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Conserved domains on  [gi|601984497|ref|NP_001278147|]
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ankyrin repeat domain-containing protein 2 isoform c [Homo sapiens]

Protein Classification

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

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
186-405 2.60e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 2.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 186 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQ 265
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 266 FRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQ 345
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 346 VEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 405
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
186-405 2.60e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 2.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 186 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQ 265
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 266 FRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQ 345
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 346 VEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 405
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
271-363 3.64e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 3.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497  271 LHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHgADTNVRDKLLsTPLHVAVRTGQVEIVE 350
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 601984497  351 HFLSLGLEINARD 363
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 246-402 3.31e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.78  E-value: 3.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 246 KMKVIEKFLADGGSADTCDQFRRTALH---RASLEGHMEILEKLLDNGATVDFQDRLDCTAMH-WACRGGHLEVVKLLQS 321
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 322 HGADTNVRDKLLSTPLHV-----AVRTGQVEIVehfLSLGLEINARDREGDTALHDAVRLNR--YKIIKLLLLHGADMMT 394
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVylsgfNINPKVIRLL---LRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYA 182


                 ....*...
gi 601984497 395 KNLAGKTP 402
Cdd:PHA03095 183 VDDRFRSL 190
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 239-371 9.10e-09

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: 57.72  E-value: 9.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 239 LKAAVEGKMKVIEKFLadggSADTCDQFRR-----TALHRASLEGHMEILEKLLDNG-------ATVDFQdrLDCTAMHW 306
Cdd:cd22192   22 LLAAKENDVQAIKKLL----KCPSCDLFQRgalgeTALHVAALYDNLEAAVVLMEAApelvnepMTSDLY--QGETALHI 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601984497 307 ACRGGHLEVVKLLQSHGADTNV-----------RDKLL---STPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALH 371
Cdd:cd22192   96 AVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLIyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 300-328 2.35e-06

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: 43.73  E-value: 2.35e-06
                           10        20
                   ....*....|....*....|....*....
gi 601984497   300 DCTAMHWACRGGHLEVVKLLQSHGADTNV 328
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 277-391 1.27e-04

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: 44.30  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497  277 EGHMEILEKLLDNGATVDFQ--DRLDCTAMHW-ACRGGHLEVVKLLQSHGADTNVRDKLLstplHVAvRTGQVEIVEHFL 353
Cdd:TIGR00870  27 RGDLASVYRDLEEPKKLNINcpDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDTLL----HAI-SLEYVDAVEAIL 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 601984497  354 SLgLEINARDR---------------EGDTALHDAVRLNRYKIIKLLLLHGAD 391
Cdd:TIGR00870 102 LH-LLAAFRKSgplelandqytseftPGITALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
186-405 2.60e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 2.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 186 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQ 265
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 266 FRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQ 345
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 346 VEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 405
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
156-405 1.09e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 1.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 156 LLVLEDEKHHGAQSAALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDE 235
Cdd:COG0666    9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 236 ETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEV 315
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 316 VKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTK 395
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                        250
                 ....*....|
gi 601984497 396 NLAGKTPTDL 405
Cdd:COG0666  249 DKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
241-401 1.45e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 1.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 241 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQ 320
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 321 SHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGK 400
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                 .
gi 601984497 401 T 401
Cdd:COG0666  287 T 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
271-363 3.64e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 3.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497  271 LHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHgADTNVRDKLLsTPLHVAVRTGQVEIVE 350
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 601984497  351 HFLSLGLEINARD 363
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
304-396 2.92e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 2.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497  304 MHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGlEINARDrEGDTALHDAVRLNRYKIIK 383
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 601984497  384 LLLLHGADMMTKN 396
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
247-402 2.58e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 2.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 247 MKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADT 326
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601984497 327 NVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 402
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 246-402 3.31e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.78  E-value: 3.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 246 KMKVIEKFLADGGSADTCDQFRRTALH---RASLEGHMEILEKLLDNGATVDFQDRLDCTAMH-WACRGGHLEVVKLLQS 321
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 322 HGADTNVRDKLLSTPLHV-----AVRTGQVEIVehfLSLGLEINARDREGDTALHDAVRLNR--YKIIKLLLLHGADMMT 394
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVylsgfNINPKVIRLL---LRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYA 182


