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Conserved domains on  [gi|172045720|sp|Q69ZU8|]
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RecName: Full=Ankyrin repeat domain-containing protein 6; AltName: Full=Diversin

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-244 9.74e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.91  E-value: 9.74e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLL 162
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 163 GGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQT 242
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                 ..
gi 172045720 243 PL 244
Cdd:COG0666  288 LL 289
geminin-like_CC super family cl45898
coiled-coil domain found in the geminin family; The geminin family includes geminin, geminin ...
 422-467 9.50e-03

coiled-coil domain found in the geminin family; The geminin family includes geminin, geminin coiled-coil domain-containing protein 1 (GemC1), and McIdas. Together, geminin, GemC1, and McIdas (also called Idas or multicilin), controls both the cell cycle and differentiation decisions in cells. They were initially identified as cell cycle regulators associated with the chromosome cycle. Geminin is required to ensure once-per-cell-cycle genome replication, while McIdas and GemC1 bind to geminin and are implicated in DNA replication control. Geminin binds to Cdt1, a key component and crucial regulator of pre-replicative complexes (pre-RC), in a timely manner to inhibit DNA replication. Geminin family members also function as early regulators of multiciliogenesis. GemC1 and McIdas specify the multiciliate cell fate by forming complexes with the E2F4/5 transcription factors, resulting in centriole amplification and cilia formation. Geminin family proteins contain a homologous central coiled-coil domain that mediates homo- and heterodimerization; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of the geminin family.


The actual alignment was detected with superfamily member cd22590:

Pssm-ID: 459243  Cd Length: 64  Bit Score: 35.16  E-value: 9.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 172045720 422 NQLEATVEEIRAELGSVQDKvNAKLGQMESKTQHQMCVLDKLMVER 467
Cdd:cd22590   20 NQLHETLTRKQEEIDSLQER-NVQLKELASQAKHLASVLDKLMTVR 64
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-244 9.74e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.91  E-value: 9.74e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLL 162
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 163 GGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQT 242
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                 ..
gi 172045720 243 PL 244
Cdd:COG0666  288 LL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-265 5.30e-30

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 123.98  E-value: 5.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  29 LINKGAKV-AVTKHGRTPLHL-AANKGHLSVVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEILTALIREGCALDRQ 104
Cdd:PHA03095  69 LLEAGADVnAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNAL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 105 DKDGNTALHeaawhGFSQSA-------KLLVKAGANVLARNKAGNTALHLACQNSHSQST--RILLLGGSRADLKNNAGD 175
Cdd:PHA03095 149 DLYGMTPLA-----VLLKSRnanvellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGN 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 176 TCLHVAARYNHL--SVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNP 253
Cdd:PHA03095 224 TPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303

                        250
                 ....*....|...
gi 172045720 254 E-VALLLTKAPQI 265
Cdd:PHA03095 304 RaVRAALAKNPSA 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 2.29e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 2.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   46 LHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIrEGCALDRQDkDGNTALHEAAWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 172045720  126 LLVKAGANVLARN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 109-244 3.14e-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: 60.03  E-value: 3.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 109 NTALHEAAWHGFSQSAK-LLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLLGGSRadLKNNA-------GDTCLHV 180
Cdd:cd22192   18 ESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHI 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 172045720 181 AARYNHLSVVRLLLN------------AFCSVHEKNQA--GDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPL 244
Cdd:cd22192   96 AVVNQNLNLVRELIArgadvvspratgTFFRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 1.37e-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: 44.89  E-value: 1.37e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 172045720    41 HGRTPLHLAANKGHLSVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-194 7.17e-05

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: 46.23  E-value: 7.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTALIREGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  107 DGNTALHeaawhgfsqsakLLVkaganVLARNKAGNTALHLACQNS------HSQSTRILllggsrADLKNNAGDTCLHV 180
Cdd:TIGR00870 207 LGNTLLH------------LLV-----MENEFKAEYEELSCQMYNFalslldKLRDSKEL------EVILNHQGLTPLKL 263

