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Conserved domains on  [gi|489124077|ref|WP_003033877|]
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MULTISPECIES: ankyrin repeat domain-containing protein [Citrobacter]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-201 1.88e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.13  E-value: 1.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   1 MSEKELITEFLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLIsc 80
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL-- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  81 ltndltllrtvlpanpdlnclsrfggvgitpASEKGHVEIVReLLLRTDINVNHTNFVGWTPLLEAIVLNDggakqQEIV 160
Cdd:COG0666  160 -------------------------------AAANGNLEIVK-LLLEAGADVNARDNDGETPLHLAAENGH-----LEIV 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489124077 161 KLLLDHGANPHMTDKYGKTPLELAREKGYHEIAELLIAAGA 201
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-201 1.88e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.13  E-value: 1.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   1 MSEKELITEFLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLIsc 80
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL-- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  81 ltndltllrtvlpanpdlnclsrfggvgitpASEKGHVEIVReLLLRTDINVNHTNFVGWTPLLEAIVLNDggakqQEIV 160
Cdd:COG0666  160 -------------------------------AAANGNLEIVK-LLLEAGADVNARDNDGETPLHLAAENGH-----LEIV 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489124077 161 KLLLDHGANPHMTDKYGKTPLELAREKGYHEIAELLIAAGA 201
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-201 1.93e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 1.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  26 LAKNVDINATNRQGRTAIIIASLNK--HYDCVSLLIAEGADINKQDQTCFNP---FLISClTNDLTLLRTVLPANPDLNC 100
Cdd:PHA03100  93 LEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLlhlYLESN-KIDLKILKLLIDKGVDINA 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077 101 LSRFggvgitpasekghveivrELLLRTDINVNHTNFVGWTPLLEAIVLNDggakqQEIVKLLLDHGANPHMTDKYGKTP 180
Cdd:PHA03100 172 KNRV------------------NYLLSYGVPINIKDVYGFTPLHYAVYNNN-----PEFVKYLLDLGANPNLVNKYGDTP 228

                        170       180
                 ....*....|....*....|.
gi 489124077 181 LELAREKGYHEIAELLIAAGA 201
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-201 1.14e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  112 ASEKGHVEIVrELLLRTDINVNHTNFVGWTPLLEAIVLNdggakQQEIVKLLLDHgANPHMTDkYGKTPLELAREKGYHE 191
Cdd:pfam12796   4 AAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNG-----HLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75

                          90
                  ....*....|
gi 489124077  192 IAELLIAAGA 201
Cdd:pfam12796  76 IVKLLLEKGA 85
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 39-198 8.59e-09

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: 54.32  E-value: 8.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   39 GRTAIIIASLNKHYDCVSLLIAEGADINKqdQTCFNPFLIScltndltllrtvlpanPDLNCLsRFGGVGITPASEKGHV 118
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFVKS----------------QGVDSF-YHGESPLNAAACLGSP 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  119 EIVReLLLRTDINVNHTNFVGWTPLLEAIVLNDGGAKQQEIV----KLLLDHGANP-------HMTDKYGKTPLELAREK 187
Cdd:TIGR00870 189 SIVA-LLSEDPADILTADSLGNTLLHLLVMENEFKAEYEELScqmyNFALSLLDKLrdskeleVILNHQGLTPLKLAAKE 267

                         170
                  ....*....|.
gi 489124077  188 GYHEIAELLIA 198
Cdd:TIGR00870 268 GRIVLFRLKLA 278
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-181 9.13e-05

