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Conserved domains on  [gi|1788675125|ref|XP_031792417|]
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ankyrin repeat and MYND domain-containing protein 1 isoform X2 [Piliocolobus tephrosceles]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4642 super family cl34799
Uncharacterized conserved protein [Function unknown];
80-156 1.33e-18

Uncharacterized conserved protein [Function unknown];


The actual alignment was detected with superfamily member COG4642:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 86.55  E-value: 1.33e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788675125  80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMYMKT 156
Cdd:COG4642   185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYAD 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
375-543 3.47e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 3.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 375 MALSMIERRKRWQTIKLLLRRGADPNLC-RVPMQVLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAAalpg 453
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGA--DVNAQDNDGN-TPLHLAA---- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 454 EEG-VQIVELLLHAITDVDAKasdkdgtykpgkldllpsslklsnepgpsqayysmdtplpDEGGRTALHMACEREDDNK 532
Cdd:COG0666   162 ANGnLEIVKLLLEAGADVNAR----------------------------------------DNDGETPLHLAAENGHLEI 201

                         170
                  ....*....|.
gi 1788675125 533 IDRLIDHGADI 543
Cdd:COG0666   202 VKLLLEAGADV 212
zf-MYND pfam01753
MYND finger;
659-699 4.03e-09

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 52.42  E-value: 4.03e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1788675125 659 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWnEFHKKDC 699
Cdd:pfam01753   1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
162-189 3.27e-03

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 3.27e-03
                          10        20
                  ....*....|....*....|....*...
gi 1788675125 162 HCHSAIVNLLLDCGADVNKCSDEGLTAL 189
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPL 157
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
80-156 1.33e-18

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 86.55  E-value: 1.33e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788675125  80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMYMKT 156
Cdd:COG4642   185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYAD 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
375-543 3.47e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 3.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 375 MALSMIERRKRWQTIKLLLRRGADPNLC-RVPMQVLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAAalpg 453
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGA--DVNAQDNDGN-TPLHLAA---- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 454 EEG-VQIVELLLHAITDVDAKasdkdgtykpgkldllpsslklsnepgpsqayysmdtplpDEGGRTALHMACEREDDNK 532
Cdd:COG0666   162 ANGnLEIVKLLLEAGADVNAR----------------------------------------DNDGETPLHLAAENGHLEI 201

                         170
                  ....*....|.
gi 1788675125 533 IDRLIDHGADI 543
Cdd:COG0666   202 VKLLLEAGADV 212
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 85-150 5.10e-14

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 75.64  E-value: 5.10e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1788675125  85 WQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYG 150
Cdd:PLN03185   28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLG 93
zf-MYND pfam01753
MYND finger;
659-699 4.03e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 52.42  E-value: 4.03e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1788675125 659 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWnEFHKKDC 699
Cdd:pfam01753   1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
388-473 4.28e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 388 TIKLLLRRGADPNLCRV-PMQVLFLAVKAGDVDGVRLLLEHGARTDicfppQLGTLTPLHIAAalpgEEG-VQIVELLLH 465
Cdd:pfam12796  12 LVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAA----RSGhLEIVKLLLE 82


                  ....*...
gi 1788675125 466 AITDVDAK 473
Cdd:pfam12796  83 KGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 388-543 6.11e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 6.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 388 TIKLLLRRGADPNLCRV----PMQVLfLAVKAGDVDGVRLLLEHGARTDICFPPqlgTLTPLHIAAALPGEEgVQIVELL 463
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNngitPLLYA-ISKKSNSYSIVEYLLDNGANVNIKNSD---GENLLHLYLESNKID-LKILKLL 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 464 LHAITDVDAKasdkdgtykpGKLDLLPSslklsnepgpsqayYSMDTPLPDEGGRTALHMACEREDDNKIDRLIDHGADI 543
Cdd:PHA03100  163 IDKGVDINAK----------NRVNYLLS--------------YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP 218
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 114-136 1.22e-04

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 39.31  E-value: 1.22e-04
                          10        20
                  ....*....|....*....|...
gi 1788675125 114 YHGQFYRDHCHGLGTYVWPDGSS 136
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 517-543 4.42e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 4.42e-04
                           10        20
                   ....*....|....*....|....*..
gi 1788675125  517 GRTALHMACEREDDNKIDRLIDHGADI 543
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
113-133 6.13e-04