                         170
                  ....*....|....
gi 172045720  181 AARYNHLSVVRLLL 194
Cdd:TIGR00870 264 AAKEGRIVLFRLKL 277
McIdas_CC cd22590
central coiled-coil domain of McIdas (or multicilin); McIdas (also called Idas or multicilin), ...
 422-467 9.50e-03

central coiled-coil domain of McIdas (or multicilin); McIdas (also called Idas or multicilin), together with geminin coiled-coil domain-containing protein 1 (GemC1) and geminin, controls both the cell cycle and differentiation decisions in cells. Idas binds to geminin and is implicated in DNA replication control. It also functions as an early regulator of multiciliogenesis. GemC1 and McIdas specify the multiciliate cell fate by forming complexes with the E2F4/5 transcription factors, resulting in centriole amplification and cilia formation. Idas belongs to the geminin family of proteins that also includes geminin and GemC1. They share a homologous central coiled-coil domain that mediates homo- and heterodimerization with other family members; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of McIdas.


Pssm-ID: 439144  Cd Length: 64  Bit Score: 35.16  E-value: 9.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 172045720 422 NQLEATVEEIRAELGSVQDKvNAKLGQMESKTQHQMCVLDKLMVER 467
Cdd:cd22590   20 NQLHETLTRKQEEIDSLQER-NVQLKELASQAKHLASVLDKLMTVR 64
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-244 9.74e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.91  E-value: 9.74e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLL 162
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 163 GGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQT 242
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                 ..
gi 172045720 243 PL 244
Cdd:COG0666  288 LL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-262 2.37e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 174.76  E-value: 2.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   1 MSQQDAVAALSERLLIAAYKGQTENVVQLINKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALH 80
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  81 RATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRIL 160
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 161 LLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAG 240
Cdd:COG0666  173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                        250       260
                 ....*....|....*....|..
gi 172045720 241 QTPLETARYHNNPEVALLLTKA 262
Cdd:COG0666  253 LTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-262 6.96e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.60  E-value: 6.96e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  24 ENVVQLINKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDR 103
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 104 QDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLLGGSRADLKNNAGDTCLHVAAR 183
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 172045720 184 YNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 262
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-262 1.40e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 1.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  55 LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANV 134
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 135 LARNKAGNTALHLACQNSHSQSTRILLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVA 214
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 172045720 215 AALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 262
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-265 5.30e-30

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 123.98  E-value: 5.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  29 LINKGAKV-AVTKHGRTPLHL-AANKGHLSVVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEILTALIREGCALDRQ 104
Cdd:PHA03095  69 LLEAGADVnAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNAL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 105 DKDGNTALHeaawhGFSQSA-------KLLVKAGANVLARNKAGNTALHLACQNSHSQST--RILLLGGSRADLKNNAGD 175
Cdd:PHA03095 149 DLYGMTPLA-----VLLKSRnanvellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGN 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 176 TCLHVAARYNHL--SVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNP 253
Cdd:PHA03095 224 TPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303

                        250
                 ....*....|...
gi 172045720 254 E-VALLLTKAPQI 265
Cdd:PHA03095 304 RaVRAALAKNPSA 316
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-262 1.19e-28

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 120.13  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  24 ENVVQLINKGAKVAVTK-HGRTPLHLAANKGH---LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTE-ILTALIREG 98
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGeYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  99 CALDRQDKDGNTALHeAAWHGFSQSAK---LLVKAGANVLARNKAGNTALH--LACQNSHSQSTRILLLGGSRADLKNNA 173
Cdd:PHA03095 108 ADVNAKDKVGRTPLH-VYLSGFNINPKvirLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDR 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 174 GDTCLHVAARYNHLS--VVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKV--LLEAGADTTIVNNAGQTPLETARY 249
Cdd:PHA03095 187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAV 266

                        250
                 ....*....|...
gi 172045720 250 HNNPEVALLLTKA 262
Cdd:PHA03095 267 FNNPRACRRLIAL 279
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 40-265 1.39e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.81  E-value: 1.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  40 KHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNteILTALIRegcaldrqdkdgntalheaawhg 119
Cdd:PHA03100  33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY--NLTDVKE----------------------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 120 fsqSAKLLVKAGANVLARNKAGNTALHLACQNsHSQSTRI---LLLGGSRADLKNNAGDTCLHVAARYNH--LSVVRLLL 194
Cdd:PHA03100  88 ---IVKLLLEYGANVNAPDNNGITPLLYAISK-KSNSYSIveyLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 195 ------NAFCSV----------HEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPE-VAL 257
Cdd:PHA03100 164 dkgvdiNAKNRVnyllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEiFKL 243