                 ....*...
gi 601984497 395 KNLAGKTP 402
Cdd:PHA03095 183 VDDRFRSL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 246-402 1.37e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.49  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 246 KMKVIEKFLADGGSADTCDQFRRTALHRASLEGH-----MEILEKLLDNGATVDFQDRLDCTAMHWA--CRGGHLEVVKL 318
Cdd:PHA03100  47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 319 LQSHGADTNVRDKLLSTPLHVAVRTGQVEI------------------VEHFLSLGLEINARDREGDTALHDAVRLNRYK 380
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPE 206

                        170       180
                 ....*....|....*....|..
gi 601984497 381 IIKLLLLHGADMMTKNLAGKTP 402
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTP 228
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 281-402 2.01e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 90.02  E-value: 2.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 281 EILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEIN 360
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 601984497 361 ARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 402
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
241-370 2.51e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.01  E-value: 2.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 241 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQ 320
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 601984497 321 SHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTAL 370
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
241-330 3.29e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 3.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497  241 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNgATVDFQDRlDCTAMHWACRGGHLEVVKLLQ 320
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 601984497  321 SHGADTNVRD 330
Cdd:pfam12796  82 EKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 245-391 9.76e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 9.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 245 GKMKVIEKFLADGGSADTCDQFRRTALHrASLEG---HMEILEKLLDNGATVDFQDRldctamhwacrgghlevVKLLQS 321
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLH-LYLESnkiDLKILKLLIDKGVDINAKNR-----------------VNYLLS 180

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 322 HGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGAD 391
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
 280-404 7.93e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.30  E-value: 7.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 280 MEILEKLLDNGATVDFQDRLDCTAMHWACRGGH---LEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVE-IVEHFLSL 355
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 601984497 356 GLEINARDREGDTALHdaVRLN----RYKIIKLLLLHGADMMTKNLAGKTPTD 404
Cdd:PHA03095 107 GADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 249-420 1.23e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 249 VIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNV 328
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 329 RDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIikLLLLHGADMMTKNLAGKTPtdlvql 408
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTP------ 257

                        170
                 ....*....|..
gi 601984497 409 wqadTRHALEHP 420
Cdd:PHA02874 258 ----LHHAINPP 265
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 241-391 2.48e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.34  E-value: 2.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 241 AAVEGKMKVIEKFLADGGSADtcDQFRR---TALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVK 317
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 601984497 318 LLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGD-TALHDAVRLNRYKIIKLLLLHGAD 391
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 248-406 4.05e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.23  E-value: 4.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 248 KVIEKFLADGGSADTCDQFR-RTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADT 326
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 327 NVRDKLLSTPLHVAV-RTGQVEIVEHFLSLGLEINARDR-EGDTALHDAVRLNRykIIKLLLLHGADMMTKNLAGKTPTD 404
Cdd:PHA02878 228 DARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLS 305


                 ..
gi 601984497 405 LV 406
Cdd:PHA02878 306 SA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 230-410 4.63e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 77.60  E-value: 4.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 230 TGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACR 309
Cdd:PLN03192 521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 310 GGHLEVVKLLQ--SHGADTNVRDKLLSTplhvAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLL 387
Cdd:PLN03192 601 AKHHKIFRILYhfASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676

