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Conserved domains on  [gi|1034645565|ref|XP_016865167|]
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ankyrin repeat family A protein 2 isoform X3 [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];
8-152 5.00e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 5.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   8 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 87
Cdd:COG0666   107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034645565  88 GTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLLQNIKE 152
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-152 5.00e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 5.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   8 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 87
Cdd:COG0666   107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034645565  88 GTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLLQNIKE 152
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
25-115 1.78e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  25 LMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCgVDVNEYDwNGGTPLLYAVHGNHVKCVK 104
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1034645565 105 MLLESGADPTI 115
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 14-129 2.10e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.70  E-value: 2.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPLMWAAAH--GQIAVVEFLLQNGADPQLLGKGRESALSLA--CSKGYTDIVKMLLDCGVDVN-----EY- 83
Cdd:PHA03100   99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINaknrvNYl 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034645565  84 ----------DWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVA 129
Cdd:PHA03100  179 lsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 20-47 9.30e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 9.30e-06
                           10        20
                   ....*....|....*....|....*...
gi 1034645565   20 EGFTPLMWAAAHGQIAVVEFLLQNGADP 47
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 20-91 1.25e-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: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  20 EGFTPLMWAAAHGQIAVVEFLLQNGADPQ---------LLGKGR-----ESALSLACSKGYTDIVKMLLDCGVDVNEYDW 85
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                  ....*.
gi 1034645565  86 NGGTPL 91
Cdd:cd22192   168 LGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 7-112 2.34e-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: 40.06  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   7 RIEQENV---INHTDEEGFTPLMWAAAHGQ-IAVVEFLLQNGADPQLlGKgresALSLACSKGYTDIVKMLL-------- 74
Cdd:TIGR00870  35 RDLEEPKklnINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV-GD----TLLHAISLEYVDAVEAILlhllaafr 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034645565  75 --DCGVDVNEYDWN----GGTPLLYAVHGNHVKCVKMLLESGAD 112
Cdd:TIGR00870 110 ksGPLELANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-152 5.00e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 5.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   8 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 87
Cdd:COG0666   107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034645565  88 GTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLLQNIKE 152
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-132 1.36e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 1.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   8 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 87
Cdd:COG0666    74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034645565  88 GTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGY 132
Cdd:COG0666   154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-152 5.12e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 5.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLY 93
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034645565  94 AVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLLQNIKE 152
Cdd:COG0666   226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
25-115 1.78e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  25 LMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCgVDVNEYDwNGGTPLLYAVHGNHVKCVK 104
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1034645565 105 MLLESGADPTI 115
Cdd:pfam12796  79 LLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-132 3.27e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 3.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  12 NVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPL 91
Cdd:COG0666    45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1034645565  92 LYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGY 132
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 14-129 2.10e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.70  E-value: 2.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPLMWAAAH--GQIAVVEFLLQNGADPQLLGKGRESALSLA--CSKGYTDIVKMLLDCGVDVN-----EY- 83
Cdd:PHA03100   99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINaknrvNYl 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034645565  84 ----------DWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVA 129
Cdd:PHA03100  179 lsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-84 1.39e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 1.39e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034645565   8 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNgADPQLLGKGReSALSLACSKGYTDIVKMLLDCGVDVNEYD 84
Cdd:pfam12796  17 LENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
58-135 1.20e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 1.20e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034645565  58 LSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGAdpTIETDSGYNSMDLAVALGYRSV 135
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEI 76
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 12-128 1.65e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  12 NVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKML------------------ 73
Cdd:PHA02874   26 NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekd 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  74 -----LDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAV 128
Cdd:PHA02874  106 miktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-147 5.37e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 5.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  23 TPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYT-----DIVKMLLDCGVDVNEYDWNGGTPLLYAV-- 95
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034645565  96 HGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYrsvqqvIESHLLKLL 147
Cdd:PHA03100  117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNK------IDLKILKLL 162
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 19-113 2.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  19 EEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGN 98
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90
                  ....*....|....*
gi 1034645565  99 HVKCVKMLLESGADP 113
Cdd:PHA02875  180 DIAICKMLLDSGANI 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 70-142 7.54e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 7.54e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034645565  70 VKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESH 142
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-135 7.62e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 7.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   1 MLYLATRIEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDV 80
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034645565  81 NEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSV 135
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
Ank_4 pfam13637
Ankyrin repeats (many copies);
54-107 2.75e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 2.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034645565  54 RESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLL 107
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 2-117 4.91e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 4.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   2 LYLATRIEQENV------------INHTDEegFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDI 69
Cdd:PHA02875  106 LHLATILKKLDImklliargadpdIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034645565  70 VKMLLDCGVDVNEYDWNGGTPLL-YAVHGNHVKCVKMLLESGADPTIET 117
Cdd:PHA02875  184 CKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-135 1.02e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLY 93
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1034645565  94 AVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVaLGYRSV 135
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSA 237
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 14-81 1.49e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.06  E-value: 1.49e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034645565  14 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVN 81
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 15-131 1.62e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  15 NHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDW-NGGTPLLY 93
Cdd:PHA02875   29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHL 108

