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Conserved domains on  [gi|300798632|ref|NP_001178567|]
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ankyrin repeat domain-containing protein 22 [Rattus norvegicus]

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];
8-189 1.03e-28

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632   8 PICQAAYQNDLGQVwRWVKESNHYVDIQDGfNGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKKRftf 87
Cdd:COG0666   90 LLHAAARNGDLEIV-KLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG--- 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  88 fdylliillmpvlligyflmvsktkqNEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKH 167
Cdd:COG0666  165 --------------------------NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                        170       180
                 ....*....|....*....|..
gi 300798632 168 GESSLDIAQRLKFNQIALMLKK 189
Cdd:COG0666  219 GKTALDLAAENGNLEIVKLLLE 240
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-189 1.03e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632   8 PICQAAYQNDLGQVwRWVKESNHYVDIQDGfNGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKKRftf 87
Cdd:COG0666   90 LLHAAARNGDLEIV-KLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG--- 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  88 fdylliillmpvlligyflmvsktkqNEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKH 167
Cdd:COG0666  165 --------------------------NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                        170       180
                 ....*....|....*....|..
gi 300798632 168 GESSLDIAQRLKFNQIALMLKK 189
Cdd:COG0666  219 GKTALDLAAENGNLEIVKLLLE 240
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 39-175 6.75e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 6.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  39 NGDTPLICA--CRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKkrftffdYLLIILLMPVLLIGYFLMV-SKTKqne 115
Cdd:PHA03100 105 NGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLE-------SNKIDLKILKLLIDKGVDInAKNR--- 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632 116 alVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESSLDIA 175
Cdd:PHA03100 175 --VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
44-165 1.91e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632   44 LICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKkrftffdylliillmpvlligyflmvsktKQNEALVRMLLN 123
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAK-----------------------------NGHLEIVKLLLE 51

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 300798632  124 aGVEVNATDcYGYTALHYACQMKNQTLIPLLLAARADPTIKN 165
Cdd:pfam12796  52 -HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 39-68 3.89e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.89e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 300798632    39 NGDTPLICACRRGHLRIVSFLLRRNADVNL 68
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 36-175 2.01e-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: 41.15  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  36 DGFNGDTPLICACRRGHLRIVSFLLRRNADVnlknLKER---TCLHYAVKKRFTFFDYLLIIllmpvlligyflmvSKTK 112
Cdd:cd22192   85 DLYQGETALHIAVVNQNLNLVRELIARGADV----VSPRatgTFFRPGPKNLIYYGEHPLSF--------------AACV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632 113 QNEALVRMLLNAGVEVNATDCYGYTALH---------YACQM--------KNQTLIPLllaaradPTIKNKHGESSLDIA 175
Cdd:cd22192  147 GNEEIVRLLIEHGADIRAQDSLGNTVLHilvlqpnktFACQMydlilsydKEDDLQPL-------DLVPNNQGLTPFKLA 219
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-189 1.03e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632   8 PICQAAYQNDLGQVwRWVKESNHYVDIQDGfNGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKKRftf 87
Cdd:COG0666   90 LLHAAARNGDLEIV-KLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG--- 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  88 fdylliillmpvlligyflmvsktkqNEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKH 167
Cdd:COG0666  165 --------------------------NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                        170       180
                 ....*....|....*....|..
gi 300798632 168 GESSLDIAQRLKFNQIALMLKK 189
Cdd:COG0666  219 GKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-187 2.18e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.87  E-value: 2.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  12 AAYQNDLGQVWRWVKESNHYVDIQDgFNGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKKRftffdyl 91
Cdd:COG0666   60 AAALAGDLLVALLLLAAGADINAKD-DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG------- 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  92 liillmpvlligyflmvsktkqNEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESS 171
Cdd:COG0666  132 ----------------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189

                        170
                 ....*....|....*.
gi 300798632 172 LDIAQRLKFNQIALML 187
Cdd:COG0666  190 LHLAAENGHLEIVKLL 205
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 39-175 6.75e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 6.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  39 NGDTPLICA--CRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKkrftffdYLLIILLMPVLLIGYFLMV-SKTKqne 115
Cdd:PHA03100 105 NGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLE-------SNKIDLKILKLLIDKGVDInAKNR--- 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632 116 alVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESSLDIA 175
Cdd:PHA03100 175 --VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
44-165 1.91e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632   44 LICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKkrftffdylliillmpvlligyflmvsktKQNEALVRMLLN 123
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAK-----------------------------NGHLEIVKLLLE 51