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: 42.31  E-value: 9.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   1 MSEKELITEFLL--AAEQGNADGLKSCL-AKNVDINATNRQGRTAIIIASLNKHYDcVSLLIAEGAdinkqdqtcfnPFL 77
Cdd:cd22192   10 LLQQKRISESPLllAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLE-AAVVLMEAA-----------PEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  78 IScltndltllrtvLPANPDLNclsrfggVGITP---ASEKGHVEIVRELLLR-TDIN---VNHTNFV---------GWT 141
Cdd:cd22192   78 VN------------EPMTSDLY-------QGETAlhiAVVNQNLNLVRELIARgADVVsprATGTFFRpgpknliyyGEH 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489124077 142 PL-LEAIVLNdggakqQEIVKLLLDHGANPHMTDKYGKTPL 181
Cdd:cd22192  139 PLsFAACVGN------EEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 38-67 1.58e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 1.58e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 489124077    38 QGRTAIIIASLNKHYDCVSLLIAEGADINK 67
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-201 1.88e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.13  E-value: 1.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   1 MSEKELITEFLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLIsc 80
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL-- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  81 ltndltllrtvlpanpdlnclsrfggvgitpASEKGHVEIVReLLLRTDINVNHTNFVGWTPLLEAIVLNDggakqQEIV 160
Cdd:COG0666  160 -------------------------------AAANGNLEIVK-LLLEAGADVNARDNDGETPLHLAAENGH-----LEIV 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489124077 161 KLLLDHGANPHMTDKYGKTPLELAREKGYHEIAELLIAAGA 201
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-201 9.02e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.50  E-value: 9.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   4 KELITEFLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTN 83
Cdd:COG0666   19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  84 DLTLLRTVLPANPDLNCLSRFGGVGITPASEKGHVEIVReLLLRTDINVNHTNFVGWTPLLEAIVLNDggakqQEIVKLL 163
Cdd:COG0666   99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK-LLLEAGADVNAQDNDGNTPLHLAAANGN-----LEIVKLL 172

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489124077 164 LDHGANPHMTDKYGKTPLELAREKGYHEIAELLIAAGA 201
Cdd:COG0666  173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-201 1.53e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.85  E-value: 1.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  26 LAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLTLLRTVLPANPDLNCLSRFG 105
Cdd:COG0666    8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077 106 GVGITPASEKGHVEIVReLLLRTDINVNHTNFVGWTPLLEAIVLNDggakqQEIVKLLLDHGANPHMTDKYGKTPLELAR 185
Cdd:COG0666   88 NTLLHAAARNGDLEIVK-LLLEAGADVNARDKDGETPLHLAAYNGN-----LEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                        170
                 ....*....|....*.
gi 489124077 186 EKGYHEIAELLIAAGA 201
Cdd:COG0666  162 ANGNLEIVKLLLEAGA 177
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-201 5.37e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 5.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   8 TEFLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQtcfnpfliscltNDLTL 87
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN------------DGETP 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  88 LrtvlpanpdlnclsrfggvgiTPASEKGHVEIVrELLLRTDINVNHTNFVGWTPLLEAIVLNDggakqQEIVKLLLDHG 167
Cdd:COG0666  190 L---------------------HLAAENGHLEIV-KLLLEAGADVNAKDNDGKTALDLAAENGN-----LEIVKLLLEAG 242

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489124077 168 ANPHMTDKYGKTPLELAREKGYHEIAELLIAAGA 201
Cdd:COG0666  243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-201 1.93e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 1.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  26 LAKNVDINATNRQGRTAIIIASLNK--HYDCVSLLIAEGADINKQDQTCFNP---FLISClTNDLTLLRTVLPANPDLNC 100
Cdd:PHA03100  93 LEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLlhlYLESN-KIDLKILKLLIDKGVDINA 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077 101 LSRFggvgitpasekghveivrELLLRTDINVNHTNFVGWTPLLEAIVLNDggakqQEIVKLLLDHGANPHMTDKYGKTP 180
Cdd:PHA03100 172 KNRV------------------NYLLSYGVPINIKDVYGFTPLHYAVYNNN-----PEFVKYLLDLGANPNLVNKYGDTP 228

                        170       180
                 ....*....|....*....|.
gi 489124077 181 LELAREKGYHEIAELLIAAGA 201
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-201 1.14e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  112 ASEKGHVEIVrELLLRTDINVNHTNFVGWTPLLEAIVLNdggakQQEIVKLLLDHgANPHMTDkYGKTPLELAREKGYHE 191
Cdd:pfam12796   4 AAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNG-----HLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75