                        170       180
                 ....*....|....*....|....
gi 601984497 388 HGADMMTKNLAGK-TPTDLVQLWQ 410
Cdd:PLN03192 677 NGADVDKANTDDDfSPTELRELLQ 700
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 281-402 3.75e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.85  E-value: 3.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 281 EILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLH-----VAVRTGQVEIVEHFLSL 355
Cdd:PHA03100  16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEY 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 601984497 356 GLEINARDREGDTALHDAV--RLNRYKIIKLLLLHGADMMTKNLAGKTP 402
Cdd:PHA03100  96 GANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENL 144
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 268-405 9.02e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 9.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 268 RTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVE 347
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 601984497 348 IVEHFLSLGLEIN-ARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 405
Cdd:PHA02875  83 AVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141
Ank_4 pfam13637
Ankyrin repeats (many copies);
267-319 9.31e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 9.31e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 601984497  267 RRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLL 319
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 257-404 1.47e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 257 GGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGH-LEVVKLLQSHGADTNVRDKLLST 335
Cdd:PHA02876 365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLST 444

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 336 PLHVAVRTG-QVEIVEHFLSLGLEINARDREGDTALhdAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTD 404
Cdd:PHA02876 445 PLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGAELRDSRVLHKSLND 512
PHA03095 PHA03095
ankyrin-like protein; Provisional
 252-386 1.62e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 252 KFLADGGSAD-TCDQFRRTALHRaslegHME-------ILEKLLDNGATVDFQDRLDCTAMHWA---CRGGHLEVVKLLQ 320
Cdd:PHA03095 171 RLLIDAGADVyAVDDRFRSLLHH-----HLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLLI 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601984497 321 sHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLL 386
Cdd:PHA03095 246 -AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 236-404 1.82e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 236 ETFLKAAVE-GKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLE 314
Cdd:PHA02874 125 KTFLHYAIKkGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 315 VVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIveHFLSLGLEINARDREGDTALHDAVRLNRYK-IIKLLLLHGADMM 393
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADIS 282

                        170
                 ....*....|.
gi 601984497 394 TKNLAGKTPTD 404
Cdd:PHA02874 283 IKDNKGENPID 293
PHA03095 PHA03095
ankyrin-like protein; Provisional
 248-402 3.41e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.05  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 248 KVIEKFLADGGSADTCDQFRRTALHR--ASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACR--GGHLEVVKLLQSHG 323
Cdd:PHA03095  98 DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrNANVELLRLLIDAG 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 324 ADTNVRDKLLSTPLH---VAVRTGQvEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKL--LLLHGADMMTKNLA 398
Cdd:PHA03095 178 ADVYAVDDRFRSLLHhhlQSFKPRA-RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRY 256


                 ....
gi 601984497 399 GKTP 402
Cdd:PHA03095 257 GQTP 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
337-402 3.05e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 3.05e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601984497  337 LHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHG-ADMMTKnlaGKTP 402
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAdVNLKDN---GRTA 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 266-421 3.53e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.22  E-value: 3.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 266 FRRTALHR---ASLEGHMEILEKLLDNGATVDF----QDRLDCTAMHWA----CR---GGHLEVVKLLQSHGADTNVRDK 331
Cdd:PTZ00322  34 FERMAAIQeeiARIDTHLEALEATENKDATPDHnlttEEVIDPVVAHMLtvelCQlaaSGDAVGARILLTGGADPNCRDY 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 332 LLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLH-------GADMMTKNLAGKTPTd 404
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGANAKPDSFTGKPPS- 192

                        170
                 ....*....|....*..
gi 601984497 405 lvqlwQADTRHALEHPE 421
Cdd:PTZ00322 193 -----LEDSPISSHHPD 204
Ank_4 pfam13637
Ankyrin repeats (many copies);
302-353 2.10e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 2.10e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 601984497  302 TAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFL 353
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 248-402 2.50e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 248 KVIEKFLADGGSADTCDQFRRTALHRASLEGH-MEILEKLLDNGATVDFQDRLDCTAMHWACR-GGHLEVVKLLQSHGAD 325
Cdd:PHA02876 288 RLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGAN 367

