTPLcavlrnREITSNKIKKI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  354 ARVLLDHGAGINTHSneFKESAlTLAC--YKGH---LDMVRFLLEAGADQEHKTDE-----MHTALmEACMDgHVEVARL 423
Cdd:PHA02989  91 VKLLLKFGADINLKT--FNGVS-PIVCfiYNSNinnCDMLRFLLSKGINVNDVKNSrgynlLHMYL-ESFSV-KKDVIKI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  424 LLDSGAQVNMPADSFE-SPLTL----AACGGHVELAALLIERGANLEEvNDEGYTPLMEAAREGHEEMValllaqganin 498
Cdd:PHA02989 166 LLSFGVNLFEKTSLYGlTPMNIylrnDIDVISIKVIKYLIKKGVNIET-NNNGSESVLESFLDNNKILS----------- 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  499 aqteeTQETaltlaccggfsEVADFL---IKAGADIELGCsTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYA 575
Cdd:PHA02989 234 -----KKEF-----------KVLNFIlkyIKINKKDKKGF-NPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296

                        330
                 ....*....|....
gi 46519154  576 CENGHTDVADVLLQ 589
Cdd:PHA02989 297 IKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
338-392 5.66e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.66e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 46519154   338 GHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKGHLDMVRFLL 392
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-325 6.07e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 6.07e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 46519154   274 TPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLL 325
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 449-599 1.55e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  449 GHVELAALLIERGANLEEVN-DEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTlACCGGFSEVADFLIKA 527
Cdd:PHA02874  12 GDIEAIEKIIKNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLT-AIKIGAHDIIKLLIDN 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46519154  528 GADIELgCSTPLMEAsqeghlELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDKQED 599
Cdd:PHA02874  91 GVDTSI-LPIPCIEK------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
Ank_4 pfam13637
Ankyrin repeats (many copies);
440-491 2.91e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.91e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 46519154   440 SPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLL 491
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 193-378 6.10e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 6.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  193 MKAENS--HNAGQVDTRSLAEAcSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNK 270
Cdd:PLN03192 512 LLGDNGgeHDDPNMASNLLTVA-STGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  271 GDiTPLMAASSGGYLDIVKlLLLHDADVNSQSATGNTaLTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGH 350
Cdd:PLN03192 591 GN-TALWNAISAKHHKIFR-ILYHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667

                        170       180
                 ....*....|....*....|....*....
gi 46519154  351 VEVARVLLDHGAGInTHSNEFKE-SALTL 378
Cdd:PLN03192 668 VDMVRLLIMNGADV-DKANTDDDfSPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
405-458 7.23e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 7.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46519154   405 MHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLI 458
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
305-358 1.35e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.35e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46519154   305 GNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLL 358
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
374-425 4.18e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 4.18e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 46519154   374 SALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLL 425
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
471-525 6.01e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 6.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 46519154   471 GYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFLI 525
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 217-492 1.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 51.28  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  217 DVNAVRKLLDEGRSVNEhTEEGESLLCLACSAGYY--ELAQVLLAMHANVEDRGNKGdiTPLMAA------SSGGYLDIV 288
Cdd:PHA02989  15 DKNALEFLLRTGFDVNE-EYRGNSILLLYLKRKDVkiKIVKLLIDNGADVNYKGYIE--TPLCAVlrnreiTSNKIKKIV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  289 KLLLLHDADVNSQSATGNTALT---YACAGGFVDIVKVLLNEGANIED-HNENGHTPL---MEAASAgHVEVARVLLDHG 361
Cdd:PHA02989  92 KLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRFLLSKGINVNDvKNSRGYNLLhmyLESFSV-KKDVIKILLSFG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  362 AGINTHSNEFKESALTLacYKGH------LDMVRFLLEAGADQEhKTDEMHTALMEACMDGH-------VEVARLLLdSG 428
Cdd:PHA02989 171 VNLFEKTSLYGLTPMNI--YLRNdidvisIKVIKYLIKKGVNIE-TNNNGSESVLESFLDNNkilskkeFKVLNFIL-KY 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46519154  429 AQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLA 492
Cdd:PHA02989 247 IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 312-465 1.90e-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: 50.85  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   312 ACAGGFVDIVKVLLNEGA--NIEDHNENGHTPLMEAASAG-HVEVARVLLDHGAGINThsnefkESALTLACYKGHLDMV 388
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV------GDTLLHAISLEYVDAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   389 ----RFLLEAGADQ-------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ES 440
Cdd:TIGR00870  98 eailLHLLAAFRKSgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgES 177