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 37.32  E-value: 6.13e-04
                           10        20
                   ....*....|....*....|.
gi 1788675125  113 SYHGQFYRDHCHGLGTYVWPD 133
Cdd:smart00698   2 RYEGEWRNGKRHGRGVYTYAN 22
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-189 3.27e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 3.27e-03
                          10        20
                  ....*....|....*....|....*...
gi 1788675125 162 HCHSAIVNLLLDCGADVNKCSDEGLTAL 189
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPL 157
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 389-490 6.24e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.00  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 389 IKLLLRRGADP---------------NLCRVPMQVLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAAALPG 453
Cdd:cd22192   105 VRELIARGADVvspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGA--DIRAQDSLGN-TVLHILVLQPN 181

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1788675125 454 EEGV-QIVELLLhaitdvdakASDKDGTYKPgkLDLLP 490
Cdd:cd22192   182 KTFAcQMYDLIL---------SYDKEDDLQP--LDLVP 208
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
80-156 1.33e-18

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 86.55  E-value: 1.33e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788675125  80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMYMKT 156
Cdd:COG4642   185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYAD 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
375-543 3.47e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 3.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 375 MALSMIERRKRWQTIKLLLRRGADPNLC-RVPMQVLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAAalpg 453
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGA--DVNAQDNDGN-TPLHLAA---- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 454 EEG-VQIVELLLHAITDVDAKasdkdgtykpgkldllpsslklsnepgpsqayysmdtplpDEGGRTALHMACEREDDNK 532
Cdd:COG0666   162 ANGnLEIVKLLLEAGADVNAR----------------------------------------DNDGETPLHLAAENGHLEI 201

                         170
                  ....*....|.
gi 1788675125 533 IDRLIDHGADI 543
Cdd:COG0666   202 VKLLLEAGADV 212
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
80-155 2.58e-16

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 79.62  E-value: 2.58e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1788675125  80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMYMK 155
Cdd:COG4642   139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYA 214
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
80-153 1.32e-15

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 77.69  E-value: 1.32e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788675125  80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMY 153
Cdd:COG4642   162 QGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLT 235
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
376-545 2.32e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 2.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 376 ALSMIERRKRWQTIKLLLRRGADPNLC-RVPMQVLFLAVKAGDVDGVRLLLEHGARTDIcfPPQLGTlTPLHIAAalpgE 454
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQdNDGNTPLHLAAANGNLEIVKLLLEAGADVNA--RDNDGE-TPLHLAA----E 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 455 EG-VQIVELLLHAITDVDAKasdkdgtykpgkldllpsslklsnepgpsqayysmdtplpDEGGRTALHMACEREDDNKI 533
Cdd:COG0666   196 NGhLEIVKLLLEAGADVNAK----------------------------------------DNDGKTALDLAAENGNLEIV 235

                         170
                  ....*....|..
gi 1788675125 534 DRLIDHGADILK 545
Cdd:COG0666   236 KLLLEAGADLNA 247
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 85-150 5.10e-14

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 75.64  E-value: 5.10e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1788675125  85 WQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYG 150
Cdd:PLN03185   28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLG 93
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
80-141 5.55e-13

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 69.99  E-value: 5.55e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788675125  80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTF 141
Cdd:COG4642   208 QGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
80-153 1.52e-11

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 65.36  E-value: 1.52e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788675125  80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMY 153
Cdd:COG4642   116 GGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLT 189
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 79-155 1.05e-09

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 61.77  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125  79 VQGVQE------WQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTM 152
Cdd:PLN03185  108 IQGLQEgpgkytWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF 187


                  ...
gi 1788675125 153 YMK 155
Cdd:PLN03185  188 YPA 190
zf-MYND pfam01753
MYND finger;
659-699 4.03e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 52.42  E-value: 4.03e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1788675125 659 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWnEFHKKDC 699
Cdd:pfam01753   1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
388-473 4.28e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 388 TIKLLLRRGADPNLCRV-PMQVLFLAVKAGDVDGVRLLLEHGARTDicfppQLGTLTPLHIAAalpgEEG-VQIVELLLH 465
Cdd:pfam12796  12 LVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAA----RSGhLEIVKLLLE 82