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 300798632  124 aGVEVNATDcYGYTALHYACQMKNQTLIPLLLAARADPTIKN 165
Cdd:pfam12796  52 -HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-191 3.95e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  14 YQNDLGQVWRWVKESNHYVDIQDGfNGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKKRFTFFDYLLI 93
Cdd:PHA02874  10 YSGDIEAIEKIIKNKGNCINISVD-ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  94 I-----LLMPVLLIgyflmvsktkqNEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHG 168
Cdd:PHA02874  89 DngvdtSILPIPCI-----------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG 157

                        170       180
                 ....*....|....*....|....
gi 300798632 169 ESSLDIAQRLKFNQ-IALMLKKGS 191
Cdd:PHA02874 158 CYPIHIAIKHNFFDiIKLLLEKGA 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-177 4.83e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 4.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  32 VDIQDgFNGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKkrftFFDYLLIILL-------MPVLLIGY 104
Cdd:PHA02874 150 VNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE----YGDYACIKLLidhgnhiMNKCKNGF 224

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798632 105 FLMVSKTKQNEALVRMLLNaGVEVNATDCYGYTALHYACQMK-NQTLIPLLLAARADPTIKNKHGESSLDIAQR 177
Cdd:PHA02874 225 TPLHNAIIHNRSAIELLIN-NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-169 7.34e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.58  E-value: 7.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  32 VDIQDGfNGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKKRftffdylliillmpvlligyflmvskt 111
Cdd:COG0666  179 VNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG--------------------------- 230

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 300798632 112 kqNEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGE 169
Cdd:COG0666  231 --NLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-172 1.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.61  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  42 TPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKKRftFFDYLLIILLMPVLLIGYFLMVSKTKQNEALVRML 121
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK--NIDTIKAIIDNRSNINKNDLSLLKAIRNEDLETSL 257

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300798632 122 L--NAGVEVNATDCYGYTALHYACQMKNQT-LIPLLLAARADPTIKNKHGESSL 172
Cdd:PHA02876 258 LlyDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPL 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
9-132 1.72e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632    9 ICQAAYQNDLGQVwRWVKESNHYVDIQDGfNGDTPLICACRRGHLRIVSFLLrRNADVNLKNlKERTCLHYAVKKRftff 88
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSG---- 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 300798632   89 dylliillmpvlligyflmvsktkqNEALVRMLLNAGVEVNATD 132
Cdd:pfam12796  73 -------------------------HLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 39-174 1.18e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  39 NGDTPLIC-ACRRGHLRIVSFLLRRNADVNLKNLKERTCLHyavkkrftffdylliillmpVLLIGYFLmvsktkqNEAL 117
Cdd:PHA03095  82 CGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLH--------------------VYLSGFNI-------NPKV 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798632 118 VRMLLNAGVEVNATDCYGYTALHyaCQMKNQT----LIPLLLAARADPTIKNKHGESSLDI 174
Cdd:PHA03095 135 IRLLLRKGADVNALDLYGMTPLA--VLLKSRNanveLLRLLIDAGADVYAVDDRFRSLLHH 193
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 118-187 1.41e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 1.41e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632 118 VRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESSLDIAQRLKFNQIALML 187
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-175 2.45e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300798632  121 LLNAG-VEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESSLDIA 175
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-175 6.14e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 6.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  37 GFNGDTPL-ICAC-RRGHLRIVSFLLRRNADVNLKNLKERTCLH-----------------------YAVKKRF-TFFDY 90
Cdd:PHA03095 114 DKVGRTPLhVYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksrnanvellrllidagadvYAVDDRFrSLLHH 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  91 L-------------LIILLMPVLLIGYF------LMVSKTKQNEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLI 151
Cdd:PHA03095 194 HlqsfkprarivreLIRAGCDPAATDMLgntplhSMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRAC 273

