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Conserved domains on  [gi|30089994|ref|NP_078984|]
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ankyrin repeat and SOCS box protein 7 isoform 1 [Homo sapiens]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-251 3.82e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 3.82e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  16 LQIQAAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLiGGFTALHYAAMHGRAR 95
Cdd:COG0666  23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  96 IARLMLEseyRSDIINAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNAN 175
Cdd:COG0666 102 IVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30089994 176 IDIQNGF---LLRYAVIKSNHSYCRMFLQRGADTNLgRLEDGQTPLHLSALRDDVLCARMLYNYGADTNTRNYEGQTPL 251
Cdd:COG0666 179 VNARDNDgetPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-251 3.82e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 3.82e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  16 LQIQAAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLiGGFTALHYAAMHGRAR 95
Cdd:COG0666  23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  96 IARLMLEseyRSDIINAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNAN 175
Cdd:COG0666 102 IVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30089994 176 IDIQNGF---LLRYAVIKSNHSYCRMFLQRGADTNLgRLEDGQTPLHLSALRDDVLCARMLYNYGADTNTRNYEGQTPL 251
Cdd:COG0666 179 VNARDNDgetPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 21-241 2.24e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.14  E-value: 2.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   21 AVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKdLIGGFTALHYAAMHGRARIARLM 100
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEEL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  101 LES-EYRSDIInakSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQ 179
Cdd:PHA02875  88 LDLgKFADDVF---YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30089994  180 NGF---LLRYAVIKSNHSYCRMFLQRGADTN-LGRleDGQTPLHLSALRDDVL-CARMLYNYGADTN 241
Cdd:PHA02875 165 DCCgctPLIIAMAKGDIAICKMLLDSGANIDyFGK--NGCVAALCYAIENNKIdIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-180 2.57e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994    85 LHYAAMHGRARIARLMLESEYRsdiINAKSNDGWTPLHVAAHYGRDSFVRLLLEfKAEVDpLSDKGTTPLQLAIIRERSS 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 30089994   165 CVKILLDHNANIDIQN 180
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 49-222 2.80e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.09  E-value: 2.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  49 TLLHFSAARGKERCVRVFLE-HGADPTVKDLIGGfTALHYAAMHGRARIARLMLEsEYRSDIINAKSND---GWTPLHVA 124
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGE-TALHVAALYDNLEAAVVLME-AAPELVNEPMTSDlyqGETALHIA 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994 125 AHYGRDSFVRLLLEFKAEV--------------DPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQNGF---LLRYA 187
Cdd:cd22192  97 VVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLgntVLHIL 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 30089994 188 VIKSNHSY-CRMF---LQRGADTNLGRLE-----DGQTPLHLSA 222
Cdd:cd22192 177 VLQPNKTFaCQMYdliLSYDKEDDLQPLDlvpnnQGLTPFKLAA 220
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 16-107 2.79e-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: 41.99  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994    16 LQIQAAVAAGDVhtVRKMLEQGYSPNGRDANGWTLLH-------FSAARGKERC-----VRVFLEHGADPTVKDLI---G 80
Cdd:TIGR00870 179 LNAAACLGSPSI--VALLSEDPADILTADSLGNTLLHllvmeneFKAEYEELSCqmynfALSLLDKLRDSKELEVIlnhQ 256

                          90       100
                  ....*....|....*....|....*..
gi 30089994    81 GFTALHYAAMHGRARIARLMLESEYRS 107
Cdd:TIGR00870 257 GLTPLKLAAKEGRIVLFRLKLAIKYKQ 283
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 116-144 3.09e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 3.09e-04
                           10        20
                   ....*....|....*....|....*....
gi 30089994    116 DGWTPLHVAAHYGRDSFVRLLLEFKAEVD 144
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-251 3.82e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 3.82e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  16 LQIQAAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLiGGFTALHYAAMHGRAR 95
Cdd:COG0666  23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  96 IARLMLEseyRSDIINAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNAN 175
Cdd:COG0666 102 IVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30089994 176 IDIQNGF---LLRYAVIKSNHSYCRMFLQRGADTNLgRLEDGQTPLHLSALRDDVLCARMLYNYGADTNTRNYEGQTPL 251
Cdd:COG0666 179 VNARDNDgetPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-180 7.00e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 7.00e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  20 AAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDlIGGFTALHYAAMHGRARIARL 99
Cdd:COG0666 126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKL 204