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601984497 326 TNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAV-RLNRYKIIKLLLLHGADMMTKNLAGKTP 402
Cdd:PHA02876 368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALcGTNPYMSVKTLIDRGANVNSKNKDLSTP 445
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 278-402 7.35e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 7.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 278 GHMEILEKLLDN-GATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVE------ 350
Cdd:PHA02874  12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKllidng 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601984497 351 -----------------HFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 402
Cdd:PHA02874  92 vdtsilpipciekdmikTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 239-371 9.10e-09

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: 57.72  E-value: 9.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 239 LKAAVEGKMKVIEKFLadggSADTCDQFRR-----TALHRASLEGHMEILEKLLDNG-------ATVDFQdrLDCTAMHW 306
Cdd:cd22192   22 LLAAKENDVQAIKKLL----KCPSCDLFQRgalgeTALHVAALYDNLEAAVVLMEAApelvnepMTSDLY--QGETALHI 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601984497 307 ACRGGHLEVVKLLQSHGADTNV-----------RDKLL---STPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALH 371
Cdd:cd22192   96 AVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLIyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
318-371 1.32e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 1.32e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 601984497  318 LLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALH 371
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
334-386 3.36e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 3.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 601984497  334 STPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLL 386
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 277-406 1.63e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 277 EGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHF---- 352
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIidnr 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 353 -------LSL------------------GLEINARDREGDTALHDAVRL-NRYKIIKLLLLHGADMMTKNLAGKTPTDLV 406
Cdd:PHA02876 235 sninkndLSLlkairnedletslllydaGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
Ank_5 pfam13857
Ankyrin repeats (many copies);
286-340 1.74e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 1.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 601984497  286 LLDNG-ATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVA 340
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 300-328 2.35e-06

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: 43.73  E-value: 2.35e-06
                           10        20
                   ....*....|....*....|....*....
gi 601984497   300 DCTAMHWACRGGHLEVVKLLQSHGADTNV 328
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 271-396 4.01e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 49.06  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 271 LHRASLEghMEILEKLLDNGATVDFQDRLD----CTAMHWACRGGH-LEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQ 345
Cdd:PHA02798  44 LQRDSPS--TDIVKLFINLGANVNGLDNEYstplCTILSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNGY 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 601984497 346 V---EIVEHFLSLGLEINARDREGDTALHDAVRLNRY---KIIKLLLLHGADMMTKN 396
Cdd:PHA02798 122 InnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHN 178
PHA02741 PHA02741
hypothetical protein; Provisional
 305-407 5.05e-06

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 46.57  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 305 HWACRGGHLEVVKLL------QSHGADTNVRDKLLSTPLHVAVRTGQ----VEIVEHFLSLGLEINARDR-EGDTALHDA 373
Cdd:PHA02741  26 HEAARCGCFDIIARFtpfirgDCHAAALNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMlEGDTALHLA 105

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 601984497 374 VRLNRYKIIKLLLLH-GADMMTKNLAGKTPTDLVQ 407
Cdd:PHA02741 106 AHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAI 140
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 301-331 7.39e-06

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: 42.66  E-value: 7.39e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 601984497  301 CTAMHWAC-RGGHLEVVKLLQSHGADTNVRDK 331
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 254-322 1.45e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 1.45e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601984497 254 LADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSH 322
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 248-343 1.48e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 248 KVIEKFLADGGSADTCDQFRRTALHRASleGHM---EILEKLLDNGATVDFQDR-LDCTAMHWACRGGhlEVVKLLQSHG 323
Cdd:PHA02878 215 PIVHILLENGASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYG 290