                 ....*...
gi 172045720 258 LLTKAPQI 265
Cdd:PHA03100 244 LLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 2.29e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 2.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   46 LHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIrEGCALDRQDkDGNTALHEAAWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 172045720  126 LLVKAGANVLARN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-237 2.84e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 2.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  145 LHLACQNSHSQSTRILLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSvhEKNQAGDTALHVAAALNHKKVVK 224
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 172045720  225 VLLEAGADTTIVN 237
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-247 5.86e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.10  E-value: 5.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLA 136
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 137 RNKAGNTALHLACQNSHSQSTRILLLGGSRADLKNNAGDTCLHVAARYNHlSVVRLLLNAfCSVHEKNQAGDTALHvaAA 216
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLH--HA 261

                        170       180       190
                 ....*....|....*....|....*....|....
gi 172045720 217 LNH---KKVVKVLLEAGADTTIVNNAGQTPLETA 247
Cdd:PHA02874 262 INPpcdIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-204 9.64e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 9.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  112 LHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLlggSRADLKN-NAGDTCLHVAARYNHLSVV 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLkDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 172045720  191 RLLLNAFCSVHEKN 204
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 5.24e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 5.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   14 LLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKaGCDLDVQDDGdQTALHRATVVGNTEILT 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAnLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 172045720   93 ALIREGCALDRQD 105
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 88-247 4.12e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.93  E-value: 4.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  88 TEILTALIREGCALDRQDKD-GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLLGGSR 166
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 167 ADLKNNAGDTCLHVAARY-NHLSVVRLLLNAFCSVHEKNQA-GDTALHVAaaLNHKKVVKVLLEAGADTTIVNNAGQTPL 244
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPL 304


                 ...
gi 172045720 245 ETA 247
Cdd:PHA02878 305 SSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-259 1.52e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  178 LHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEaGADTTIVNNaGQTPLETARYHNNPEVAL 257
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 172045720  258 LL 259
Cdd:pfam12796  79 LL 80
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-262 1.85e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.32  E-value: 1.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  10 LSERLLIAAYKGQTENVVQLI-NKGAKVAVT-KHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGN 87
Cdd:PHA02874   1 ASQDLRMCIYSGDIEAIEKIIkNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  88 TEILTALIREGC---ALDRQDKDGNTAlheaawhgfsqsaKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLLGG 164
Cdd:PHA02874  81 HDIIKLLIDNGVdtsILPIPCIEKDMI-------------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 165 SRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPL 244
Cdd:PHA02874 148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227

                        250
                 ....*....|....*...
gi 172045720 245 ETARYHNNPEVALLLTKA 262
Cdd:PHA02874 228 HNAIIHNRSAIELLINNA 245
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 62-237 2.16e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 83.38  E-value: 2.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  62 LKAGcDLDVQDDGDQTALHRA----TVV--GNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVL 135
Cdd:PLN03192 507 LNVG-DLLGDNGGEHDDPNMAsnllTVAstGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 136 ARNKAGNTALHLACQNSHSQSTRILLLGGSRADlKNNAGDTcLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAA 215
Cdd:PLN03192 586 IRDANGNTALWNAISAKHHKIFRILYHFASISD-PHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663

                        170       180
                 ....*....|....*....|..
gi 172045720 216 ALNHKKVVKVLLEAGADTTIVN 237
Cdd:PLN03192 664 AEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-251 2.22e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 2.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  14 LLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLS-VVQILLKAGCDLDVQDDGDQTALHRATVVG-NTEI 90
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVnSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  91 LTALIREGCALDRQDKDGNTALHEAA-WHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLLGGSRADL 169
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 170 KNNAGDTCLHVA-ARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHK-KVVKVLLEAGADTTIVNNAGQTPLETA 247
Cdd:PHA02876 404 LSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA 483