                        170       180
                 ....*....|....*....|....
gi 300798632 152 PLLLAARADPTIKNKHGESSLDIA 175
Cdd:PHA03095 274 RRLIALGADINAVSSDGNTPLSLM 297
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-190 5.29e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.41  E-value: 5.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  89 DYLLIILLMPVLLIGYFLMVSKTKQNEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHG 168
Cdd:COG0666   41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                         90       100
                 ....*....|....*....|...
gi 300798632 169 ESSLDIAQRLKFNQIA-LMLKKG 190
Cdd:COG0666  121 ETPLHLAAYNGNLEIVkLLLEAG 143
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-191 6.92e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 6.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  28 SNHYVDIQDGFNGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVkkrftffdylliillmpvlligyflM 107
Cdd:PHA02875  90 LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV-------------------------M 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632 108 VSKTKqneaLVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESSL--DIAQRLKFNQIAL 185
Cdd:PHA02875 145 MGDIK----GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAlcYAIENNKIDIVRL 220


                 ....*.
gi 300798632 186 MLKKGS 191
Cdd:PHA02875 221 FIKRGA 226
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 41-160 1.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  41 DTPLICACRRGHL-RIVSFLLRRNADVNLKNLKERTCLHYAVKKRFTFFDYLLIILL------MPVLLIGYFLMVSKTKQ 113
Cdd:PHA02876 274 NTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLgadvnaADRLYITPLHQASTLDR 353

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 300798632 114 NEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARAD 160
Cdd:PHA02876 354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 39-94 1.33e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 1.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 300798632  39 NGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKKRFTFFDYLLII 94
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
PHA03095 PHA03095
ankyrin-like protein; Provisional
 45-190 1.65e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  45 ICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYavkkrftffdylliillmpvlligyfLMVSKTKQNEALVRMLLNA 124
Cdd:PHA03095  19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL--------------------------YLHYSSEKVKDIVRLLLEA 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300798632 125 GVEVNATDCYGYTALHyaCQMKNQTLIP---LLLAARADPTIKNKHGESSLDI---AQRLKFNQIALMLKKG 190
Cdd:PHA03095  73 GADVNAPERCGFTPLH--LYLYNATTLDvikLLIKAGADVNAKDKVGRTPLHVylsGFNINPKVIRLLLRKG 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
114-187 1.66e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.66e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798632  114 NEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLaARADPTIKNkHGESSLDIAQRLKFNQIALML 187
Cdd:pfam12796   9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVKLL 80
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 39-70 1.74e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 1.74e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 300798632   39 NGDTPLICAC-RRGHLRIVSFLLRRNADVNLKN 70
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-190 4.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  55 IVSFLLRRNADVNLKNLKERTCLHYAVKKRFTFfdylliillmpvlligyflmvsktKQNEALVRMLLNAGVEVNATDCY 134
Cdd:PHA03100  50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYNL------------------------TDVKEIVKLLLEYGANVNAPDNN 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798632 135 GYTALHYACQMK--NQTLIPLLLAARADPTIKNKHGESSLDIAQR---LKFNQIALMLKKG 190
Cdd:PHA03100 106 GITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkIDLKILKLLIDKG 166
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 106-175 4.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 4.34e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798632 106 LMVSKTKQNEALV-RMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESSLDIA 175
Cdd:PHA02876 148 LIKERIQQDELLIaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECA 218
Ank_4 pfam13637
Ankyrin repeats (many copies);
5-60 1.99e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300798632    5 YSEPICQAAYQNDLgQVWRWVKESNHYVDIQDGfNGDTPLICACRRGHLRIVSFLL 60
Cdd:pfam13637   1 ELTALHAAAASGHL-ELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 39-68 3.89e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.89e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 300798632    39 NGDTPLICACRRGHLRIVSFLLRRNADVNL 68
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
40-92 7.06e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 7.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300798632   40 GDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKK-RFTFFDYLL 92
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNgNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 33-171 8.78e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 8.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  33 DIQDGfNGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAV-KKRFTFFDYLLIILLMPVLLIGYFLMVSKT 111
Cdd:PLN03192 552 DIGDS-KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIsAKHHKIFRILYHFASISDPHAAGDLLCTAA 630