                         90       100
                 ....*....|....*....|
gi 601984497 324 ADTNVRDKLLSTPLHVAVRT 343
Cdd:PHA02878 291 ADINSLNSYKLTPLSSAVKQ 310
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 261-407 1.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 261 DTCDQFRRTALHrASLEG---HMEILEKLLDNGATVDFQDRLD-CTAMHWAC---RGGHLEVVKLLQSHGADTNVRDKLL 333
Cdd:PHA02859  45 NDCNDLYETPIF-SCLEKdkvNVEILKFLIENGADVNFKTRDNnLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDG 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601984497 334 STPLHVAVR--TGQVEIVEHFLSLGLEINARDREGDTALHDAVRL-NRYKIIKLLLLHGADMMTKNLAGKTPTDLVQ 407
Cdd:PHA02859 124 KNLLHMYMCnfNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIK 200
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 304-402 2.54e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.10  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 304 MHWACRGGhlEVVKLLQSHGADTNVRDKLLS-------TPLHVAVRTGQVEIVEHFLSL---GLEINARDR-EGDTALHD 372
Cdd:PHA02736  21 LHYLCRNG--GVTDLLAFKNAISDENRYLVLeynrhgkQCVHIVSNPDKADPQEKLKLLmewGADINGKERvFGNTPLHI 98

                         90       100       110
                 ....*....|....*....|....*....|.
gi 601984497 373 AVRLNRYKIIKLLLLH-GADMMTKNLAGKTP 402
Cdd:PHA02736  99 AVYTQNYELATWLCNQpGVNMEILNYAFKTP 129
Ank_5 pfam13857
Ankyrin repeats (many copies);
348-406 6.16e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 6.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 601984497  348 IVEHFLslgLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDLV 406
Cdd:pfam13857   1 LLEHGP---IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 234-328 7.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 7.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 234 DEETFLKAAV-EGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVD-FQDRLDCTAMHWACRGG 311
Cdd:PHA02875 134 DKFSPLHLAVmMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENN 213

                         90
                 ....*....|....*..
gi 601984497 312 HLEVVKLLQSHGADTNV 328
Cdd:PHA02875 214 KIDIVRLFIKRGADCNI 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 353-424 7.54e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 7.54e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601984497 353 LSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDLV------QLWQADTRHALEHPEPGA 424
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAeengfrEVVQLLSRHSQCHFELGA 179
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 335-361 1.09e-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: 1.09e-04
                           10        20
                   ....*....|....*....|....*..
gi 601984497   335 TPLHVAVRTGQVEIVEHFLSLGLEINA 361
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
236-287 1.24e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 601984497  236 ETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLL 287
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 277-391 1.27e-04

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: 44.30  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497  277 EGHMEILEKLLDNGATVDFQ--DRLDCTAMHW-ACRGGHLEVVKLLQSHGADTNVRDKLLstplHVAvRTGQVEIVEHFL 353
Cdd:TIGR00870  27 RGDLASVYRDLEEPKKLNINcpDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDTLL----HAI-SLEYVDAVEAIL 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 601984497  354 SLgLEINARDR---------------EGDTALHDAVRLNRYKIIKLLLLHGAD 391
Cdd:TIGR00870 102 LH-LLAAFRKSgplelandqytseftPGITALHLAAHRQNYEIVKLLLERGAS 153
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 302-328 2.34e-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: 38.39  E-value: 2.34e-04
                          10        20
                  ....*....|....*....|....*..
gi 601984497  302 TAMHWACRGGHLEVVKLLQSHGADTNV 328
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 365-392 3.17e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 3.17e-04
                           10        20
                   ....*....|....*....|....*...
gi 601984497   365 EGDTALHDAVRLNRYKIIKLLLLHGADM 392
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 316-390 3.36e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 41.34  E-value: 3.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601984497 316 VKLLQSHGADTNVRDKLL-STPLHVAVRTGQVEIVEHFL-SLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGA 390
Cdd:PHA02743  76 IELLVNMGADINARELGTgNTLLHIAASTKNYELAEWLCrQLGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 268-294 3.86e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 3.86e-04
                           10        20
                   ....*....|....*....|....*..
gi 601984497   268 RTALHRASLEGHMEILEKLLDNGATVD 294
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 271-402 4.35e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 271 LHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQS------------------HGADTNVRDKL 332
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafNNRNVEIFKII 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 333 LSTPLH-------VAVRTG------QVEIVEHFLSLGLEINARDRE-GDTALHDAVRLNRYKIIKLLLLHGADMMTKNLA 398
Cdd:PHA02878 121 LTNRYKniqtidlVYIDKKskddiiEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200