                 ....*
gi 172045720 248 -RYHN 251
Cdd:PHA02876 484 lEYHG 488
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-253 2.40e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 2.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  29 LINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRAT------------------------ 83
Cdd:PHA02876 164 LLEGGADVnAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiidnrsninkndls 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  84 ---VVGNTEILTALI--REGCALDRQDKDGNTALHEAAWH-GFSQSAKLLVKAGANVLARNKAGNTALHLACQNSH-SQS 156
Cdd:PHA02876 244 llkAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 157 TRILLLGGSRADLKNNAGDTCLHVAA---RYNHLSVVRLLLNAfcSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADT 233
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQAStldRNKDIVITLLELGA--NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                        250       260
                 ....*....|....*....|
gi 172045720 234 TIVNNAGQTPLETARYHNNP 253
Cdd:PHA02876 402 EALSQKIGTALHFALCGTNP 421
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-171 1.13e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.52  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQdkDGNTALHEAAWHGFS 121
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDL 635

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 172045720 122 QSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLLGGSRADLKN 171
Cdd:PLN03192 636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-254 1.39e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.49  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGC-ALDRQDKDGNTALHEAAWHGF 120
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKK 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 121 SQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSV 200
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 172045720 201 HEKNQAGDTALHVAAALNHK-KVVKVLLEAGADTTI---VNNAGQTPLETAR-YHNNPE 254
Cdd:PHA02875 195 DYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNImfmIEGEECTILDMICnMCTNLE 253
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-198 1.17e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  22 QTENVVQLINKGAKV-AVTKH-GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGC 99
Cdd:PHA02878 146 EAEITKLLLSYGADInMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 100 ALDRQDKDGNTALHEAAWHGFSQSA-KLLVKAGANVLARNKA-GNTALHLACQNshSQSTRILLLGGSRADLKNNAGDTC 177
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYIlGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303

                        170       180
                 ....*....|....*....|..
gi 172045720 178 LHVAAR-YNHLSVVRLLLNAFC 198
Cdd:PHA02878 304 LSSAVKqYLCINIGRILISNIC 325
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-195 1.37e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.86  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  15 LIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAAN-KGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILT 92
Cdd:PHA02876 313 LMAKNGYDTENIRTLIMLGADVnAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  93 ALIREGCALDRQDKDGNTALHeAAWHGFS--QSAKLLVKAGANVLARNKAGNTALHLACQ-NSHSQSTRILLLGGSRADL 169
Cdd:PHA02876 393 TLLDYGADIEALSQKIGTALH-FALCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVNA 471

                        170       180
                 ....*....|....*....|....*.
gi 172045720 170 KNNAGDTCLHVAARYNhlSVVRLLLN 195
Cdd:PHA02876 472 INIQNQYPLLIALEYH--GIVNILLH 495
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-95 1.46e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 1.46e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 172045720   42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALI 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-169 1.69e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  17 AAYKGQTENVVQLI--NKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTAL 94
Cdd:PHA02875  75 AVEEGDVKAVEELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 172045720  95 IREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGN-TALHLACQNSHSQSTRILLLGGSRADL 169
Cdd:PHA02875 155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-227 7.85e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 7.85e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 172045720  174 GDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLL 227
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-252 9.64e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 9.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  55 LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREG---------------CALDRQDKD------------ 107
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGadvniialddlsvleCAVDSKNIDtikaiidnrsni 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 108 --GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQN-SHSQSTRILLLGGSRADLKNNAGDTCLHVAARY 184
Cdd:PHA02876 238 nkNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKN 317