                          90
                  ....*....|
gi 489124077  192 IAELLIAAGA 201
Cdd:pfam12796  76 IVKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
43-174 5.73e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 5.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   43 IIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCltndltllrtvlpanpdlnclsrfggvgitpasEKGHVEIVR 122
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAA---------------------------------KNGHLEIVK 47

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489124077  123 ELLLRTDINVNHTnfvGWTPLLEAIVLNdggakQQEIVKLLLDHGANPHMTD 174
Cdd:pfam12796  48 LLLEHADVNLKDN---GRTALHYAARSG-----HLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-201 6.55e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.85  E-value: 6.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  10 FLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIAS-LNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLTLL 88
Cdd:PHA02876 312 YLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  89 RTVLPANPDLNCLSRFGGVGITPASEKGHVEIVRELLLRTDINVNHTNFVGWTPLLEAIVLNdggaKQQEIVKLLLDHGA 168
Cdd:PHA02876 392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN----CKLDVIEMLLDNGA 467

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489124077 169 NPHMTDKYGKTPLELARekGYHEIAELLIAAGA 201
Cdd:PHA02876 468 DVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-200 1.27e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   1 MSEKELITEFLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADinkqdqTCFNPflISC 80
Cdd:PHA02874  30 ISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD------TSILP--IPC 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  81 LTNDLtlLRTVLPANPDLNCLSRFGGVGITPASEKGHVEIVRELL-LRTDINVNHTNfvGWTPLLEAIVLNdggakQQEI 159
Cdd:PHA02874 102 IEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFeYGADVNIEDDN--GCYPIHIAIKHN-----FFDI 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489124077 160 VKLLLDHGANPHMTDKYGKTPLELAREKGYHEIAELLIAAG 200
Cdd:PHA02874 173 IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-99 5.94e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 5.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   10 FLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIaEGADINKQDQTcFNPFLISCLTNDLTLLR 89
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|
gi 489124077   90 TVLPANPDLN 99
Cdd:pfam12796  79 LLLEKGADIN 88
PHA03095 PHA03095
ankyrin-like protein; Provisional
 10-200 8.15e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 8.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  10 FLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDC---VSLLIAEGADINKQDQTCFNPfLISCLTNDLT 86
Cdd:PHA03095  18 YLLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTP-LHLYLYNATT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  87 L--LRTVLPANPDLNclsRFGGVGITP-----ASEKGHVEIVReLLLRTDINVNHTNFVGWTPLleAIVLNDGGAkQQEI 159
Cdd:PHA03095  97 LdvIKLLIKAGADVN---AKDKVGRTPlhvylSGFNINPKVIR-LLLRKGADVNALDLYGMTPL--AVLLKSRNA-NVEL 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489124077 160 VKLLLDHGANPHMTDKYGKTPLE--LAREKGYHEIAELLIAAG 200
Cdd:PHA03095 170 LRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAG 212
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 39-198 8.59e-09

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: 54.32  E-value: 8.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   39 GRTAIIIASLNKHYDCVSLLIAEGADINKqdQTCFNPFLIScltndltllrtvlpanPDLNCLsRFGGVGITPASEKGHV 118
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFVKS----------------QGVDSF-YHGESPLNAAACLGSP 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  119 EIVReLLLRTDINVNHTNFVGWTPLLEAIVLNDGGAKQQEIV----KLLLDHGANP-------HMTDKYGKTPLELAREK 187
Cdd:TIGR00870 189 SIVA-LLSEDPADILTADSLGNTLLHLLVMENEFKAEYEELScqmyNFALSLLDKLrdskeleVILNHQGLTPLKLAAKE 267