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994 100 MLEseyRSDIINAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQ 179
Cdd:COG0666 205 LLE---AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281


                .
gi 30089994 180 N 180
Cdd:COG0666 282 L 282
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 21-241 2.24e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.14  E-value: 2.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   21 AVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKdLIGGFTALHYAAMHGRARIARLM 100
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEEL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  101 LES-EYRSDIInakSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQ 179
Cdd:PHA02875  88 LDLgKFADDVF---YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30089994  180 NGF---LLRYAVIKSNHSYCRMFLQRGADTN-LGRleDGQTPLHLSALRDDVL-CARMLYNYGADTN 241
Cdd:PHA02875 165 DCCgctPLIIAMAKGDIAICKMLLDSGANIDyFGK--NGCVAALCYAIENNKIdIVRLFIKRGADCN 229
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-251 4.60e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.71  E-value: 4.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  76 KDLIGGFTALHYAAMHGRARIARLMLESEYRSDIINAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQ 155
Cdd:COG0666  13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994 156 LAIIRERSSCVKILLDHNANIDIQNGF---LLRYAVIKSNHSYCRMFLQRGADTNLgRLEDGQTPLHLSALRDDVLCARM 232
Cdd:COG0666  93 AAARNGDLEIVKLLLEAGADVNARDKDgetPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGNLEIVKL 171

                       170
                ....*....|....*....
gi 30089994 233 LYNYGADTNTRNYEGQTPL 251
Cdd:COG0666 172 LLEAGADVNARDNDGETPL 190
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 63-255 2.87e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.64  E-value: 2.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   63 VRVFLEHGADPTVKDLIGGFTALHYAAMHGRARIARLMLESEYRSDIINAKSNdgwTPLHVAAHYGRDSFVRLLLEFKAE 142
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNN---SPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  143 VDPLSDKGTTPLQLAIirersscvkilldhnanidiqnGFLLRYAVIKsnhsycrMFLQRGADTNLGRLEDGQTPLHLSA 222
Cdd:PHA02878 227 TDARDKCGNTPLHISV----------------------GYCKDYDILK-------LLLEHGVDVNAKSYILGLTALHSSI 277

                        170       180       190
                 ....*....|....*....|....*....|...
gi 30089994  223 LRDDVLcaRMLYNYGADTNTRNYEGQTPLAVSI 255
Cdd:PHA02878 278 KSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-180 2.57e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994    85 LHYAAMHGRARIARLMLESEYRsdiINAKSNDGWTPLHVAAHYGRDSFVRLLLEfKAEVDpLSDKGTTPLQLAIIRERSS 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 30089994   165 CVKILLDHNANIDIQN 180
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 29-255 6.79e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.79  E-value: 6.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   29 TVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDlIGGFTALHYAAMHGRARIARLMLEseyRSD 108
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLE---KGA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  109 IINAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSscVKILLDHNANIDIQNgfllryav 188
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINNASINDQD-------- 251

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30089994  189 iksnhsycrmflqrgadtnlgrlEDGQTPLH--LSALRDDVLCARMLYNyGADTNTRNYEGQTPLAVSI 255
Cdd:PHA02874 252 -----------------------IDGSTPLHhaINPPCDIDIIDILLYH-KADISIKDNKGENPIDTAF 296
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-242 3.86e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 3.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   30 VRKMLEQGYSPNGRDANGWTLLHF------SAARGKErCVRVFLEHGADPTVKDlIGGFTALHYAAMHGRARIARLMLES 103
Cdd:PHA03100  51 VKILLDNGADINSSTKNNSTPLHYlsnikyNLTDVKE-IVKLLLEYGANVNAPD-NNGITPLLYAISKKSNSYSIVEYLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  104 EYRSDiINAKSNDGWTPLHVAAHYGRDSF--VRLLLEFKAEVDplsdkgttplqlAIIRersscVKILLDHNANIDIQN- 180
Cdd:PHA03100 129 DNGAN-VNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN------------AKNR-----VNYLLSYGVPINIKDv 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30089994  181 -GFL-LRYAVIKSNHSYCRMFLQRGADTNLgRLEDGQTPLHLSALRDDVLCARMLYNYGADTNT 242
Cdd:PHA03100 191 yGFTpLHYAVYNNNPEFVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-144 1.08e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994    51 LHFSAARGKERCVRVFLEHGADPTVKDLIgGFTALHYAAMHGRARIARLMLESEyrsdIINAKsNDGWTPLHVAAHYGRD 130
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHA----DVNLK-DNGRTALHYAARSGHL 74