                         170       180
                  ....*....|....*....|....*
gi 46519154   441 PLTLAACGGHVELAALLIERGANLE 465
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADIL 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 342-446 2.19e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  342 LMEAASAGHVEVARVLLDHGAgiNTHSNEFKESA-LTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEV 420
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGA--DPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 46519154  421 ARLLL-----DSGAQVNMPADSF--------ESPLTLAA 446
Cdd:PTZ00322 164 VQLLSrhsqcHFELGANAKPDSFtgkppsleDSPISSHH 202
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 222-460 2.38e-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: 50.85  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   222 RKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLL----AMHANVEDRGNKGDItpLMAASSGGYLDIVKLLLLHDAD 297
Cdd:TIGR00870   1 RGPLDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLeepkKLNINCPDRLGRSAL--FVAAIENENLELTELLLNLSCR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   298 VnsqsATGNTALtYACAGGFVDIVKVLLN-------EGANIEDHNEN-------GHTPLMEAASAGHVEVARVLLDHGAG 363
Cdd:TIGR00870  79 G----AVGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGAS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154   364 INT--HSNEFKESALT---------LACYK--GHLDMVRFLLEAGADQEhKTDEM-----HTALMEA------------C 413
Cdd:TIGR00870 154 VPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelscqM 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 46519154   414 MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 460
Cdd:TIGR00870 233 YNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 394-491 2.70e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  394 AGADQEHKTDE------MHTALMEAC---MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANL 464
Cdd:PTZ00322  62 ATPDHNLTTEEvidpvvAHMLTVELCqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141

                         90       100
                 ....*....|....*....|....*..
gi 46519154  465 EEVNDEGYTPLMEAAREGHEEMVALLL 491
Cdd:PTZ00322 142 TLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 288-371 2.79e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  288 VKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLL-----DHGA 362
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqcHFEL 177


                 ....*....
gi 46519154  363 GINTHSNEF 371
Cdd:PTZ00322 178 GANAKPDSF 186
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 388-457 5.60e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 5.60e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  388 VRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALL 457
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 209-364 6.80e-06

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: 49.24  E-value: 6.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 209 LAEACSDGDVNAVRKLLdEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAmhaNVEDRGN--------KGDiTPLMA 278
Cdd:cd22192  21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLME---AAPELVNepmtsdlyQGE-TALHI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 279 ASSGGYLDIVKLLLLHDADVNSQSATGntalTYacaggFVDIVKVLLNEGanieDHnenghtPLMEAASAGHVEVARVLL 358
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSPRATG----TF-----FRPGPKNLIYYG----EH------PLSFAACVGNEEIVRLLI 156


                ....*.
gi 46519154 359 DHGAGI 364
Cdd:cd22192 157 EHGADI 162
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 473-598 8.88e-06

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: 48.86  E-value: 8.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 473 TPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTLACCGGFSEVADFLIKAG---------ADIELGcSTPLMEAS 543
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnepmtSDLYQG-ETALHIAV 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46519154 544 QEGHLELVKYLLASGANVHATTAT--------------GDTALTYACENGHTDVADVLLQAGADLDKQE 598
Cdd:cd22192  98 VNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
Ank_5 pfam13857
Ankyrin repeats (many copies);
266-312 1.61e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 46519154   266 DRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYA 312
Cdd:pfam13857  10 NRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 470-502 1.77e-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: 1.77e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 46519154   470 EGYTPLMEAA-REGHEEMVALLLAQGANINAQTE 502
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 470-499 2.63e-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: 41.42  E-value: 2.63e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 46519154    470 EGYTPLMEAAREGHEEMVALLLAQGANINA 499
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 337-365 2.84e-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: 41.03  E-value: 2.84e-05
                           10        20
                   ....*....|....*....|....*....
gi 46519154    337 NGHTPLMEAASAGHVEVARVLLDHGAGIN 365
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
 318-578 2.99e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  318 VDIVKVLLNEGANIEDHNENGHTPLMEAASaghvevarvlldhgaginthsnEFKEsaltlacYKGHLDMVRFLLEAGAD 397
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILS----------------------NIKD-------YKHMLDIVKILIENGAD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  398 QEHKTDEMHTALMEACMDGHV---EVARLLLDSGAQVNM-PADSFESPLTLAACGGHV--ELAALLIERGANLEEVND-E 470
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLlDKDGFTMLQVYLQSNHHIdiEIIKLLLEKGVDINTHNNkE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  471 GYTPLMEAAREGHE----EMVALLLAQGANINAQTEETQETALT-----LACCGGF-SEVADFLIKAgADI----ELGCs 536
Cdd:PHA02798 182 KYDTLHCYFKYNIDridaDILKLFVDNGFIINKENKSHKKKFMEylnslLYDNKRFkKNILDFIFSY-IDInqvdELGF- 259