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034645565  94 AVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALG 131
Cdd:PHA02875  109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 14-117 1.74e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEE-GFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLL 92
Cdd:PHA02878  160 INMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          90       100
                  ....*....|....*....|....*.
gi 1034645565  93 YAV-HGNHVKCVKMLLESGADPTIET 117
Cdd:PHA02878  240 ISVgYCKDYDILKLLLEHGVDVNAKS 265
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-140 2.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLG---------------------KGRESA--LSLACSKGYTDIV 70
Cdd:PHA02874   61 INHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPipciekdmiktildcgidvniKDAELKtfLHYAIKKGDLESI 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034645565  71 KMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALG-YRSVQQVIE 140
Cdd:PHA02874  141 KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGdYACIKLLID 211
PHA03095 PHA03095
ankyrin-like protein; Provisional
 14-125 3.45e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPL---MWAAAHGQIAVVEFLLQNGADPQLLGKGRESAL-SLACSKGYTDIVKMLLDCGVDVNEYDWNGGT 89
Cdd:PHA03095   40 VNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034645565  90 PL-LYAVHGN-HVKCVKMLLESGADPTIETDSGYNSMD 125
Cdd:PHA03095  120 PLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA 157
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 11-118 6.70e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 6.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  11 ENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLL-GKGReSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGT 89
Cdd:PLN03192  515 DNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGdSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNT 593

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034645565  90 PLLYAVHGNHVKCVKML--LESGADPTIETD 118
Cdd:PLN03192  594 ALWNAISAKHHKIFRILyhFASISDPHAAGD 624
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 15-87 1.65e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.65e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034645565  15 NHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 87
Cdd:PTZ00322  109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
23-74 1.38e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034645565  23 TPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLL 74
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-117 1.59e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  37 VEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGadPTIE 116
Cdd:PHA03100  175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIK 252


                  .
gi 1034645565 117 T 117
Cdd:PHA03100  253 T 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-94 2.09e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 2.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034645565  40 LLQNG-ADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYA 94
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
14-61 6.52e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 6.52e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1034645565  14 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLA 61
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 8-127 8.63e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 8.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   8 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGadpqllgkgreSALSLACSKGYT----------DIVKMLLDcG 77
Cdd:PHA02874  177 LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-----------NHIMNKCKNGFTplhnaiihnrSAIELLIN-N 244

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034645565  78 VDVNEYDWNGGTPLLYAVHGN-HVKCVKMLLESGADPTIETDSGYNSMDLA 127
Cdd:PHA02874  245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 33-122 2.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.89  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  33 QIAVVEFLLQNGADPQLLG----------KGRESAlslacSKGYTDIVKMLLDCGVDVNEYDWNGGTPL---LYAVHGNH 99
Cdd:PHA02989   49 KIKIVKLLIDNGADVNYKGyietplcavlRNREIT-----SNKIKKIVKLLLKFGADINLKTFNGVSPIvcfIYNSNINN 123

