NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1788675122|ref|XP_031792416|]
View 

ankyrin repeat and MYND domain-containing protein 1 isoform X1 [Piliocolobus tephrosceles]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
605-855 6.70e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 6.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  605 MALSMIERRKRWQTIKLLLRRGADPNLCRVPMQ-VLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAAAlpg 683
Cdd:COG0666     56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNtLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGE-TPLHLAAY--- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  684 EEGVQIVELLLHAITDVDAKasdkdgtykpgkldllpsslklsnepgpsqayysmdtplpDEGGRTALHMACEREDdnkc 763
Cdd:COG0666    130 NGNLEIVKLLLEAGADVNAQ----------------------------------------DNDGNTPLHLAAANGN---- 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  764 aRDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNDLVVKELLTHGADPNLPLTKGlGSALCVACDLtyehqrsvdDRLAL 842
Cdd:COG0666    166 -LEIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG-KTALDLAAEN---------GNLEI 234

                          250
                   ....*....|...
gi 1788675122  843 IDRLIDHGADILK 855
Cdd:COG0666    235 VKLLLEAGADLNA 247
COG4642 super family cl34799
Uncharacterized conserved protein [Function unknown];
80-186 1.01e-22

Uncharacterized conserved protein [Function unknown];


The actual alignment was detected with superfamily member COG4642:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 99.26  E-value: 1.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122   80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMYMKT-QL 158
Cdd:COG4642    139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADgDR 218

                           90       100
                   ....*....|....*....|....*...
gi 1788675122  159 FQGLYKADQRFGPGVETYPDGSQDVGLW 186
Cdd:COG4642    219 YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
346-419 1.36e-09

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 1.36e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788675122  346 ERLSTEMILKAEEGNHDwICGILKDNFASADVADAKGYTVLAAAATHCHSAIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:COG0666     85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
zf-MYND pfam01753
MYND finger;
969-1009 2.36e-09

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 53.58  E-value: 2.36e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1788675122  969 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWnEFHKKDC 1009
Cdd:pfam01753    1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
605-855 6.70e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 6.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  605 MALSMIERRKRWQTIKLLLRRGADPNLCRVPMQ-VLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAAAlpg 683
Cdd:COG0666     56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNtLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGE-TPLHLAAY--- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  684 EEGVQIVELLLHAITDVDAKasdkdgtykpgkldllpsslklsnepgpsqayysmdtplpDEGGRTALHMACEREDdnkc 763
Cdd:COG0666    130 NGNLEIVKLLLEAGADVNAQ----------------------------------------DNDGNTPLHLAAANGN---- 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  764 aRDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNDLVVKELLTHGADPNLPLTKGlGSALCVACDLtyehqrsvdDRLAL 842
Cdd:COG0666    166 -LEIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG-KTALDLAAEN---------GNLEI 234

                          250
                   ....*....|...
gi 1788675122  843 IDRLIDHGADILK 855
Cdd:COG0666    235 VKLLLEAGADLNA 247
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
80-186 1.01e-22

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 99.26  E-value: 1.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122   80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMYMKT-QL 158
Cdd:COG4642    139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADgDR 218

                           90       100
                   ....*....|....*....|....*...
gi 1788675122  159 FQGLYKADQRFGPGVETYPDGSQDVGLW 186
Cdd:COG4642    219 YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 85-186 6.03e-17

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 86.04  E-value: 6.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122   85 WQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYG-TMYMKTQLFQGLY 163
Cdd:PLN03185    28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107

                           90       100
                   ....*....|....*....|...
gi 1788675122  164 KADQRFGPGVETYPDGSQDVGLW 186
Cdd:PLN03185   108 IQGLQEGPGKYTWANGNVYLGDM 130
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 639-852 3.13e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 3.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  639 LFLAVKAGDVDGVRLLLEHGARTDICFPpqlGTLTPLHIAAalpgEEG-VQIVELLLHAITDVDakasdkDGTYKPGKLD 717
Cdd:PHA02875    39 IKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIESELHDAV----EEGdVKAVEELLDLGKFAD------DVFYKDGMTP 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  718 LLPSSLKLSNEPGPSQAYYSMDTPLPDEGGRTALHMACEREDDNkcardIVRLLLSHGANPNLL-WSGHSPLSLSIASGN 796
Cdd:PHA02875   106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLDIEdCCGCTPLIIAMAKGD 180

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1788675122  797 DLVVKELLTHGADPNLPLTKGLGSALCVACDltyehqrsvDDRLALIDRLIDHGAD 852
Cdd:PHA02875   181 IAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
739-812 6.56e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 6.56e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788675122  739 DTPLPDEGGRTALHMACEREDdnkcaRDIVRLLLSHgANPNLLWSGHSPLSLSIASGNDLVVKELLTHGADPNL 812
Cdd:pfam12796   22 DANLQDKNGRTALHLAAKNGH-----LEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
346-419 1.36e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 1.36e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788675122  346 ERLSTEMILKAEEGNHDwICGILKDNFASADVADAKGYTVLAAAATHCHSAIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:COG0666     85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
zf-MYND pfam01753
MYND finger;
969-1009 2.36e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 53.58  E-value: 2.36e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1788675122  969 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWnEFHKKDC 1009
Cdd:pfam01753    1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 639-810 1.77e-07