                          90
                  ....*....|....
gi 30089994   131 SFVRLLLEFKAEVD 144
Cdd:pfam12796  75 EIVKLLLEKGADIN 88
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-177 1.51e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.99  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   26 DVHTVRKMLEQGYSPNGRDANGWTLLHFSA--ARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAMHGRARiarlmles 103
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGN-TPLHSMATGSSCK-------- 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  104 eyRSDI---------INAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNA 174
Cdd:PHA03095 237 --RSLVlplliagisINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNP 314


                 ...
gi 30089994  175 NID 177
Cdd:PHA03095 315 SAE 317
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-251 2.20e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 2.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   26 DVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERC---VRVFLEHGADPTVKDlIGGFTALHYAAMHG-RARIARLML 101
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPE-RCGFTPLHLYLYNAtTLDVIKLLI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  102 EseYRSDIiNAKSNDGWTPLHV-----AAHYGrdsFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSS--CVKILLDHNA 174
Cdd:PHA03095 105 K--AGADV-NAKDKVGRTPLHVylsgfNINPK---VIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  175 NI----DIQNGFLLRYAV-IKSNHSYCRMFLQRGADTNlGRLEDGQTPLHLSALRDDvlCARML-YNY---GADTNTRNY 245
Cdd:PHA03095 179 DVyavdDRFRSLLHHHLQsFKPRARIVRELIRAGCDPA-ATDMLGNTPLHSMATGSS--CKRSLvLPLliaGISINARNR 255


                 ....*.
gi 30089994  246 EGQTPL 251
Cdd:PHA03095 256 YGQTPL 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
21-111 2.56e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 2.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994    21 AVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGAdptVKDLIGGFTALHYAAMHGRARIARLM 100
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD---VNLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 30089994   101 LESEYRSDIIN 111
Cdd:pfam12796  81 LEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 58-255 3.17e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.78  E-value: 3.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   58 GKERCVRVFLEHGA-------DPTVKDLIggfTALHYAAMHGRARIARLMLESEYRsdiINAKSNDGWTPLHVAAHY--- 127
Cdd:PHA03100   8 TKSRIIKVKNIKYIimeddlnDYSYKKPV---LPLYLAKEARNIDVVKILLDNGAD---INSSTKNNSTPLHYLSNIkyn 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  128 -GRD-SFVRLLLEFKAEVDPLSDKGTTPLQLAIIRER--SSCVKILLDHNANIDIQN--GFLLRYAVIKSNH---SYCRM 198
Cdd:PHA03100  82 lTDVkEIVKLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNsdGENLLHLYLESNKidlKILKL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30089994  199 FLQRGADTN----------LGRLED-----GQTPLHLSALRDDVLCARMLYNYGADTNTRNYEGQTPLAVSI 255
Cdd:PHA03100 162 LIDKGVDINaknrvnyllsYGVPINikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 13-259 4.28e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   13 QEELQIQAAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHF-SAARGKERCVRVFLEHGADPTVKDlIGGFTALHYAAMH 91
Cdd:PHA02876 239 KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHaSQAPSLSRLVPKLLERGADVNAKN-IKGETPLYLMAKN 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   92 G--RARIARLMLeseyRSDIINAKSNDGWTPLHVAAHYGRDS-FVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKI 168
Cdd:PHA02876 318 GydTENIRTLIM----LGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINT 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  169 LLDHNANIDIQN---GFLLRYAVIKSN-HSYCRMFLQRGADTNlGRLEDGQTPLHLSALRD---DVLcaRMLYNYGADTN 241
Cdd:PHA02876 394 LLDYGADIEALSqkiGTALHFALCGTNpYMSVKTLIDRGANVN-SKNKDLSTPLHYACKKNcklDVI--EMLLDNGADVN 470