                  ....*...
gi 1788675125 466 AITDVDAK 473
Cdd:pfam12796  83 KGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
409-543 2.38e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 409 LFLAVKAGDVDGVRLLLEHGARTDICFPPQlgtLTPLHIAAAlpgEEGVQIVELLL-HAITDVdakasdkdgtykpgkld 487
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNG---RTALHLAAK---NGHLEIVKLLLeHADVNL----------------- 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1788675125 488 llpsslklsnepgpsqayysmdtplpDEGGRTALHMACEREDDNKIDRLIDHGADI 543
Cdd:pfam12796  58 --------------------------KDNGRTALHYAARSGHLEIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 388-543 6.11e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 6.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 388 TIKLLLRRGADPNLCRV----PMQVLfLAVKAGDVDGVRLLLEHGARTDICFPPqlgTLTPLHIAAALPGEEgVQIVELL 463
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNngitPLLYA-ISKKSNSYSIVEYLLDNGANVNIKNSD---GENLLHLYLESNKID-LKILKLL 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 464 LHAITDVDAKasdkdgtykpGKLDLLPSslklsnepgpsqayYSMDTPLPDEGGRTALHMACEREDDNKIDRLIDHGADI 543
Cdd:PHA03100  163 IDKGVDINAK----------NRVNYLLS--------------YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP 218
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
75-155 2.62e-06

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 49.57  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125  75 YLQLVQGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMYM 154
Cdd:COG4642    88 GGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTY 167


                  .
gi 1788675125 155 K 155
Cdd:COG4642   168 A 168
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
409-543 3.35e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.57  E-value: 3.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 409 LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLGTLTPLHIAAAlpgEEGVQIVELLLHAITDVDAKasdkdgtykpgkldl 488
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINA---KDDGGNTLLHAAAR---NGDLEIVKLLLEAGADVNAR--------------- 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1788675125 489 lpsslklsnepgpsqayysmdtplpDEGGRTALHMACEREDDNKIDRLIDHGADI 543
Cdd:COG0666   117 -------------------------DKDGETPLHLAAYNGNLEIVKLLLEAGADV 146
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 409-541 3.74e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 409 LFLAVKAGDVDGVRLLLEHGARTDICFPpqlGTLTPLHIAAalpgEEG-VQIVELLLHAITDVDakasdkDGTYKPGKLD 487
Cdd:PHA02875   39 IKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIESELHDAV----EEGdVKAVEELLDLGKFAD------DVFYKDGMTP 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1788675125 488 LLPSSLKLSNEPGPSQAYYSMDTPLPDEGGRTALHMACEREDDNKIDRLIDHGA 541
Cdd:PHA02875  106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 87-156 2.31e-05

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 47.91  E-value: 2.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125  87 DGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTmYMKT 156
Cdd:PLN03185    7 NGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGT-YTGT 75
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 114-136 1.22e-04

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 39.31  E-value: 1.22e-04
                          10        20
                  ....*....|....*....|...
gi 1788675125 114 YHGQFYRDHCHGLGTYVWPDGSS 136
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 374-475 1.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 374 KMALSMIERRKRWQTIKLLLRRGADPN-LCRVPMQVLFLAVKAGDVDGVRLLLEHGARTDIcfPPQLGTlTPLHIAAALP 452
Cdd:PHA02878  169 NTALHYATENKDQRLTELLLSYGANVNiPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA--RDKCGN-TPLHISVGYC 245

                          90       100
                  ....*....|....*....|...
gi 1788675125 453 geEGVQIVELLLHAITDVDAKAS 475
Cdd:PHA02878  246 --KDYDILKLLLEHGVDVNAKSY 266
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 377-471 1.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 377 LSMIERRKRWQTIKLLLRRGADPNLCRVP-MQVLFLAVKAGDVDGVRLLLEHGARTDI--CFppqlgTLTPLHIAAAlpg 453
Cdd:PHA02875  106 LHLATILKKLDIMKLLIARGADPDIPNTDkFSPLHLAVMMGDIKGIELLIDHKACLDIedCC-----GCTPLIIAMA--- 177

                          90
                  ....*....|....*...
gi 1788675125 454 EEGVQIVELLLHAITDVD 471
Cdd:PHA02875  178 KGDIAICKMLLDSGANID 195
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 517-543 4.42e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 4.42e-04
                           10        20
                   ....*....|....*....|....*..
gi 1788675125  517 GRTALHMACEREDDNKIDRLIDHGADI 543
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 517-543 5.68e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 5.68e-04
                          10        20
                  ....*....|....*....|....*...
gi 1788675125 517 GRTALHMACEREDDNKI-DRLIDHGADI 543
Cdd:pfam00023   2 GNTPLHLAAGRRGNLEIvKLLLSKGADV 29
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
113-133 6.13e-04