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: 55.02  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  639 LFLAVKAGDVDGVRLLLEHgARTDICfppQLGTL--TPLHIAAALpgeEGVQIVELLLHAITDvdakasdkdgtykpgkl 716
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALY---DNLEAAVVLMEAAPE----------------- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  717 dllpsslkLSNEPGPSQAYYsmdtplpdegGRTALHMACEREDDNkcardIVRLLLSHGA---NP------------NLL 781
Cdd:cd22192     77 --------LVNEPMTSDLYQ----------GETALHIAVVNQNLN-----LVRELIARGAdvvSPratgtffrpgpkNLI 133

                          170       180
                   ....*....|....*....|....*....
gi 1788675122  782 WSGHSPLSLSIASGNDLVVKELLTHGADP 810
Cdd:cd22192    134 YYGEHPLSFAACVGNEEIVRLLIEHGADI 162
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 376-428 1.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 1.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1788675122  376 DVADAKGYTVLAAAATHCHSAIVNLLLDCGADVNKCSDEGLTALSMCFLVYYP 428
Cdd:PHA03100   186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 747-780 5.42e-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: 41.03  E-value: 5.42e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1788675122   747 GRTALHMACEREDdnkcaRDIVRLLLSHGANPNL 780
Cdd:smart00248    2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
356-419 7.33e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 7.33e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788675122  356 AEEGNHDwICGILKDNFASADVADAKGYTVLAAAATHCHSAIVNLLLDCgADVNKCsDEGLTAL 419
Cdd:pfam12796    5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTAL 65
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 114-136 1.34e-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: 39.70  E-value: 1.34e-04
                           10        20
                   ....*....|....*....|...
gi 1788675122  114 YHGQFYRDHCHGLGTYVWPDGSS 136
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
113-133 7.45e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 37.71  E-value: 7.45e-04
                            10        20
                    ....*....|....*....|.
gi 1788675122   113 SYHGQFYRDHCHGLGTYVWPD 133
Cdd:smart00698    2 RYEGEWRNGKRHGRGVYTYAN 22
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 632-812 6.78e-03

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: 40.45  E-value: 6.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  632 CRVPM--QVLFLAVKAGDV-DGVRLLLEHGARTDIcfppqlGTlTPLHIAAalpgEEGVQIVELLLhaitdVDAKASDKD 708
Cdd:TIGR00870   47 CPDRLgrSALFVAAIENENlELTELLLNLSCRGAV------GD-TLLHAIS----LEYVDAVEAIL-----LHLLAAFRK 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  709 GTykpgkldllpsSLKLSNEPgpsqayySMDTPLPDEggrTALHMACEREDDNkcardIVRLLLSHGAN----------- 777
Cdd:TIGR00870  111 SG-----------PLELANDQ-------YTSEFTPGI---TALHLAAHRQNYE-----IVKLLLERGASvparacgdffv 164

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1788675122  778 ----PNLLWSGHSPLSLSIASGNDLVVKELLTHGADPNL 812
Cdd:TIGR00870  165 ksqgVDSFYHGESPLNAAACLGSPSIVALLSEDPADILT 203
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
605-855 6.70e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 6.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  605 MALSMIERRKRWQTIKLLLRRGADPNLCRVPMQ-VLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAAAlpg 683
Cdd:COG0666     56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNtLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGE-TPLHLAAY--- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  684 EEGVQIVELLLHAITDVDAKasdkdgtykpgkldllpsslklsnepgpsqayysmdtplpDEGGRTALHMACEREDdnkc 763
Cdd:COG0666    130 NGNLEIVKLLLEAGADVNAQ----------------------------------------DNDGNTPLHLAAANGN---- 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  764 aRDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNDLVVKELLTHGADPNLPLTKGlGSALCVACDLtyehqrsvdDRLAL 842
Cdd:COG0666    166 -LEIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG-KTALDLAAEN---------GNLEI 234

                          250
                   ....*....|...
gi 1788675122  843 IDRLIDHGADILK 855
Cdd:COG0666    235 VKLLLEAGADLNA 247
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
80-186 1.01e-22

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 99.26  E-value: 1.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122   80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMYMKT-QL 158
Cdd:COG4642    139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADgDR 218

                           90       100
                   ....*....|....*....|....*...
gi 1788675122  159 FQGLYKADQRFGPGVETYPDGSQDVGLW 186
Cdd:COG4642    219 YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
80-186 2.46e-19

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 89.25  E-value: 2.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122   80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMYMKTQ-L 158
Cdd:COG4642    116 GGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGdV 195

                           90       100
                   ....*....|....*....|....*...
gi 1788675122  159 FQGLYKADQRFGPGVETYPDGSQDVGLW 186
Cdd:COG4642    196 YEGEFKNGQRHGQGTYTYADGDRYEGEF 223
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
80-186 2.46e-19

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 89.25  E-value: 2.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122   80 QGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMymktqlf 159
Cdd:COG4642    185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTM------- 257