                        250
                 ....*....|....*...
gi 30089994  242 TRNYEGQTPLAVSISISG 259
Cdd:PHA02876 471 AINIQNQYPLLIALEYHG 488
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-184 7.59e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 7.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   26 DVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKE--RCVRVFLEHGADPTVKDLIGgFTALHYAAMHGRA--RIARLML 101
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNsySIVEYLLDNGANVNIKNSDG-ENLLHLYLESNKIdlKILKLLI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  102 ES--------------EYRSDIiNAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVK 167
Cdd:PHA03100 164 DKgvdinaknrvnyllSYGVPI-NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242

                        170
                 ....*....|....*..
gi 30089994  168 ILLDHNANIDIQNGFLL 184
Cdd:PHA03100 243 LLLNNGPSIKTIIETLL 259
PHA03095 PHA03095
ankyrin-like protein; Provisional
 6-232 8.39e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.91  E-value: 8.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994    6 CRRNPelqeeLQIQAAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLH--FSAARGKERCVRVFLEHGADPTVKDLIGgFT 83
Cdd:PHA03095 116 VGRTP-----LHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRF-RS 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   84 ALHYAAMHGRARiARLMLESEYRSDIINAKSNDGWTPLHVAAHYG--RDSFVRLLLEFKAEVDPLSDKGTTPLQlaiire 161
Cdd:PHA03095 190 LLHHHLQSFKPR-ARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLH------ 262

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30089994  162 rsscvkilldhnanidiqngfllrYAVIKSNHSYCRMFLQRGADTNLgRLEDGQTPLHLSALRDDVLCARM 232
Cdd:PHA03095 263 ------------------------YAAVFNNPRACRRLIALGADINA-VSSDGNTPLSLMVRNNNGRAVRA 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-244 9.83e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 9.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   121 LHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHnANIDIQNgfllryaviksnhsycrmfl 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-------------------- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 30089994   201 qrgadtnlgrleDGQTPLHLSALRDDVLCARMLYNYGADTNTRN 244
Cdd:pfam12796  60 ------------NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 8-180 1.81e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.69  E-value: 1.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994    8 RNPELQEELQIqaAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHY 87
Cdd:PHA02874 120 KDAELKTFLHY--AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   88 AAMHGRARIARLMLesEYRSDIINaKSNDGWTPLHVAAHYGRdSFVRLLLEfKAEVDPLSDKGTTPLQLAIireRSSC-- 165
Cdd:PHA02874 197 AAEYGDYACIKLLI--DHGNHIMN-KCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAI---NPPCdi 268

                        170
                 ....*....|....*..
gi 30089994  166 --VKILLDHNANIDIQN 180
Cdd:PHA02874 269 diIDILLYHKADISIKD 285
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-158 7.26e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 7.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   18 IQAAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKdLIGGFTALHYAAMHGRARIA 97
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGFTPLHNAIIHNRSAIE 239

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30089994   98 RLMleseyRSDIINAKSNDGWTPLHVAAHYGRD-SFVRLLLEFKAEVDPLSDKGTTPLQLAI 158
Cdd:PHA02874 240 LLI-----NNASINDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAF 296
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 20-180 1.43e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.50  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   20 AAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDlIGGFTALHYAAMHGRARIARL 99
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRD-ANGNTALWNAISAKHHKIFRI 609

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  100 MLESEYRSDiinakSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQ 179
Cdd:PLN03192 610 LYHFASISD-----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684


                 .
gi 30089994  180 N 180
Cdd:PLN03192 685 N 685
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 84-256 3.88e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 3.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   84 ALHYAAMHGRARIARLMLESEYRSdiiNAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERS 163
Cdd:PHA02875   5 ALCDAILFGELDIARRLLDIGINP---NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  164 SCVKILLDHNANID---IQNGFL-LRYAVIKSNHSYCRMFLQRGADTNLGRlEDGQTPLHLSALRDDVLCARMLYNYGAD 239
Cdd:PHA02875  82 KAVEELLDLGKFADdvfYKDGMTpLHLATILKKLDIMKLLIARGADPDIPN-TDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                        170
                 ....*....|....*..
gi 30089994  240 TNTRNYEGQTPLAVSIS 256
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMA 177
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 4-239 5.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 5.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994    4 HHCRRNPELQEELQIQAAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLiGGFT 83
Cdd:PHA02876 135 HYDKINESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL-DDLS 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   84 ALHYAAMHGRARIARLMLESeyRSDI-------INAKSNDGW---------------------TPLHVAAHygRDSFVRL 135
Cdd:PHA02876 214 VLECAVDSKNIDTIKAIIDN--RSNInkndlslLKAIRNEDLetslllydagfsvnsiddcknTPLHHASQ--APSLSRL 289