                          90       100
                  ....*....|....*....|....
gi 1034645565 100 VKCVKMLLESGAD-PTIETDSGYN 122
Cdd:PHA02989  124 CDMLRFLLSKGINvNDVKNSRGYN 147
Ank_5 pfam13857
Ankyrin repeats (many copies);
73-127 4.93e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 4.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034645565  73 LLDCG-VDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLA 127
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 36-147 7.06e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  36 VVEFLLQNGADpqLLGKGRESALSLaCS--------KGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHG---NHVKCVK 104
Cdd:PHA02798   53 IVKLFINLGAN--VNGLDNEYSTPL-CTilsnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034645565 105 MLLESGADPTIETDSGYNSMDLAVALGYRsvqqvIESHLLKLL 147
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHH-----IDIEIIKLL 167
PHA03095 PHA03095
ankyrin-like protein; Provisional
 14-74 8.66e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 8.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034645565  14 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLL 74
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 20-47 9.30e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 9.30e-06
                           10        20
                   ....*....|....*....|....*...
gi 1034645565   20 EGFTPLMWAAAHGQIAVVEFLLQNGADP 47
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-91 1.00e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   8 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVDVNEYDWNG 87
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                  ....
gi 1034645565  88 GTPL 91
Cdd:COG0666   286 LTLL 289
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 36-140 1.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.27  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  36 VVEFLLQNGADPQLLGKGRE-SALS--LACSKGYT-DIVKMLLDCGVDVNEYDWNGGTPL-LYAVHGN-HVKCVKMLLES 109
Cdd:PHA02859   68 ILKFLIENGADVNFKTRDNNlSALHhyLSFNKNVEpEILKILIDSGSSITEEDEDGKNLLhMYMCNFNvRINVIKLLIDS 147

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034645565 110 GADPtIETDSGYNSMdLAVALGYRSVQQVIE 140
Cdd:PHA02859  148 GVSF-LNKDFDNNNI-LYSYILFHSDKKIFD 176
PHA02792 PHA02792
ankyrin-like protein; Provisional
 36-150 1.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 43.78  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  36 VVEFLLQNGAD---------------PQLLGKGRESALSLACSKGYTDivkmlldcgvDVNEYDWNGGTPLLYAVHGNHV 100
Cdd:PHA02792  354 VVEYILKNGNVvvedddniinimplfPTLSIHESDVLSILKLCKPYID----------DINKIDKHGRSILYYCIESHSV 423

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034645565 101 KCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHlLKLLQNI 150
Cdd:PHA02792  424 SLVEWLIDNGADINITTKYGSTCIGICVILAHACIPEIAELY-IKILEII 472
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-140 1.94e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPLMWAAAHG-QIAVVEFLLQNGADPQLLGKGRESALSLACS-KGYTDIVKMLLDCGVDVNEYDWNGGTPL 91
Cdd:PHA02876  300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPI 379

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034645565  92 LYAVHGNHVKCVKMLLESGADptIETDSGYNSMDLAVAL----GYRSVQQVIE 140
Cdd:PHA02876  380 HYAAVRNNVVIINTLLDYGAD--IEALSQKIGTALHFALcgtnPYMSVKTLID 430
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 20-47 2.30e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.30e-05
                          10        20
                  ....*....|....*....|....*....
gi 1034645565  20 EGFTPLMWAAAH-GQIAVVEFLLQNGADP 47
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADV 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 20-47 2.59e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 2.59e-05
                          10        20
                  ....*....|....*....|....*...
gi 1034645565  20 EGFTPLMWAAAHGQIAVVEFLLQNGADP 47
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 14-139 3.27e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPlMW---AAAHGQIAVVEFLLQNGADPQLLGkgreSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTP 90
Cdd:PLN03192  584 VHIRDANGNTA-LWnaiSAKHHKIFRILYHFASISDPHAAG----DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034645565  91 LLYAVHGNHVKCVKMLLESGADPT-IETDSGYNSMDLAVALGYRSVQQVI 139
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRELLQKRELGHSI 708
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 23-139 3.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  23 TPLMWAAAHGQIAVVEFLLQNG--ADPQLLGKGReSALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHV 100
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034645565 101 KCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVI 139
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-132 4.98e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVK---------------------- 71
Cdd:PHA02876  171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairn 250