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 37.32  E-value: 6.13e-04
                           10        20
                   ....*....|....*....|.
gi 1788675125  113 SYHGQFYRDHCHGLGTYVWPD 133
Cdd:smart00698   2 RYEGEWRNGKRHGRGVYTYAN 22
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 517-543 9.17e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 9.17e-04
                          10        20
                  ....*....|....*....|....*..
gi 1788675125 517 GRTALHMACEREDDNKIDRLIDHGADI 543
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
406-464 1.27e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788675125 406 MQVLFLAVKAGDVDGVRLLLEHGA---RTDICFppqlgtLTPLHIAAAlpgEEGVQIVELLL 464
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGAdinAVDGNG------ETALHFAAS---NGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 389-543 1.29e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 389 IKLLLRRGADPNLC----RVPMQVlFLAVKAGDVDGVRLLLEHGArtDICFPPQLGtLTPLHIAAALPGEEgVQIVELLL 464
Cdd:PHA03095  100 IKLLIKAGADVNAKdkvgRTPLHV-YLSGFNINPKVIRLLLRKGA--DVNALDLYG-MTPLAVLLKSRNAN-VELLRLLI 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 465 HAITDVDAKASDKDGTykpgkLDLLPSSLKLSNEPGPSQAYYSMDTPLPDEGGRTALHMA-----CEReddNKIDRLIDH 539
Cdd:PHA03095  175 DAGADVYAVDDRFRSL-----LHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgssCKR---SLVLPLLIA 246


                  ....
gi 1788675125 540 GADI 543
Cdd:PHA03095  247 GISI 250
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 389-496 1.52e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 389 IKLLLRRGADPNlCR--VPMQVLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAaalpGEEGV-QIVELLL- 464
Cdd:PTZ00322   98 ARILLTGGADPN-CRdyDGRTPLHIACANGHVQVVRVLLEFGA--DPTLLDKDGK-TPLELA----EENGFrEVVQLLSr 169

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1788675125 465 HAITDVDAKASDkdgtyKPGKLDLLPSSLKLS 496
Cdd:PTZ00322  170 HSQCHFELGANA-----KPDSFTGKPPSLEDS 196
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 377-543 1.89e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 377 LSMIERRKRWQTIKLLLRRGADPNLCRVPMQV-LFLAVKAGDVDGVRLLLEHGARTDICFPPQlgTLTPLHIAAALpgeE 455
Cdd:PHA02875   39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESeLHDAVEEGDVKAVEELLDLGKFADDVFYKD--GMTPLHLATIL---K 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 456 GVQIVELLLHAITDVDAKASDKdgtYKPGKLDLLPSSLKLSNEPGPSQAYysmdTPLPDEGGRTALHMACEREDDNKIDR 535
Cdd:PHA02875  114 KLDIMKLLIARGADPDIPNTDK---FSPLHLAVMMGDIKGIELLIDHKAC----LDIEDCCGCTPLIIAMAKGDIAICKM 186


                  ....*...
gi 1788675125 536 LIDHGADI 543
Cdd:PHA02875  187 LLDSGANI 194
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-189 3.27e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 3.27e-03
                          10        20
                  ....*....|....*....|....*...
gi 1788675125 162 HCHSAIVNLLLDCGADVNKCSDEGLTAL 189
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPL 157
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 377-543 4.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 377 LSMIERRKRWQTIKLLLRRGA----DPNLCRVPMQV--LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLGTLTPLHIAAA 450
Cdd:PHA03100    1 LYSYIVLTKSRIIKVKNIKYIimedDLNDYSYKKPVlpLYLAKEARNIDVVKILLDNGADINS---STKNNSTPLHYLSN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 451 LPG--EEGVQIVELLLHAITDVDAkasdkdgTYKPGKLDLLPSSLKLSNepgpsqaYYSMDTPLPDEG---------GRT 519
Cdd:PHA03100   78 IKYnlTDVKEIVKLLLEYGANVNA-------PDNNGITPLLYAISKKSN-------SYSIVEYLLDNGanvniknsdGEN 143

                         170       180
                  ....*....|....*....|....*.
gi 1788675125 520 ALHMACE-REDDNKIDR-LIDHGADI 543
Cdd:PHA03100  144 LLHLYLEsNKIDLKILKlLIDKGVDI 169
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 389-490 6.24e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.00  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675125 389 IKLLLRRGADP---------------NLCRVPMQVLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAAALPG 453
Cdd:cd22192   105 VRELIARGADVvspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGA--DIRAQDSLGN-TVLHILVLQPN 181

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1788675125 454 EEGV-QIVELLLhaitdvdakASDKDGTYKPgkLDLLP 490
Cdd:cd22192   182 KTFAcQMYDLIL---------SYDKEDDLQP--LDLVP 208
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 443-473 7.05e-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: 34.57  E-value: 7.05e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1788675125 443 TPLHIAAALPGeeGVQIVELLLHAITDVDAK 473
Cdd:pfam00023   4 TPLHLAAGRRG--NLEIVKLLLSKGADVNAR 32
 
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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