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  136 ---LLEFKAEVDPLSDKGTTPLQL-AIIRERSSCVKILL----DHNANIDIQNGFLLRYAVIKSNHSYCRMFLQRGADTN 207
Cdd:PHA02876 290 vpkLLERGADVNAKNIKGETPLYLmAKNGYDTENIRTLImlgaDVNAADRLYITPLHQASTLDRNKDIVITLLELGANVN 369

                        250       260       270
                 ....*....|....*....|....*....|..
gi 30089994  208 LGRLEDgQTPLHLSALRDDVLCARMLYNYGAD 239
Cdd:PHA02876 370 ARDYCD-KTPIHYAAVRNNVVIINTLLDYGAD 400
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 95-251 1.84e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.85  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   95 RIARLMLEseyRSDIINAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNA 174
Cdd:PHA02876 159 LIAEMLLE---GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  175 NIDiQNGFLLRYAVIKSNHSYCRMFLQRGADTNlgRLEDGQ-TPLHLSALRDDV--LCARMLyNYGADTNTRNYEGQTPL 251
Cdd:PHA02876 236 NIN-KNDLSLLKAIRNEDLETSLLLYDAGFSVN--SIDDCKnTPLHHASQAPSLsrLVPKLL-ERGADVNAKNIKGETPL 311
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 23-101 7.06e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 7.06e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30089994   23 AAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAMHGRARIARLML 101
Cdd:PTZ00322  91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 26-192 4.78e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   26 DVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAmhGRAR---IARLMLE 102
Cdd:PHA02878 180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN-TPLHISV--GYCKdydILKLLLE 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  103 seyRSDIINAKSN-DGWTPLHVAAHYGRDsfVRLLLEFKAEVDPLSDKGTTPLQLAII-RERSSCVKILLDH-----NAN 175
Cdd:PHA02878 257 ---HGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILISNicllkRIK 331

                        170
                 ....*....|....*....
gi 30089994  176 IDIQN--GFLLRYAVIKSN 192
Cdd:PHA02878 332 PDIKNseGFIDNMDCITSN 350
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-101 5.52e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 5.52e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30089994    47 GWTLLHFSAARGKERCVRVFLEHGADPTVKDlIGGFTALHYAAMHGRARIARLML 101
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 72-172 7.20e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 7.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   72 DPTVKDLIGgfTALHYAAMHGRARIARLMLESEYRSdiiNAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGT 151
Cdd:PTZ00322  75 DPVVAHMLT--VELCQLAASGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK 149

                         90       100
                 ....*....|....*....|.
gi 30089994  152 TPLQLAIIRERSSCVKILLDH 172
Cdd:PTZ00322 150 TPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-170 2.00e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 2.00e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 30089994   117 GWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILL 170
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 86-256 2.03e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   86 HYAAMHGrARIARLMLESEYRSDIINAKSNdgwtpLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSC 165
Cdd:PLN03192 500 HHKELHD-LNVGDLLGDNGGEHDDPNMASN-----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDC 573

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  166 VKILLDHNANI---DIQNGFLLRYAVIKSNHSYCRMFLQrgadtnLGRLEDGQTP---LHLSALRDDVLCARMLYNYGAD 239
Cdd:PLN03192 574 VLVLLKHACNVhirDANGNTALWNAISAKHHKIFRILYH------FASISDPHAAgdlLCTAAKRNDLTAMKELLKQGLN 647