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 46519154  537 TPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACEN 578
Cdd:PHA02798 260 NPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 206-305 3.68e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 3.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  206 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVE--DRGNKgdiTPLMAASSGG 283
Cdd:PTZ00322  83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTllDKDGK---TPLELAEENG 159

                         90       100
                 ....*....|....*....|..
gi 46519154  284 YLDIVKLLLLHDADVNSQSATG 305
Cdd:PTZ00322 160 FREVVQLLSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
357-409 4.18e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 4.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46519154   357 LLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTAL 409
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 319-491 4.30e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 46.68  E-value: 4.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 319 DIVKVLLNegANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGIN----------THSNE---FKESALTLACYKGHL 385
Cdd:cd22194 124 GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEgfyFGETPLALAACTNQP 201

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 386 DMVRFLLEAGADQEHKTDEMHTALMEACmdghVEVARlllDSGAQVNMPADSFESPLTlaACGGHvelaalliergaNLE 465
Cdd:cd22194 202 EIVQLLMEKESTDITSQDSRGNTVLHAL----VTVAE---DSKTQNDFVKRMYDMILL--KSENK------------NLE 260

                       170       180
                ....*....|....*....|....*..
gi 46519154 466 EV-NDEGYTPLMEAAREGHEEMVALLL 491
Cdd:cd22194 261 TIrNNEGLTPLQLAAKMGKAEILKYIL 287
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 317-414 6.58e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  317 FVDIVKVLLNEGANIE---DHNENGHT-PLMEAASAGHVEVARVLLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLL 392
Cdd:PHA02884  45 YTDIIDAILKLGADPEapfPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124

                         90       100
                 ....*....|....*....|..
gi 46519154  393 EAGADQEHKTDEMHTALMEACM 414
Cdd:PHA02884 125 SYGADINIQTNDMVTPIELALM 146
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 221-342 6.90e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 6.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  221 VRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGdITPLMAASSggYLDIVKLLLLHDADVNS 300
Cdd:PHA02874 173 IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG-FTPLHNAII--HNRSAIELLINNASIND 249

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 46519154  301 QSATGNTALTYA----CAggfVDIVKVLLNEGANIEDHNENGHTPL 342
Cdd:PHA02874 250 QDIDGSTPLHHAinppCD---IDIIDILLYHKADISIKDNKGENPI 292
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 520-598 9.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 9.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  520 VADFLIKAGADI---ELGCSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDK 596
Cdd:PHA02876 160 IAEMLLEGGADVnakDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239


                 ..
gi 46519154  597 QE 598
Cdd:PHA02876 240 ND 241
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 470-499 1.10e-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: 39.55  E-value: 1.10e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 46519154   470 EGYTPLMEAAREGHEEMVALLLAQGANINA 499
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 285-399 1.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.65  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  285 LDIVKLLLLHDADVNSQSATGNTAL--TYACAGGFV--DIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVL 357
Cdd:PHA02859  66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV-RINVIKLL 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 46519154  358 LDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQE 399
Cdd:PHA02859 145 IDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDIN 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 568-596 1.61e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.61e-04
                           10        20
                   ....*....|....*....|....*....
gi 46519154    568 GDTALTYACENGHTDVADVLLQAGADLDK 596
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 206-299 1.62e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  206 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDITPLMAASSGGYL 285
Cdd:PHA02875 136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKI 215

                         90
                 ....*....|....
gi 46519154  286 DIVKLLLLHDADVN 299
Cdd:PHA02875 216 DIVRLFIKRGADCN 229
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 336-555 1.64e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.75  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 336 ENGHTPLMEAasaghvevarvLLDhgagINTHSNEFKESALTLACYKGHLDmvRFLleaGADQEHKTDEMHTALMEACMD 415
Cdd:cd22194  92 DTGKTCLMKA-----------LLN----INENTKEIVRILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIER 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 416 GHVEVARLLLDSGAQVNMPA-----------DSF---ESPLTLAACGGHVELAALLIERGANLEEVNDE-GYTPLmeaar 480
Cdd:cd22194 152 RQGDIVKLLIAKGADVNAHAkgvffnpkykhEGFyfgETPLALAACTNQPEIVQLLMEKESTDITSQDSrGNTVL----- 226