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034645565  72 -------MLLDCGVDVNEYDWNGGTPLLYAVHGNHV-KCVKMLLESGADPTIETDSGYNSMDLAVALGY 132
Cdd:PHA02876  251 edletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGY 319
PHA02791 PHA02791
ankyrin-like protein; Provisional
 18-108 5.27e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.95  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  18 DEEGFTPLMWAAAHGQIAVVEFLLQNGADPQLLGKgrESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHG 97
Cdd:PHA02791   27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                          90
                  ....*....|.
gi 1034645565  98 NHVKCVKMLLE 108
Cdd:PHA02791  105 GNMQTVKLFVK 115
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 69-128 7.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 7.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  69 IVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAV 128
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAV 219
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 86-118 8.35e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 8.35e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034645565  86 NGGTPLLYAV-HGNHVKCVKMLLESGADPTIETD 118
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 34-125 1.19e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.97  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  34 IAVVEFLLQNGADPQLLGKGRESALSLACSKGYT---DIVKMLLDCGVDVNEYDWNGGTPL-LYAVHGNHV--KCVKMLL 107
Cdd:PHA02798   89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLqVYLQSNHHIdiEIIKLLL 168

                          90
                  ....*....|....*....
gi 1034645565 108 ESGAD-PTIETDSGYNSMD 125
Cdd:PHA02798  169 EKGVDiNTHNNKEKYDTLH 187
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 20-91 1.25e-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: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  20 EGFTPLMWAAAHGQIAVVEFLLQNGADPQ---------LLGKGR-----ESALSLACSKGYTDIVKMLLDCGVDVNEYDW 85
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                  ....*.
gi 1034645565  86 NGGTPL 91
Cdd:cd22192   168 LGNTVL 173
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 36-147 1.81e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  36 VVEFLLQNGADPQLLGKGR-ESALSLACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGAdpT 114
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA--S 226

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034645565 115 IETDSGYNSMDLAVALGYrsvqqVIESHLLKLL 147
Cdd:PHA02878  227 TDARDKCGNTPLHISVGY-----CKDYDILKLL 254
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 7-112 2.34e-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: 40.06  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   7 RIEQENV---INHTDEEGFTPLMWAAAHGQ-IAVVEFLLQNGADPQLlGKgresALSLACSKGYTDIVKMLL-------- 74
Cdd:TIGR00870  35 RDLEEPKklnINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV-GD----TLLHAISLEYVDAVEAILlhllaafr 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034645565  75 --DCGVDVNEYDWN----GGTPLLYAVHGNHVKCVKMLLESGAD 112
Cdd:TIGR00870 110 ksGPLELANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAS 153
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 23-112 2.53e-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: 40.00  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  23 TPLMWAAAHGQI-AVVEFLLQNGADPQLLGKGRESALSLACSKGYTDIVKMLLDCGVD-VNE------YDwnGGTPLLYA 94
Cdd:cd22192    19 SPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEpmtsdlYQ--GETALHIA 96

                          90
                  ....*....|....*...
gi 1034645565  95 VHGNHVKCVKMLLESGAD 112
Cdd:cd22192    97 VVNQNLNLVRELIARGAD 114
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 86-115 2.66e-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: 36.41  E-value: 2.66e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034645565   86 NGGTPLLYAVHGNHVKCVKMLLESGADPTI 115
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
14-41 3.05e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 3.05e-04
                          10        20
                  ....*....|....*....|....*...
gi 1034645565  14 INHTDEEGFTPLMWAAAHGQIAVVEFLL 41
Cdd:pfam13637  27 INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 8-81 4.90e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.05  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565   8 IEQENVINHTDEEGFTPLMWAAAHGQIAVVEFLL---QNGADPQLLGKGRESALSLACSKGYT---DIVKMLLDCGVDVN 81
Cdd:PHA02798   96 IENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDIN 175
PHA03095 PHA03095
ankyrin-like protein; Provisional
 14-129 5.46e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPLmwaAA----HG-QIAVVEFLLQNGADPQLLGKGRESAL-SLACS-KGYTDIVKMLLD----------- 75
Cdd:PHA03095  145 VNALDLYGMTPL---AVllksRNaNVELLRLLIDAGADVYAVDDRFRSLLhHHLQSfKPRARIVRELIRagcdpaatdml 221