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 185 NH-LSVVRLLLNAFCSVHEKNQAGDTALHVAAALN-HKKVVKVLLEAGADTTIVNNAGQTPLETARYHNN 252
Cdd:PHA02876 318 GYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 109-244 3.14e-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: 60.03  E-value: 3.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 109 NTALHEAAWHGFSQSAK-LLVKAGANVLARNKAGNTALHLACQNSHSQSTRILLLGGSRadLKNNA-------GDTCLHV 180
Cdd:cd22192   18 ESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHI 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 172045720 181 AARYNHLSVVRLLLN------------AFCSVHEKNQA--GDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPL 244
Cdd:cd22192   96 AVVNQNLNLVRELIArgadvvspratgTFFRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-82 6.57e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 6.57e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 172045720   40 KHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-261 8.43e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 8.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  53 GHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGA 132
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 133 ---NVLArnKAGNTALHLACQNSHSQSTRILLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDT 209
Cdd:PHA02875  93 fadDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 172045720 210 ALHVAAALNHKKVVKVLLEAGADTTIVNNAGQ-TPLETARYHNNPEVALLLTK 261
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 13-247 8.63e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 8.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  13 RLLIAAYKGQTENVVQLINKGAKvavTKHGRT--------PLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATV 84
Cdd:PHA02878   3 KLYKSMYTDNYETILKYIEYIDH---TENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  85 VGNTEILTALIREgcalDRQDKDGNT--ALHEAAWHGFSQSAKLLVkaganvLARNKAGNTA-LHLACQNSHSQS----- 156
Cdd:PHA02878  80 EPNKLGMKEMIRS----INKCSVFYTlvAIKDAFNNRNVEIFKIIL------TNRYKNIQTIdLVYIDKKSKDDIieaei 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 157 TRILLLGGSRADLKN-NAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTI 235
Cdd:PHA02878 150 TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                        250
                 ....*....|..
gi 172045720 236 VNNAGQTPLETA 247
Cdd:PHA02878 230 RDKCGNTPLHIS 241
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 11-187 1.28e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.10  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  11 SERLLIAAYKgqtENVVQLINKGAKVAVTK------HGRTPLHLAANKGHLSVVQILLKAGCDL-DVQDDGD----QTAL 79
Cdd:cd22192   17 SESPLLLAAK---ENDVQAIKKLLKCPSCDlfqrgaLGETALHVAALYDNLEAAVVLMEAAPELvNEPMTSDlyqgETAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  80 HRATVVGNTEILTALIREG-----------CALDRQDKD---GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTAL 145
Cdd:cd22192   94 HIAVVNQNLNLVRELIARGadvvspratgtFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 172045720 146 H-LACQNSHSQSTRI--LLLGGSRAD-------LKNNAGDTCLHVAAR------YNHL 187
Cdd:cd22192  174 HiLVLQPNKTFACQMydLILSYDKEDdlqpldlVPNNQGLTPFKLAAKegnivmFQHL 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 190-264 3.13e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 3.13e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 172045720 190 VRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQ 264
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-259 4.70e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 4.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 172045720  207 GDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLL 259
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-255 5.78e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.17  E-value: 5.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  44 TPLHLAANKGHLSVVQILLK-AGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDK-----DGNTALHEAAW 117
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 118 HGFSQSAKLLVKAGANVlARNKAGNTALHLacqnshsqstrilllggsRADLKNNAGDTCLHVAARYNHLSVVRLLLNAF 197
Cdd:cd22192   99 NQNLNLVRELIARGADV-VSPRATGTFFRP------------------GPKNLIYYGEHPLSFAACVGNEEIVRLLIEHG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 172045720 198 CSVHEKNQAGDTALHVAAALNHKKVVKVL------LEAGADT----TIVNNAGQTPLETARYHNNPEV 255
Cdd:cd22192  160 ADIRAQDSLGNTVLHILVLQPNKTFACQMydlilsYDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVM 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-73 5.84e-08

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: 49.21  E-value: 5.84e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 172045720   41 HGRTPLHLAANK-GHLSVVQILLKAGCDLDVQDD 73
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-161 1.65e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 172045720  108 GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRILL 161
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-194 2.26e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 2.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 172045720  141 GNTALHLACQNSHSQSTRILLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLL 194
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
159-214 2.94e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 2.94e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 172045720  159 ILLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVA 214
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 75-270 3.76e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  75 DQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHS 154
Cdd:PHA02875   2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 155 QSTRILLLGGSRA-DLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADT 233
Cdd:PHA02875  82 KAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 172045720 234 TIVNNAGQTPLETARYHNNPEVA-LLLTKAPQILRFSR 270
Cdd:PHA02875 162 DIEDCCGCTPLIIAMAKGDIAICkMLLDSGANIDYFGK 199
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 79-259 4.00e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 4.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  79 LHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKaganVLARNKAGNT--ALHLACQNSHSQS 156
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVEI 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 157 TRILLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQ-AGDTALHVAAALNHKKVVKVLLEAGADTTI 235
Cdd:PHA02878 117 FKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNI 196