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 481 egHeemvALLLAqganinAQTEETQETALTlaccggfsEVADFLIKAGADIELGCS------TPLMEASQEGHLELVKYL 554
Cdd:cd22194 227 --H----ALVTV------AEDSKTQNDFVK--------RMYDMILLKSENKNLETIrnneglTPLQLAAKMGKAEILKYI 286


                .
gi 46519154 555 L 555
Cdd:cd22194 287 L 287
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 305-333 2.19e-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: 2.19e-04
                           10        20
                   ....*....|....*....|....*....
gi 46519154    305 GNTALTYACAGGFVDIVKVLLNEGANIED 333
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 337-366 2.32e-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: 38.78  E-value: 2.32e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 46519154   337 NGHTPLMEAASAGHVEVARVLLDHGAGINT 366
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 337-365 3.62e-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: 38.04  E-value: 3.62e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 46519154   337 NGHTPLMEAA-SAGHVEVARVLLDHGAGIN 365
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 478-588 3.67e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  478 AAREGHEEMVAlllaqGANINAQTEETQETA----LTLACC----GGFSEVADFLIKAGAD---IELGCSTPLMEASQEG 546
Cdd:PTZ00322  52 EALEATENKDA-----TPDHNLTTEEVIDPVvahmLTVELCqlaaSGDAVGARILLTGGADpncRDYDGRTPLHIACANG 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 46519154  547 HLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLL 588
Cdd:PTZ00322 127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 407-597 4.23e-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: 43.46  E-value: 4.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 407 TALMEACMDGHVE-VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIE---RGANLEEVND--EGYTPLMEAAR 480
Cdd:cd22192  19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 481 EGHEEMVALLLAQGANInaqteetqetaLTLACCGGFsevadFLIKAGADIELGcSTPLMEASQEGHLELVKYLLASGAN 560
Cdd:cd22192  99 NQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNLIYYG-EHPLSFAACVGNEEIVRLLIEHGAD 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 46519154 561 VHATTATGDTAL---------TYACEnghtdVADVLLQAGADLDKQ 597
Cdd:cd22192 162 IRAQDSLGNTVLhilvlqpnkTFACQ-----MYDLILSYDKEDDLQ 202
Ank_5 pfam13857
Ankyrin repeats (many copies);
290-342 5.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 5.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46519154   290 LLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL 342
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
457-512 5.72e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 5.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 46519154   457 LIERG-ANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETqETALTLA 512
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 383-463 6.34e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 6.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 383 GHLDMVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA--DSF----------- 438
Cdd:cd21882  40 GVNEAIMLLLEAAPDSgnpkelvnAPCTDEFyqgQTALHIAIENRNLNLVRLLVENGADVSARAtgRFFrkspgnlfyfg 119

                        90       100
                ....*....|....*....|....*
gi 46519154 439 ESPLTLAACGGHVELAALLIERGAN 463
Cdd:cd21882 120 ELPLSLAACTNQEEIVRLLLENGAQ 144
Ank_4 pfam13637
Ankyrin repeats (many copies);
240-292 6.56e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 6.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46519154   240 SLLCLACSAGYYELAQVLLAMHANVEDRgNKGDITPLMAASSGGYLDIVKLLL 292
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 537-563 1.04e-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: 36.80  E-value: 1.04e-03
                           10        20
                   ....*....|....*....|....*..
gi 46519154    537 TPLMEASQEGHLELVKYLLASGANVHA 563
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
530-575 1.05e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 46519154   530 DIELGCSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYA 575
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 444-550 1.30e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  444 LAACGGHVElAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAqTEETQETALTLACCGGFSEVADF 523
Cdd:PTZ00322  89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQL 166