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798632 112 KQNE-ALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESS 171
Cdd:PLN03192 631 KRNDlTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFS 691
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 36-175 2.01e-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: 41.15  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  36 DGFNGDTPLICACRRGHLRIVSFLLRRNADVnlknLKER---TCLHYAVKKRFTFFDYLLIIllmpvlligyflmvSKTK 112
Cdd:cd22192   85 DLYQGETALHIAVVNQNLNLVRELIARGADV----VSPRatgTFFRPGPKNLIYYGEHPLSF--------------AACV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632 113 QNEALVRMLLNAGVEVNATDCYGYTALH---------YACQM--------KNQTLIPLllaaradPTIKNKHGESSLDIA 175
Cdd:cd22192  147 GNEEIVRLLIEHGADIRAQDSLGNTVLHilvlqpnktFACQMydlilsydKEDDLQPL-------DLVPNNQGLTPFKLA 219
Ank_4 pfam13637
Ankyrin repeats (many copies);
114-155 2.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 2.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 300798632  114 NEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLL 155
Cdd:pfam13637  13 HLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 41-181 3.08e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  41 DTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVkkrftffdylliillmpvlliGYFLmvsktkqNEALVRM 120
Cdd:PHA02878 202 NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV---------------------GYCK-------DYDILKL 253

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798632 121 LLNAGVEVNA-TDCYGYTALHYAcqMKNQTLIPLLLAARADPTIKNKHGESSLDIA--QRLKFN 181
Cdd:PHA02878 254 LLEHGVDVNAkSYILGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCIN 315
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 39-67 7.92e-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: 35.70  E-value: 7.92e-04
                          10        20
                  ....*....|....*....|....*....
gi 300798632   39 NGDTPLICACRRGHLRIVSFLLRRNADVN 67
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
32-80 1.15e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 1.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 300798632   32 VDIQDGFnGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYA 80
Cdd:pfam13857   9 LNRLDGE-GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 114-172 1.24e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 1.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 300798632 114 NEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESSL 172
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPL 109
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 134-166 1.40e-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: 1.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 300798632  134 YGYTALHYACQMKNQT-LIPLLLAARADPTIKNK 166
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-175 1.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.51  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  55 IVSFLLRRNADVNLKNLKERTCLHYAVKKRF-----TFFDYLLIILLMPvLLIGYFLMVSKTKQNEAL-VRMLLNAGVEV 128
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNvviinTLLDYGADIEALS-QKIGTALHFALCGTNPYMsVKTLIDRGANV 435

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 300798632 129 NATDCYGYTALHYACQMKNQ-TLIPLLLAARADPTIKNKHGESSLDIA 175
Cdd:PHA02876 436 NSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 38-187 2.24e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.05  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  38 FNGDTPLICACRRGHLRIVSFLLRRNADVNLKNLKERTCLHYAVKKRftffdylLIILLMPVLLIGYF------------ 105
Cdd:PHA02875  33 YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG-------DVKAVEELLDLGKFaddvfykdgmtp 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632 106 LMVSKTKQNEALVRMLLNAGVEVNATDCYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESSLDIAQRLKFNQIAL 185
Cdd:PHA02875 106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185


                 ..
gi 300798632 186 ML 187
Cdd:PHA02875 186 ML 187
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 117-191 2.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.94  E-value: 2.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798632 117 LVRMLLNAGVEVNATDCY-GYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESSLDIAQRLKFNQIA-LMLKKGS 191
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVhILLENGA 225
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-191 4.38e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.17  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632  54 RIVSFLLRRNADVNLKNL-KERTCLHYAVkkrftffdylliillmpvlligyflmvskTKQNEALVRMLLNAGVEVNATD 132
Cdd:PHA02878 148 EITKLLLSYGADINMKDRhKGNTALHYAT-----------------------------ENKDQRLTELLLSYGANVNIPD 198

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798632 133 CYGYTALHYACQMKNQTLIPLLLAARADPTIKNKHGESSLDIA--QRLKFNQIALMLKKGS 191
Cdd:PHA02878 199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgYCKDYDILKLLLEHGV 259
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-142 6.17e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 33.86  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798632   59 LLRRNADVNLKNLKERTCLHYAVKKRftffdylliillmpvlligyflmvsktkqNEALVRMLLNAGVEVNATDCYGYTA 138
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYG-----------------------------ALEIVRVLLAYGVDLNLKDEEGLTA 52


                  ....
gi 300798632  139 LHYA 142
Cdd:pfam13857  53 LDLA 56
 
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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