                         170
                  ....*....|.
gi 489124077  188 GYHEIAELLIA 198
Cdd:TIGR00870 268 GRIVLFRLKLA 278
Ank_4 pfam13637
Ankyrin repeats (many copies);
13-59 3.84e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 3.84e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 489124077   13 AAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLI 59
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-69 3.98e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 3.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489124077   12 LAAEQGNADGLKsCLAKNVDINATNrQGRTAIIIASLNKHYDCVSLLIAEGADINKQD 69
Cdd:pfam12796  36 LAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 11-201 4.94e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  11 LLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDqtcfnpfliscltndltllrt 90
Cdd:PLN03192 530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRD--------------------- 588

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  91 vlpANpdlnclsrfGGVGITPASEKGHVEIVRELLLRTDINVNHTnfvGWTPLLEAIVLNDGGAkqqeiVKLLLDHGANP 170
Cdd:PLN03192 589 ---AN---------GNTALWNAISAKHHKIFRILYHFASISDPHA---AGDLLCTAAKRNDLTA-----MKELLKQGLNV 648

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489124077 171 HMTDKYGKTPLELAREKGYHEIAELLIAAGA 201
Cdd:PLN03192 649 DSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 124-196 5.39e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 5.39e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124077 124 LLLRTDINVNHTNFVGWTPLLEAIVLNdggakQQEIVKLLLDHGANPHMTDKYGKTPLELAREKGYHEIAELL 196
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANG-----HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 12-67 7.89e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 7.89e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489124077  12 LAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINK 67
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-201 1.90e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  26 LAKNVDINATNRQGRTAIII--ASLNKHYDCVSLLIAEGADINKQDQTCFNP---FLISclTN-DLTLLRTVL-----PA 94
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPlavLLKS--RNaNVELLRLLIdagadVY 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  95 NPDLNCLSRFGgvgITPASEKGHVEIVRELLlRTDINVNHTNFVGWTPLLeaiVLNDGGAKQQEIVKLLLDHGANPHMTD 174
Cdd:PHA03095 182 AVDDRFRSLLH---HHLQSFKPRARIVRELI-RAGCDPAATDMLGNTPLH---SMATGSSCKRSLVLPLLIAGISINARN 254

                        170       180
                 ....*....|....*....|....*..
gi 489124077 175 KYGKTPLELAREKGYHEIAELLIAAGA 201
Cdd:PHA03095 255 RYGQTPLHYAAVFNNPRACRRLIALGA 281
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-184 2.20e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  18 NADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLTLLRTVLPANPD 97
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  98 LNCLSRFGGVGITPASEKGHVEIVRELLLRTDINVNHTNfVGWTPLLEAIVLNdggakqQEIVKLLLDHgANPHMTDKYG 177
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHN------RSAIELLINN-ASINDQDIDG 254


                 ....*..
gi 489124077 178 KTPLELA 184
Cdd:PHA02874 255 STPLHHA 261
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-197 8.84e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 8.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  22 LKSCLAKNVDINATNR-QGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLTLLRTVLPANPDLNC 100
Cdd:PHA02878 150 TKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077 101 LSRFGGVGITPASEK-GHVEIVRELLLR-TDINVNHTnFVGWTPLLEAIvlndggaKQQEIVKLLLDHGANPHMTDKYGK 178
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHgVDVNAKSY-ILGLTALHSSI-------KSERKLKLLLEYGADINSLNSYKL 301

                        170       180
                 ....*....|....*....|
gi 489124077 179 TPLELAREKGY-HEIAELLI 197
Cdd:PHA02878 302 TPLSSAVKQYLcINIGRILI 321
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-127 1.42e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  26 LAKNVDINATNRQGRTAIIIAS-LNKHYDCVSlLIAEGADINKQDQTCFNPFLISCLTNDLTLLRTVLPANPD------- 97
Cdd:PHA03095 244 LIAGISINARNRYGQTPLHYAAvFNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSaetvaat 322

                         90       100       110
                 ....*....|....*....|....*....|
gi 489124077  98 LNCLSRFGGVGITPASEkghvEIVRELLLR 127
Cdd:PHA03095 323 LNTASVAGGDIPSDATR----LCVAKVVLR 348
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 123-201 3.13e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077 123 ELLLRTDINVNHTNFVGWTPL----LEAIVLNDGgakqQEIVKLLLDHGANPHMTDKYGKTPLELA--REKGYHEIAELL 196
Cdd:PHA03100  52 KILLDNGADINSSTKNNSTPLhylsNIKYNLTDV----KEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYL 127