                        170       180
                 ....*....|....*....|....*
gi 172045720 236 VNNAGQTPLETA-RYHNNPEVALLL 259
Cdd:PHA02878 197 PDKTNNSPLHHAvKHYNKPIVHILL 221
PHA02791 PHA02791
ankyrin-like protein; Provisional
 41-204 7.96e-07

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 51.20  E-value: 7.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDgdQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGF 120
Cdd:PHA02791  29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 121 SQSAKLLVKAGANVLARNKAG--NTALHLACQNSHSQSTRILLLGGSRADLKNNAgdTCLHVAARYNHLSVVRLLLNAFC 198
Cdd:PHA02791 107 MQTVKLFVKKNWRLMFYGKTGwkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAILL--SCIHITIKNGHVDMMILLLDYMT 184


                 ....*.
gi 172045720 199 SVHEKN 204
Cdd:PHA02791 185 STNTNN 190
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 175-261 1.08e-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: 51.94  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 175 DTCLHVAARYNHL-SVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEagADTTIVNNA-------GQTPLET 246
Cdd:cd22192   18 ESPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALHI 95

                         90
                 ....*....|....*.
gi 172045720 247 ARYHNNPE-VALLLTK 261
Cdd:cd22192   96 AVVNQNLNlVRELIAR 111
Ank_2 pfam12796
Ankyrin repeats (3 copies);
211-273 1.12e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 1.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 172045720  211 LHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQILRFSRGRS 273
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 57-244 1.25e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.84  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGN--TEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLlVKAGANV 134
Cdd:PHA02716 194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNINPEI-TNIYIES 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 135 LARNKAGNTALHLACQNSHSQSTRI-----LLLGGSRADLKNNAGDTCLH--VAARYNHLSVVRLLLNAFCSVHEKNQAG 207
Cdd:PHA02716 273 LDGNKVKNIPMILHSYITLARNIDIsvvysFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIG 352

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 172045720 208 DTALH-------VAAALNHK-------KVVKVLLEAGADTTIVNNAGQTPL 244
Cdd:PHA02716 353 NTVLHtylsmlsVVNILDPEtdndirlDVIQCLISLGADITAVNCLGYTPL 403
Ank_5 pfam13857
Ankyrin repeats (many copies);
94-148 1.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 172045720   94 LIREG-CALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLA 148
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 1.37e-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: 44.89  E-value: 1.37e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 172045720    41 HGRTPLHLAANKGHLSVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 71-202 1.40e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  71 QDDGDQTALHRATVvgnteiltalirEGCALdrqdkdgntalheaAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQ 150
Cdd:PTZ00322  71 EEVIDPVVAHMLTV------------ELCQL--------------AASGDAVGARILLTGGADPNCRDYDGRTPLHIACA 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 172045720 151 NSHSQSTRILLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLNAFCSVHE 202
Cdd:PTZ00322 125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 131-232 2.57e-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: 50.78  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 131 GANVLARNKAGNTALHLACQNSHSQSTRILLLGgSRADL--KNNAGDTCLHVAARYNHLSVVRLLLNAfcsVHE-KNQA- 206
Cdd:cd22192    7 ELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLMEA---APElVNEPm 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 172045720 207 ------GDTALHVAAALNHKKVVKVLLEAGAD 232
Cdd:cd22192   83 tsdlyqGETALHIAVVNQNLNLVRELIARGAD 114
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-247 2.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 2.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 172045720  192 LLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETA 247
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 10-96 5.08e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  10 LSERLLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNT 88
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGADPnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                 ....*...
gi 172045720  89 EILTALIR 96
Cdd:PTZ00322 162 EVVQLLSR 169
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 207-238 9.18e-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: 9.18e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 172045720  207 GDTALHVAAA-LNHKKVVKVLLEAGADTTIVNN 238
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-70 1.24e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 1.24e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 172045720   41 HGRTPLHLAANKGHLSVVQILLKAGCDLDV 70
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-139 1.40e-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: 42.28  E-value: 1.40e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 172045720  107 DGNTALHEAAWH-GFSQSAKLLVKAGANVLARNK 139
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-181 2.23e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 172045720  127 LVKAG-ANVLARNKAGNTALHLACQNSHSQSTRILLLGGSRADLKNNAGDTCLHVA 181
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 29-147 4.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.20  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  29 LINKGAKV-AVTKH-GRTPLH--LAANKG-HLSVVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEILTALIREGCAL 101
Cdd:PHA02859  72 LIENGADVnFKTRDnNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSF 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 172045720 102 DRQDKDGNTALHE-AAWHGFSQSAKLLVKAGANVLARNKAGNTALHL 147
Cdd:PHA02859 152 LNKDFDNNNILYSyILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-194 7.17e-05