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034645565  76 -------------C-----------GVDVNEYDWNGGTPLLYA-VHGNHVKCVKmLLESGADPTIETDSGYNSMDLAVA 129
Cdd:PHA03095  222 gntplhsmatgssCkrslvlplliaGISINARNRYGQTPLHYAaVFNNPRACRR-LIALGADINAVSSDGNTPLSLMVR 299
PHA02798 PHA02798
ankyrin-like protein; Provisional
 18-120 7.50e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  18 DEEGFTPL---MWAAAHGQIAVVEFLLQNGADPQLLGKgRESALSLACSKGYT------DIVKMLLDCG----------- 77
Cdd:PHA02798  142 DKDGFTMLqvyLQSNHHIDIEIIKLLLEKGVDINTHNN-KEKYDTLHCYFKYNidridaDILKLFVDNGfiinkenkshk 220

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034645565  78 ----------------------------VDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSG 120
Cdd:PHA02798  221 kkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELG 291
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 37-112 8.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.51  E-value: 8.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034645565  37 VEFLLQNGADPQLLGKGRESALSLACSKG-YTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVkcVKMLLESGAD 112
Cdd:PHA02876  425 VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAE 499
Ank_4 pfam13637
Ankyrin repeats (many copies);
87-135 9.10e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 9.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1034645565  87 GGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSV 135
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEV 49
PHA02795 PHA02795
ankyrin-like protein; Provisional
 68-147 1.04e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 38.05  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  68 DIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAVALGYRSVQQVIESHLLKLL 147
Cdd:PHA02795  202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARRETHLKILEIL 281
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 36-139 1.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 37.66  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  36 VVEFLLQNGADPQLLGKGRESA----LSLACSKGYTDIVKMLLDCGVDVNEY-DWNGGTPLLYAVHGNHVKCVKMLLESG 110
Cdd:PHA02884   48 IIDAILKLGADPEAPFPLSENSktnpLIYAIDCDNDDAAKLLIRYGADVNRYaEEAKITPLYISVLHGCLKCLEILLSYG 127

                          90       100
                  ....*....|....*....|....*....
gi 1034645565 111 ADPTIETDSGYNSMDLAVALGYRSVQQVI 139
Cdd:PHA02884  128 ADINIQTNDMVTPIELALMICNNFLAFMI 156
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 55-82 1.52e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|....*...
gi 1034645565  55 ESALSLACSKGYTDIVKMLLDCGVDVNE 82
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 14-121 1.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.55  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  14 INHTDEEGFTPLMWAAAH-GQIAVVEFLLQNGADPQLLGKGRE-SALSLACSKgyTDIVKMLLDCGVDVNEYDWNGGTPL 91
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPL 304

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034645565  92 LYAVHGNH-VKCVKML-----LESGADPTIETDSGY 121
Cdd:PHA02878  305 SSAVKQYLcINIGRILisnicLLKRIKPDIKNSEGF 340
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-126 2.53e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 36.93  E-value: 2.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034645565  60 LACSKGYTDIVKMLLDCGVDVNEYDWNGGTPLLYAVHGNHVKC---VKMLLESGADPTIETDSGYNSMDL 126
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHL 89
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 86-115 3.97e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.38  E-value: 3.97e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034645565  86 NGGTPLLYAVHGNHVKCVKMLLESGADPTI 115
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 56-82 5.01e-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: 32.94  E-value: 5.01e-03
                           10        20
                   ....*....|....*....|....*..
gi 1034645565   56 SALSLACSKGYTDIVKMLLDCGVDVNE 82
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02917 PHA02917
ankyrin-like protein; Provisional
 79-128 5.21e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 36.13  E-value: 5.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034645565  79 DVNEYDWNGGTPLLYAVHGNHVKCVKMLLESGADPTIETDSGYNSMDLAV 128
Cdd:PHA02917  444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAI 493
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 55-84 6.82e-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: 32.65  E-value: 6.82e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034645565  55 ESALSLACSK-GYTDIVKMLLDCGVDVNEYD 84
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
 
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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