                 ....*
gi 489124077 197 IAAGA 201
Cdd:PHA03100 128 LDNGA 132
Ank_5 pfam13857
Ankyrin repeats (many copies);
124-184 6.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 6.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489124077  124 LLLRTDINVNHTNFVGWTPLLEAIvlndgGAKQQEIVKLLLDHGANPHMTDKYGKTPLELA 184
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAA-----KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-201 7.87e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  17 GNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLTLLRTVLPANP 96
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  97 DLNCLsrFGGVGITP---ASEKGHVEIVRELLLR-TDINVNHTNfvGWTPLLEAIVLNDggakqQEIVKLLLDHGANPHM 172
Cdd:PHA02875  93 FADDV--FYKDGMTPlhlATILKKLDIMKLLIARgADPDIPNTD--KFSPLHLAVMMGD-----IKGIELLIDHKACLDI 163

                        170       180
                 ....*....|....*....|....*....
gi 489124077 173 TDKYGKTPLELAREKGYHEIAELLIAAGA 201
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-201 7.90e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 7.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   7 ITEFLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLT 86
Cdd:PHA02876 179 ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLETSLL 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  87 LLRTVLPANPDLNC-------------LSRF------GGVGITPASEKGH------------VEIVRELLLRtDINVNHT 135
Cdd:PHA02876 259 LYDAGFSVNSIDDCkntplhhasqapsLSRLvpklleRGADVNAKNIKGEtplylmakngydTENIRTLIML-GADVNAA 337

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489124077 136 NFVGWTPLLEAIVLNdggaKQQEIVKLLLDHGANPHMTDKYGKTPLELAREKGYHEIAELLIAAGA 201
Cdd:PHA02876 338 DRLYITPLHQASTLD----RNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399
Ank_4 pfam13637
Ankyrin repeats (many copies);
139-197 1.35e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 1.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489124077  139 GWTPLLEAIVLNDggakqQEIVKLLLDHGANPHMTDKYGKTPLELAREKGYHEIAELLI 197
Cdd:pfam13637   1 ELTALHAAAASGH-----LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 76-201 2.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  76 FLISCLTNDLTLLRTVLPANPDLNCLsrfGGVGITPASEKGH------VEIVReLLLRTDINVNHTNFVGWTPLlEAIVL 149
Cdd:PHA03095  18 YLLNASNVTVEEVRRLLAAGADVNFR---GEYGKTPLHLYLHyssekvKDIVR-LLLEAGADVNAPERCGFTPL-HLYLY 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489124077 150 NdggAKQQEIVKLLLDHGANPHMTDKYGKTPLE--LAREKGYHEIAELLIAAGA 201
Cdd:PHA03095  93 N---ATTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGA 143
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-201 4.04e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  32 INATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLTLLRTVLPANPDLNCLSrfggvgiTP 111
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILP-------IP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077 112 ASEKGHVEIVrellLRTDINVNHTNFVGWTPLLEAIVLNDggakqQEIVKLLLDHGANPHMTDKYGKTPLELAREKGYHE 191
Cdd:PHA02874 101 CIEKDMIKTI----LDCGIDVNIKDAELKTFLHYAIKKGD-----LESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171

                        170
                 ....*....|
gi 489124077 192 IAELLIAAGA 201
Cdd:PHA02874 172 IIKLLLEKGA 181
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-201 5.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 5.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  13 AAEQGNADGLKSCLAKNVDIN-ATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLTLLrtv 91
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI--- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  92 lpanpdlnclsrfggvgitpasekghveivrELLLRTDINVNHTNFVGWTPLLEAIvlndgGAKQQEIVKLLLDHGANPH 171
Cdd:PHA02875 152 -------------------------------ELLIDHKACLDIEDCCGCTPLIIAM-----AKGDIAICKMLLDSGANID 195