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: 46.23  E-value: 7.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTALIREGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  107 DGNTALHeaawhgfsqsakLLVkaganVLARNKAGNTALHLACQNS------HSQSTRILllggsrADLKNNAGDTCLHV 180
Cdd:TIGR00870 207 LGNTLLH------------LLV-----MENEFKAEYEELSCQMYNFalslldKLRDSKEL------EVILNHQGLTPLKL 263

                         170
                  ....*....|....
gi 172045720  181 AARYNHLSVVRLLL 194
Cdd:TIGR00870 264 AAKEGRIVLFRLKL 277
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 47-127 7.37e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 7.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  47 HLAANkGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKL 126
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 .
gi 172045720 127 L 127
Cdd:PTZ00322 167 L 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 207-235 1.06e-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: 39.88  E-value: 1.06e-04
                           10        20
                   ....*....|....*....|....*....
gi 172045720   207 GDTALHVAAALNHKKVVKVLLEAGADTTI 235
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 193-263 1.08e-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: 45.52  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 193 LLNAfcSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTI---------VNNA-----GQTPLETARYHNNPE-VAL 257
Cdd:cd22194  129 FINA--EYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEiVQL 206


                 ....*.
gi 172045720 258 LLTKAP 263
Cdd:cd22194  207 LMEKES 212
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 174-202 1.14e-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: 39.49  E-value: 1.14e-04
                           10        20
                   ....*....|....*....|....*....
gi 172045720   174 GDTCLHVAARYNHLSVVRLLLNAFCSVHE 202
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-204 1.48e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 1.48e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 172045720  174 GDTCLHVAA-RYNHLSVVRLLLNAFCSVHEKN 204
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 125-251 1.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.27  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 125 KLLVKAGANVLARNKAGN-TALHLAC---QNSHSQSTRILLLGGSRADLKNNAGDTCLHV-AARYN-HLSVVRLLLNAFC 198
Cdd:PHA02859  70 KFLIENGADVNFKTRDNNlSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLLIDSGV 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 172045720 199 SVHEKNQAGDTALHVAAAL-NHKKVVKVLLEAGADTTIVNNAGQTPLETARYHN 251
Cdd:PHA02859 150 SFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA03095 PHA03095
ankyrin-like protein; Provisional
 187-262 2.32e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 187 LSVVRLLLNAFCSVHEKNQAGDTALHVAAALNH---KKVVKVLLEAGADTTIVNNAGQTPLETARYHNN-PEVALLLTKA 262
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 145-267 2.70e-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: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  145 LHLACQNSHSQSTRILLLGGSRADLknnaGDTCLHvAARYNHLSVVRLLLNAFCSVHEKN--------------QAGDTA 210
Cdd:TIGR00870  57 FVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSgplelandqytsefTPGITA 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 172045720  211 LHVAAALNHKKVVKVLLEAGADTTIVNNA--------------GQTPLETARYHNNPEVALLLTKAPQILR 267
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADIL 202
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 42-259 4.95e-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: 43.53  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   42 GRTPLHLAANKG-HLSVVQILLKAGCDLDVQDdgdqTALHRAT--VVGNTEILTALI----REGC----ALDRQDKD--- 107
Cdd:TIGR00870  52 GRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISleYVDAVEAILLHLlaafRKSGplelANDQYTSEftp 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  108 GNTALHEAAWHGFSQSAKLLVKAGANVLARnkagntalhlACQNSHSQSTRILLLGGSRADLknNAgdtclhvAARYNHL 187
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPAR----------ACGDFFVKSQGVDSFYHGESPL--NA-------AACLGSP 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  188 SVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKV------------VKVLLEAGADTT----IVNNAGQTPLETARYHN 251
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLHLLVMENEFKAeyeelscqmynfALSLLDKLRDSKelevILNHQGLTPLKLAAKEG 268