                        170
                 ....*....|....*..
gi 30089994  240 TNTRNYEGQTPLAVSIS 256
Cdd:PLN03192 648 VDSEDHQGATALQVAMA 664
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 127-256 1.36e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  127 YGRDSFVRLLLEFKA-----EVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQNGFLLRYAVIKSNHSY------ 195
Cdd:PHA03100   7 LTKSRIIKVKNIKYIimeddLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvk 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30089994  196 --CRMFLQRGADTNLGRLEdGQTPLH--LSALRDDVLCARMLYNYGADTNTRNYEGQTPLAVSIS 256
Cdd:PHA03100  87 eiVKLLLEYGANVNAPDNN-GITPLLyaISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLE 150
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 106-255 2.72e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  106 RSDIINAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNAN---------- 175
Cdd:PHA02874  24 KGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipcie 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  176 -------------IDIQNGFL---LRYAVIKSNHSYCRMFLQRGADTNLgRLEDGQTPLHLSALRDDVLCARMLYNYGAD 239
Cdd:PHA02874 104 kdmiktildcgidVNIKDAELktfLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                        170
                 ....*....|....*.
gi 30089994  240 TNTRNYEGQTPLAVSI 255
Cdd:PHA02874 183 ANVKDNNGESPLHNAA 198
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 19-176 2.78e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   19 QAAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGAD-PTVKDLIGgfTALHYAAMHGRARIA 97
Cdd:PHA02876 347 QASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADiEALSQKIG--TALHFALCGTNPYMS 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   98 RLMLESeyRSDIINAKSNDGWTPLHVAAHYG-RDSFVRLLLEFKAEVDPLSDKGTTPLQLAIirERSSCVKILLDHNANI 176
Cdd:PHA02876 425 VKTLID--RGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 21-265 2.87e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   21 AVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTV-------KDLIggftalhyaamhgr 93
Cdd:PHA02874  42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpipcieKDMI-------------- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   94 ariaRLMLESEYRSDIINAKSNdgwTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHN 173
Cdd:PHA02874 108 ----KTILDCGIDVNIKDAELK---TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  174 AnidiqngfllrYAVIKSNHsycrmflqrgadtnlgrledGQTPLHLSALRDDVLCARMLYNYGADTNTRNYEGQTPLAV 253
Cdd:PHA02874 181 A-----------YANVKDNN--------------------GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229

                        250
                 ....*....|..
gi 30089994  254 SISISGSSRPCL 265
Cdd:PHA02874 230 AIIHNRSAIELL 241
PHA02946 PHA02946
ankyin-like protein; Provisional
 26-255 3.59e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.82  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   26 DVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAMHGRARIARLMLESEY 105
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHK-TPLYYLSGTDDEVIERINLLVQY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  106 RSDIINAKSNDGWTPLHVAAHYGRDSFVRLL-LEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDhnanidiqngflL 184
Cdd:PHA02946 130 GAKINNSVDEEGCGPLLACTDPSERVFKKIMsIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMK------------L 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30089994  185 RYAVIKSNHsycrmflqrgadtnlgrleDGQTPLHlsalrddVLCARMLYNY--------GADTNTRNYEGQTPLAVSI 255
Cdd:PHA02946 198 GISPSKPDH-------------------DGNTPLH-------IVCSKTVKNVdiinlllpSTDVNKQNKFGDSPLTLLI 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
83-137 7.41e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 7.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30089994    83 TALHYAAMHGRARIARLMLESEYRsdiINAKSNDGWTPLHVAAHYGRDSFVRLLL 137
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-117 1.45e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.41  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  20 AAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALHYAAMHGRARIARL 99
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL-TALLLAAAAGAALIVKL 270

                        90
                ....*....|....*...
gi 30089994 100 MLESEYRSDIINAKSNDG 117
Cdd:COG0666 271 LLLALLLLAAALLDLLTL 288
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 197-254 1.65e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.65e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30089994  197 RMFLQRGADTNlGRLEDGQTPLHLSALRDDVLCARMLYNYGADTNTRNYEGQTPLAVS 254
Cdd:PTZ00322  99 RILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 49-222 2.80e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.09  E-value: 2.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  49 TLLHFSAARGKERCVRVFLE-HGADPTVKDLIGGfTALHYAAMHGRARIARLMLEsEYRSDIINAKSND---GWTPLHVA 124
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGE-TALHVAALYDNLEAAVVLME-AAPELVNEPMTSDlyqGETALHIA 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994 125 AHYGRDSFVRLLLEFKAEV--------------DPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQNGF---LLRYA 187
Cdd:cd22192  97 VVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLgntVLHIL 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 30089994 188 VIKSNHSY-CRMF---LQRGADTNLGRLE-----DGQTPLHLSA 222
Cdd:cd22192 177 VLQPNKTFaCQMYdliLSYDKEDDLQPLDlvpnnQGLTPFKLAA 220
Ank_4 pfam13637
Ankyrin repeats (many copies);
18-67 3.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 3.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 30089994    18 IQAAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFL 67
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
104-157 6.31e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 6.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 30089994   104 EYRSDIINAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLA 157
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 184-271 7.59e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.51  E-value: 7.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  184 LRYAVIKSNHSYCRMFLQRGADTNLGRLEDGQTPLHLSALRDDVLCARMLYNYGADTNTRNYEGQTPLAVsisisgSSRP 263
Cdd:PHA02884  74 LIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIEL------ALMI 147