                 ....
gi 601984497 399 GKTP 402
Cdd:PHA02878 201 NNSP 204
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 234-374 7.88e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.05  E-value: 7.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 234 DEETFLKAAVEGKMKVIEKFLADggSADTCDQFR------------------RTALHRASL---EGHMEILEKLLDNGAT 292
Cdd:cd22194   45 DKKKRLKKVSEAAVEELGELLKE--LKDLSRRRRktdvpdflmhkltasdtgKTCLMKALLninENTKEIVRILLAFAEE 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 293 VDFQDRL-----------DCTAMHWACRGGHLEVVKLLQSHGADTNVRDK--------------LLSTPLHVAVRTGQVE 347
Cdd:cd22194  123 NGILDRFinaeyteeayeGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPE 202

                        170       180
                 ....*....|....*....|....*...
gi 601984497 348 IVEHFLSLG-LEINARDREGDTALHDAV 374
Cdd:cd22194  203 IVQLLMEKEsTDITSQDSRGNTVLHALV 230
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 365-396 8.74e-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: 36.50  E-value: 8.74e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 601984497  365 EGDTALHDAV-RLNRYKIIKLLLLHGADMMTKN 396
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 335-364 1.32e-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: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 601984497  335 TPLHVAV-RTGQVEIVEHFLSLGLEINARDR 364
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
 349-402 1.73e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 1.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 601984497 349 VEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 402
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTP 108
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 365-391 2.22e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 2.22e-03
                          10        20
                  ....*....|....*....|....*..
gi 601984497  365 EGDTALHDAVRLNRYKIIKLLLLHGAD 391
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 280-402 2.28e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.28  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 280 MEILEKLLDNGATVDFQDRLDCTAMH-WACRGG-HLEVVKLLQSHGADTNVRDKLLSTPLHVavrtgqveivehFLSLGL 357
Cdd:PHA02716 297 ISVVYSFLQPGVKLHYKDSAGRTCLHqYILRHNiSTDIIKLLHEYGNDLNEPDNIGNTVLHT------------YLSMLS 364

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 601984497 358 EINARDREGDTALhdavrlnRYKIIKLLLLHGADMMTKNLAGKTP 402
Cdd:PHA02716 365 VVNILDPETDNDI-------RLDVIQCLISLGADITAVNCLGYTP 402
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 268-298 2.53e-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: 35.34  E-value: 2.53e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 601984497  268 RTALHRASLE-GHMEILEKLLDNGATVDFQDR 298
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 317-394 2.83e-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: 40.00  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984497 317 KLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLS-----LGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGAD 391
Cdd:cd22192   35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGAD 114


                 ...
gi 601984497 392 MMT 394
Cdd:cd22192  115 VVS 117
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 335-361 3.26e-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: 34.93  E-value: 3.26e-03
                          10        20
                  ....*....|....*....|....*..
gi 601984497  335 TPLHVAVRTGQVEIVEHFLSLGLEINA 361
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 268-294 3.90e-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: 34.93  E-value: 3.90e-03
                          10        20
                  ....*....|....*....|....*..
gi 601984497  268 RTALHRASLEGHMEILEKLLDNGATVD 294
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
 346-402 5.96e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.05  E-value: 5.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 601984497 346 VEIVEHFLSLGLEINARDREGDTALHDAV-RLNRYK----IIKLLLLHGADMMTKNLAGKTP 402
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILsNIKDYKhmldIVKILIENGADINKKNSDGETP 112
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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