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489124077 172 MTDKYGK-TPLELAREKGYHEIAELLIAAGA 201
Cdd:PHA02875 196 YFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-181 9.13e-05

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: 42.31  E-value: 9.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   1 MSEKELITEFLL--AAEQGNADGLKSCL-AKNVDINATNRQGRTAIIIASLNKHYDcVSLLIAEGAdinkqdqtcfnPFL 77
Cdd:cd22192   10 LLQQKRISESPLllAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLE-AAVVLMEAA-----------PEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  78 IScltndltllrtvLPANPDLNclsrfggVGITP---ASEKGHVEIVRELLLR-TDIN---VNHTNFV---------GWT 141
Cdd:cd22192   78 VN------------EPMTSDLY-------QGETAlhiAVVNQNLNLVRELIARgADVVsprATGTFFRpgpknliyyGEH 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489124077 142 PL-LEAIVLNdggakqQEIVKLLLDHGANPHMTDKYGKTPL 181
Cdd:cd22192  139 PLsFAACVGN------EEIVRLLIEHGADIRAQDSLGNTVL 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 4-165 1.14e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   4 KELITEFLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTN 83
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  84 DLTLLRTVLPANPDLNCLSRFGGVG-ITPASEKGHVEIVRELLLR-TDINVNHTNFVGWTPLLEAIVLNDGGAKQQEIVK 161
Cdd:PHA02875 180 DIAICKMLLDSGANIDYFGKNGCVAaLCYAIENNKIDIVRLFIKRgADCNIMFMIEGEECTILDMICNMCTNLESEAIDA 259


                 ....
gi 489124077 162 LLLD 165
Cdd:PHA02875 260 LIAD 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 50-201 2.18e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  50 KHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLTLLRTVLPANpdLNCLSRFGGVGITPASEKGHVEIVRELLLRTD 129
Cdd:PHA02878  48 RNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSI--NKCSVFYTLVAIKDAFNNRNVEIFKIILTNRY 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124077 130 INVNHTNFVgwtpLLEAIVLNDggAKQQEIVKLLLDHGANPHMTDKY-GKTPLELAREKGYHEIAELLIAAGA 201
Cdd:PHA02878 126 KNIQTIDLV----YIDKKSKDD--IIEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGA 192
PHA02798 PHA02798
ankyrin-like protein; Provisional
 18-133 5.66e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 5.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  18 NADGLKSCLAKNVDINATNRQGRTAII-----IASLNKHYDCVSL-LIAEGADINKQDQTCFNPFLISCLTNDLTLLRTV 91
Cdd:PHA02798 198 DADILKLFVDNGFIINKENKSHKKKFMeylnsLLYDNKRFKKNILdFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYL 277