                 ....*...
gi 30089994  264 CLDFLQEV 271
Cdd:PHA02884 148 CNNFLAFM 155
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-256 1.40e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  110 INAKSNDGWTPLHVAAHYGRD---SFVRLLLEFKAEVDPLSDKGTTPLQLaiirersscvkiLLDHNANIDIqngfllry 186
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHL------------YLYNATTLDV-------- 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30089994  187 aviksnhsyCRMFLQRGADTNLgRLEDGQTPLH--LSALRDDVLCARMLYNYGADTNTRNYEGQTPLAVSIS 256
Cdd:PHA03095 100 ---------IKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLK 161
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-124 3.58e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 3.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 30089994    67 LEHGADPTVKDLIGGFTALHYAAMHGRARIARLMLesEYRSDiINAKSNDGWTPLHVA 124
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL--AYGVD-LNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
184-256 5.51e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 5.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30089994   184 LRYAVIKSNHSYCRMFLQRGADTNLgRLEDGQTPLHLSALRDDVLCARMLYNYgADTNTRNYeGQTPLAVSIS 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAAR 70
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 21-127 8.69e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 8.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994   21 AVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGFTALHYAAMHGRARIARLM 100
Cdd:PHA02875 142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221

                         90       100
                 ....*....|....*....|....*..
gi 30089994  101 LESEYRSDIINAKSNDGWTPLHVAAHY 127
Cdd:PHA02875 222 IKRGADCNIMFMIEGEECTILDMICNM 248
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 116-144 1.52e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 1.52e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 30089994   116 DGWTPLHVAA-HYGRDSFVRLLLEFKAEVD 144
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 116-144 1.54e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 1.54e-04
                          10        20
                  ....*....|....*....|....*....
gi 30089994   116 DGWTPLHVAAHYGRDSFVRLLLEFKAEVD 144
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 16-107 2.79e-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: 41.99  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994    16 LQIQAAVAAGDVhtVRKMLEQGYSPNGRDANGWTLLH-------FSAARGKERC-----VRVFLEHGADPTVKDLI---G 80
Cdd:TIGR00870 179 LNAAACLGSPSI--VALLSEDPADILTADSLGNTLLHllvmeneFKAEYEELSCqmynfALSLLDKLRDSKELEVIlnhQ 256

                          90       100
                  ....*....|....*....|....*..
gi 30089994    81 GFTALHYAAMHGRARIARLMLESEYRS 107
Cdd:TIGR00870 257 GLTPLKLAAKEGRIVLFRLKLAIKYKQ 283
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 116-144 3.09e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 3.09e-04
                           10        20
                   ....*....|....*....|....*....
gi 30089994    116 DGWTPLHVAAHYGRDSFVRLLLEFKAEVD 144
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 166-256 3.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  166 VKILLDHNANIDIQN----GFLLRYAVIKSNHSYCRMFLQRGADTNLGRLEDgQTPLH--LSALRDDVLcaRMLYNYGAD 239
Cdd:PHA02878 150 TKLLLSYGADINMKDrhkgNTALHYATENKDQRLTELLLSYGANVNIPDKTN-NSPLHhaVKHYNKPIV--HILLENGAS 226