                         90       100
                 ....*....|....*....|....*....
gi 46519154  524 LIK-AGADIELG-CSTPLMEASQEGHLEL 550
Cdd:PTZ00322 167 LSRhSQCHFELGaNAKPDSFTGKPPSLED 195
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 242-335 1.31e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  242 LCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIV 321
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                         90
                 ....*....|....
gi 46519154  322 KVLLneGANIEDHN 335
Cdd:PTZ00322 165 QLLS--RHSQCHFE 176
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 536-594 1.32e-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: 41.92  E-value: 1.32e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 536 STPLMEASQEGHLELVKYLLAS-GANVHATTATGDTALTYACENGHTDVADVLLQAGADL 594
Cdd:cd22192  18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL 77
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 406-433 1.33e-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: 36.41  E-value: 1.33e-03
                           10        20
                   ....*....|....*....|....*...
gi 46519154    406 HTALMEACMDGHVEVARLLLDSGAQVNM 433
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
324-379 1.47e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 46519154   324 LLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINThSNEFKESALTLA 379
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 551-605 1.64e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46519154  551 VKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGAD---LDKqeDMKTILE 605
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADptlLDK--DGKTPLE 153
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 369-498 1.75e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  369 NEFKESALtLACY---KGHLDMVRFLLEAGADQEHKTDEMHTALMEACM----DGHVEVARLLLDSGAQVNMPADSFESP 441
Cdd:PHA02859  48 NDLYETPI-FSCLekdKVNVEILKFLIENGADVNFKTRDNNLSALHHYLsfnkNVEPEILKILIDSGSSITEEDEDGKNL 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46519154  442 L--TLAACGGHVELAALLIERGANLEEVNDEG----YTPLMeaaREGHEEMVALLLAQGANIN 498
Cdd:PHA02859 127 LhmYMCNFNVRINVIKLLIDSGVSFLNKDFDNnnilYSYIL---FHSDKKIFDFLTSLGIDIN 186
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 537-565 1.80e-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: 1.80e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 46519154   537 TPLMEAS-QEGHLELVKYLLASGANVHATT 565
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02795 PHA02795
ankyrin-like protein; Provisional
 285-355 2.01e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.13  E-value: 2.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46519154  285 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVAR 355
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARR 271
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 274-301 2.10e-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: 2.10e-03
                          10        20
                  ....*....|....*....|....*....
gi 46519154   274 TPLM-AASSGGYLDIVKLLLLHDADVNSQ 301
Cdd:pfam00023   4 TPLHlAAGRRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 568-596 2.55e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 2.55e-03
                          10        20
                  ....*....|....*....|....*....
gi 46519154   568 GDTALTYACENGHTDVADVLLQAGADLDK 596
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 341-595 3.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  341 PLMEAASAGHVEVARVLLDHGAGINTHSNEFKeSALTLACYKGHLDMVRFLLEAgaDQEHKTDEMHTALMEACMDGHVEV 420
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDL-TPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEI 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  421 ARLLLdsgaqvnmpADSFESpltlaacgghvelaalliERGANLEEVNDEGYTPLMEAaregheEMVALLLAQGANINAQ 500
Cdd:PHA02878 117 FKIIL---------TNRYKN------------------IQTIDLVYIDKKSKDDIIEA------EITKLLLSYGADINMK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154  501 TEETQetaltlaccggfsevadflikagadielgcSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGH 580
Cdd:PHA02878 164 DRHKG------------------------------NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213

                        250
                 ....*....|....*
gi 46519154  581 TDVADVLLQAGADLD 595
Cdd:PHA02878 214 KPIVHILLENGASTD 228
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 374-397 4.74e-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: 4.74e-03
                           10        20
                   ....*....|....*....|....
gi 46519154    374 SALTLACYKGHLDMVRFLLEAGAD 397
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 274-299 4.88e-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: 4.88e-03
                           10        20
                   ....*....|....*....|....*.
gi 46519154    274 TPLMAASSGGYLDIVKLLLLHDADVN 299
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 274-358 5.13e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.78  E-value: 5.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519154 274 TPLMAASSGGYLDIVKLLLLH---DADVNSQSATGNTAL--TYACAGGFVDIVKV-------LLNEGANI-------EDH 334
Cdd:cd22193 125 LPLSLAACTNQPDIVQYLLENehqPADIEAQDSRGNTVLhaLVTVADNTKENTKFvtrmydmILIRGAKLcptveleEIR 204

                        90       100
                ....*....|....*....|....
gi 46519154 335 NENGHTPLMEAASAGHVEVARVLL 358
Cdd:cd22193 205 NNDGLTPLQLAAKMGKIEILKYIL 228
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 568-597 7.42e-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: 34.57  E-value: 7.42e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 46519154   568 GDTALTYACE-NGHTDVADVLLQAGADLDKQ 597
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 407-433 8.08e-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: 34.16  E-value: 8.08e-03
                          10        20
                  ....*....|....*....|....*..
gi 46519154   407 TALMEACMDGHVEVARLLLDSGAQVNM 433
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 305-331 9.74e-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: 34.16  E-value: 9.74e-03
                          10        20
                  ....*....|....*....|....*..
gi 46519154   305 GNTALTYACAGGFVDIVKVLLNEGANI 331
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
 
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