                  ....*...
gi 172045720  252 NPEVALLL 259
Cdd:TIGR00870 269 RIVLFRLK 276
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 207-232 9.17e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 9.17e-04
                          10        20
                  ....*....|....*....|....*.
gi 172045720  207 GDTALHVAAALNHKKVVKVLLEAGAD 232
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 137-261 1.37e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 137 RNKAGNTALHLAC-----------QNSHSQSTRILLLGgsradlKNNAGDTCLHVAARYNHL---SVVRLLLNAFCSVHE 202
Cdd:PHA02736  13 PDIEGENILHYLCrnggvtdllafKNAISDENRYLVLE------YNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADING 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 172045720 203 KNQA-GDTALHVAAALNHKKVVKVLL-EAGADTTIVNNAGQTPLETARYHNNPEVALLLTK 261
Cdd:PHA02736  87 KERVfGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRA 147
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-202 1.39e-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: 36.47  E-value: 1.39e-03
                          10        20
                  ....*....|....*....|....*....
gi 172045720  174 GDTCLHVAARYNHLSVVRLLLNAFCSVHE 202
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 42-150 1.98e-03

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: 41.67  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTaLIREGCALD--RQD 105
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQ-LLMEKESTDitSQD 219

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 172045720 106 KDGNTALH---EAAWHGFSQSA-------KLLVKAGANVL--ARNKAGNTALHLACQ 150
Cdd:cd22194  220 SRGNTVLHalvTVAEDSKTQNDfvkrmydMILLKSENKNLetIRNNEGLTPLQLAAK 276
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-134 2.07e-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: 36.03  E-value: 2.07e-03
                           10        20
                   ....*....|....*....|....*...
gi 172045720   107 DGNTALHEAAWHGFSQSAKLLVKAGANV 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 4-113 6.39e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.86  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720   4 QDAVAALSERLLIAAYKgqTENVVQLINKGAKVAVTKhGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD-------- 75
Cdd:cd21882   38 NDGVNEAIMLLLEAAPD--SGNPKELVNAPCTDEFYQ-GQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgn 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 172045720  76 -----QTALHRATVVGNTEILTALIREG---CALDRQDKDGNTALH 113
Cdd:cd21882  115 lfyfgELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
PHA02798 PHA02798
ankyrin-like protein; Provisional
 55-212 6.90e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 6.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720  55 LSVVQILLKAgCDLDV---QDDGDQTALHRATVvgNTEILTALIREGCALDRQDKDGNTAL-----HEAAWHGFSQSAKL 126
Cdd:PHA02798  18 LSTVKLLIKS-CNPNEivnEYSIFQKYLQRDSP--STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045720 127 LVKAGANVLARNKAGNTALHLACQNSHSQSTRILLL---GGSRADLKNNAGDTCLHVAARYNH---LSVVRLLLNAFCSV 200
Cdd:PHA02798  95 LIENGADINKKNSDGETPLYCLLSNGYINNLEILLFmieNGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDI 174

                        170
                 ....*....|...
gi 172045720 201 HE-KNQAGDTALH 212
Cdd:PHA02798 175 NThNNKEKYDTLH 187
McIdas_CC cd22590
central coiled-coil domain of McIdas (or multicilin); McIdas (also called Idas or multicilin), ...
 422-467 9.50e-03

central coiled-coil domain of McIdas (or multicilin); McIdas (also called Idas or multicilin), together with geminin coiled-coil domain-containing protein 1 (GemC1) and geminin, controls both the cell cycle and differentiation decisions in cells. Idas binds to geminin and is implicated in DNA replication control. It also functions as an early regulator of multiciliogenesis. GemC1 and McIdas specify the multiciliate cell fate by forming complexes with the E2F4/5 transcription factors, resulting in centriole amplification and cilia formation. Idas belongs to the geminin family of proteins that also includes geminin and GemC1. They share a homologous central coiled-coil domain that mediates homo- and heterodimerization with other family members; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of McIdas.


Pssm-ID: 439144  Cd Length: 64  Bit Score: 35.16  E-value: 9.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 172045720 422 NQLEATVEEIRAELGSVQDKvNAKLGQMESKTQHQMCVLDKLMVER 467
Cdd:cd22590   20 NQLHETLTRKQEEIDSLQER-NVQLKELASQAKHLASVLDKLMTVR 64
 
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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