                         90
                 ....*....|....*..
gi 30089994  240 TNTRNYEGQTPLAVSIS 256
Cdd:PHA02878 227 TDARDKCGNTPLHISVG 243
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 46-77 3.86e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 3.86e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 30089994    46 NGWTLLHFSAAR-GKERCVRVFLEHGADPTVKD 77
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 120-256 4.30e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  120 PLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLA-----------IIRERSSC------VKI-LLDHNANIDIQNG 181
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkeMIRSINKCsvfytlVAIkDAFNNRNVEIFKI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  182 FLLRYavIKSNHS------------------YCRMFLQRGADTNLGRLEDGQTPLHLSALRDDVLCARMLYNYGADTNTR 243
Cdd:PHA02878 120 ILTNR--YKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIP 197

                        170
                 ....*....|...
gi 30089994  244 NYEGQTPLAVSIS 256
Cdd:PHA02878 198 DKTNNSPLHHAVK 210
Ank_5 pfam13857
Ankyrin repeats (many copies);
39-88 6.37e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 6.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 30089994    39 SPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDlIGGFTALHYA 88
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 21-128 6.51e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.77  E-value: 6.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  21 AVAAGDVHTVRKMLEQG--------------YSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGfTALH 86
Cdd:cd22192  96 AVVNQNLNLVRELIARGadvvspratgtffrPGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN-TVLH 174

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 30089994  87 YAAMHGRARIARLM----LESEYRSDII---NAKSNDGWTPLHVAAHYG 128
Cdd:cd22192 175 ILVLQPNKTFACQMydliLSYDKEDDLQpldLVPNNQGLTPFKLAAKEG 223
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 119-179 6.73e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 6.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30089994  119 TPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGT-TPLQLAIIRERSSCVKILLDHNANIDIQ 179
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQ 133
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 149-180 9.37e-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: 9.37e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 30089994   149 KGTTPLQLAIIRERS-SCVKILLDHNANIDIQN 180
Cdd:pfam00023   1 DGNTPLHLAAGRRGNlEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
202-251 1.69e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 1.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 30089994   202 RGADTNLGRLEdGQTPLHLSALRDDVLCARMLYNYGADTNTRNYEGQTPL 251
Cdd:pfam13857   5 GPIDLNRLDGE-GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 213-244 2.08e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 34.96  E-value: 2.08e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 30089994   213 DGQTPLHLSALR-DDVLCARMLYNYGADTNTRN 244
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-200 3.45e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 3.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 30089994   150 GTTPLQLAIIRERSSCVKILLDHNANIDIQNGF---LLRYAVIKSNHSYCRMFL 200
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNgetALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 149-178 4.11e-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: 34.10  E-value: 4.11e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 30089994    149 KGTTPLQLAIIRERSSCVKILLDHNANIDI 178
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02917 PHA02917
ankyrin-like protein; Provisional
 110-177 4.73e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.06  E-value: 4.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30089994  110 INAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERS-SCVKILLDHNANID 177
Cdd:PHA02917 445 INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNiELLKMLLCHKPTLD 513
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 46-75 6.09e-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: 33.72  E-value: 6.09e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 30089994     46 NGWTLLHFSAARGKERCVRVFLEHGADPTV 75
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 117-183 7.70e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 37.58  E-value: 7.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30089994  117 GWTPLHVA------AHYGRDSFVrLLLEFKAEVDPLSDKGTTPLQLAIIRERSS-----CVKILLDHNANIDIQNGFL 183
Cdd:PHA02716 497 GMTPLHVSiishtnANIVMDSFV-YLLSIQYNINIPTKNGVTPLMLTMRNNRLSghqwyIVKNILDKRPNVDIVIIFL 573
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 81-103 8.10e-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: 33.33  E-value: 8.10e-03
                           10        20
                   ....*....|....*....|...
gi 30089994     81 GFTALHYAAMHGRARIARLMLES 103
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDK 24
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 219-254 8.79e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.57  E-value: 8.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 30089994  219 HLSALRDDVlCARMLYNYGADTNTRNYEGQTPLAVS 254
Cdd:PTZ00322  88 QLAASGDAV-GARILLTGGADPNCRDYDGRTPLHIA 122
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 196-254 8.91e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 36.01  E-value: 8.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089994  196 CRMFLQRGADTNLGRLEDGQTPLHLSALRDDVLCARMLYNY-GADTNTRNYEGQTPLAVS 254
Cdd:PHA02736  74 LKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVA 133
 
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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