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489124077  92 LPANPDLNCLSRFGGVGITPASEKGHVEIVRElLLRTDINVN 133
Cdd:PHA02798 278 LQLGGDINIITELGNTCLFTAFENESKFIFNS-ILNKKPNKN 318
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-175 6.01e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 6.01e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 489124077  139 GWTPLLEAIVLNDggakQQEIVKLLLDHGANPHMTDK 175
Cdd:pfam00023   2 GNTPLHLAAGRRG----NLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-99 8.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 8.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489124077  26 LAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLTLLRTVLPANPDLN 99
Cdd:PHA03100 179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-92 1.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 1.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489124077   39 GRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPFLISCLTNDLTLLRTVL 92
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 7-75 1.42e-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: 38.97  E-value: 1.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077   7 ITEFLLAAEQGNaDGLKSCLakNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQ-TCFNP 75
Cdd:cd22194  112 IVRILLAFAEEN-GILDRFI--NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgVFFNP 178
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 38-67 1.58e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 1.58e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 489124077    38 QGRTAIIIASLNKHYDCVSLLIAEGADINK 67
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 38-69 2.99e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 2.99e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 489124077   38 QGRTAIIIASL-NKHYDCVSLLIAEGADINKQD 69
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 154-201 3.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 37.72  E-value: 3.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489124077 154 AKQQEIVKLLLDHGANPHMTDKYGKTPLELAREKGYH-----EIAELLIAAGA 201
Cdd:PHA03100  45 ARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGA 97
PHA02946 PHA02946
ankyin-like protein; Provisional
 115-181 3.48e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 37.73  E-value: 3.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124077 115 KGHVEIVRELLLRTDINVNHTNFVGWTPLLEAIVLNDggakqQEIVKLLLDHGANPHMTDKYGKTPL 181
Cdd:PHA02946  48 KGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINN-----NRIVAMLLTHGADPNACDKQHKTPL 109
Ank_5 pfam13857
Ankyrin repeats (many copies);
27-69 3.78e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 3.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 489124077   27 AKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQD 69
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD 46
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-76 5.29e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.19  E-value: 5.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489124077   6 LITEFLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIASLNKHYDCVSLLIAEGADINKQDQTCFNPF 76
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 123-201 5.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 36.78  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077 123 ELLLRTDINVNHTNFVGWTPLLEAIvlndgGAKQQEIVKLLLDHGANPHMTDKYGKTPLELA--REKGYhEIAELLIAAG 200
Cdd:PHA02878 185 ELLLSYGANVNIPDKTNNSPLHHAV-----KHYNKPIVHILLENGASTDARDKCGNTPLHISvgYCKDY-DILKLLLEHG 258


                 .
gi 489124077 201 A 201
Cdd:PHA02878 259 V 259
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 11-192 6.44e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 36.76  E-value: 6.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  11 LLAAEQGNADGLksclaknVDINATNR--QGRTAIIIASLNKHYDCVSLLIAEGADIN---------KQDQTCFN----P 75
Cdd:cd22197   71 EIDKDSGNPKPL-------VNAQCTDEyyRGHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqKKQGTCFYfgelP 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  76 FLISCLTNDLTLLRTVLPANPDLNCLSRFGGVGITpasekghveIVRELLLRTDINVNHTNFVG--WTPLLEAIVLNDGG 153
Cdd:cd22197  144 LSLAACTKQWDVVNYLLENPHQPASLQAQDSLGNT---------VLHALVMIADNSPENSALVIkmYDGLLQAGARLCPT 214

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489124077 154 AKQQEIvkllldhganphmTDKYGKTPLELAREKGYHEI 192
Cdd:cd22197  215 VQLEEI-------------SNHEGLTPLKLAAKEGKIEI 240
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-201 6.57e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 36.91  E-value: 6.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  74 NPFLISCLTNDLTLLRTVLpANPDLNCLSRfGGVGITP---ASEKGHVEIVRELL--LRTDINVNHTN--FVGWTPLLEA 146
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQR-GALGETAlhvAALYDNLEAAVVLMeaAPELVNEPMTSdlYQGETALHIA 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489124077 147 IVLNDggakqQEIVKLLLDHGA---NPHMTDK-----------YGKTPLELAREKGYHEIAELLIAAGA 201
Cdd:cd22192   97 VVNQN-----LNLVRELIARGAdvvSPRATGTffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGA 160
Ank_5 pfam13857
Ankyrin repeats (many copies);
1-46 7.60e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 33.47  E-value: 7.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 489124077    1 MSEKELITEFLLAAEQGNADGLKSCLAKNVDINATNRQGRTAIIIA 46
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 53-181 7.74e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 36.74  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124077  53 DCVSLLIAEGADINKQDQTCFNPflISCL-----TNDLTLLRTVLPANPDLNCLSRFGGVGITPASEKGH---VEIVrEL 124
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETP--LYCLlsngyINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEII-KL 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489124077 125 LLRTDINVN-HTNFVGWTPLLEAIVLNDGGAkQQEIVKLLLDHGANPHMTDKYGKTPL 181
Cdd:PHA02798 167 LLEKGVDINtHNNKEKYDTLHCYFKYNIDRI-DADILKLFVDNGFIINKENKSHKKKF 223
 
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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