                           90       100
                   ....*....|....*....|....*..
gi 1788675122  160 qglykadqrfgpgveTYPDGSQDVGLW 186
Cdd:COG4642    258 ---------------TYADGSVYEGEW 269
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 85-186 6.03e-17

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 86.04  E-value: 6.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122   85 WQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYG-TMYMKTQLFQGLY 163
Cdd:PLN03185    28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107

                           90       100
                   ....*....|....*....|...
gi 1788675122  164 KADQRFGPGVETYPDGSQDVGLW 186
Cdd:PLN03185   108 IQGLQEGPGKYTWANGNVYLGDM 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
606-854 2.45e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 2.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  606 ALSMIERRKRWQTIKLLLRRGADPNLC-RVPMQVLFLAVKAGDVDGVRLLLEHGArtdicfppqlgtltplhiaaalpge 684
Cdd:COG0666    123 PLHLAAYNGNLEIVKLLLEAGADVNAQdNDGNTPLHLAAANGNLEIVKLLLEAGA------------------------- 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  685 egvqivelllhaitDVDAKasdkdgtykpgkldllpsslklsnepgpsqayysmdtplpDEGGRTALHMACEREDDnkca 764
Cdd:COG0666    178 --------------DVNAR----------------------------------------DNDGETPLHLAAENGHL---- 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  765 rDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNDLVVKELLTHGADPNLPLTKGLGSALCVACDLTYEHQRSVDDRLALI 843
Cdd:COG0666    200 -EIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                          250
                   ....*....|.
gi 1788675122  844 DRLIDHGADIL 854
Cdd:COG0666    279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
692-853 2.06e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.07  E-value: 2.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  692 LLLHAITDVDAKASDKDGTYKPGKLDLLPSSLKLSNEPGPSQAYYSMDTPLPDEGGRTALHMACEREDdnkcaRDIVRLL 771
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD-----LEIVKLL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  772 LSHGANPNLL-WSGHSPLSLSIASGNDLVVKELLTHGADPNLPLTKGLgSALCVACDltyehqrsvDDRLALIDRLIDHG 850
Cdd:COG0666    107 LEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAA---------NGNLEIVKLLLEAG 176


                   ...
gi 1788675122  851 ADI 853
Cdd:COG0666    177 ADV 179
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
75-186 3.11e-12

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 68.06  E-value: 3.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122   75 YLQLVQGVQEWQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTMYM 154
Cdd:COG4642     88 GGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTY 167

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1788675122  155 KTQL-FQGLYKADQRFGPGVETYPDGSQDVGLW 186
Cdd:COG4642    168 ADGDrYEGEFKNGKRHGQGTLTYANGDVYEGEF 200
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 639-852 3.13e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 3.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  639 LFLAVKAGDVDGVRLLLEHGARTDICFPpqlGTLTPLHIAAalpgEEG-VQIVELLLHAITDVDakasdkDGTYKPGKLD 717
Cdd:PHA02875    39 IKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIESELHDAV----EEGdVKAVEELLDLGKFAD------DVFYKDGMTP 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  718 LLPSSLKLSNEPGPSQAYYSMDTPLPDEGGRTALHMACEREDDNkcardIVRLLLSHGANPNLL-WSGHSPLSLSIASGN 796
Cdd:PHA02875   106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLDIEdCCGCTPLIIAMAKGD 180

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1788675122  797 DLVVKELLTHGADPNLPLTKGLGSALCVACDltyehqrsvDDRLALIDRLIDHGAD 852
Cdd:PHA02875   181 IAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGAD 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 602-809 9.37e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.15  E-value: 9.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  602 MRKMALSMIERRKRWQTIKLLLRRGADPN------LCRVPMQVLFLAVKAGDVDGVRLLLEHGARTDICFPPQlgtLTPL 675
Cdd:PHA03100    34 KPVLPLYLAKEARNIDVVKILLDNGADINsstknnSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNG---ITPL 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  676 HIAAALPGEEgVQIVELLLHAITDVDAKASDKDG------TYKPGKLDLLpsSLKLSNEPGPSQA----Y---YSMDTPL 742
Cdd:PHA03100   111 LYAISKKSNS-YSIVEYLLDNGANVNIKNSDGENllhlylESNKIDLKIL--KLLIDKGVDINAKnrvnYllsYGVPINI 187

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1788675122  743 PDEGGRTALHMACERedDNKcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNDLVVKELLTHGAD 809
Cdd:PHA03100   188 KDVYGFTPLHYAVYN--NNP---EFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
739-812 6.56e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 6.56e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788675122  739 DTPLPDEGGRTALHMACEREDdnkcaRDIVRLLLSHgANPNLLWSGHSPLSLSIASGNDLVVKELLTHGADPNL 812
Cdd:pfam12796   22 DANLQDKNGRTALHLAAKNGH-----LEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
639-780 7.81e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 7.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  639 LFLAVKAGDVDGVRLLLEHGARTDICFPPQlgtLTPLHIAAAlpgEEGVQIVELLL-HAITDVdakasdkdgtykpgkld 717
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG---RTALHLAAK---NGHLEIVKLLLeHADVNL----------------- 57

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1788675122  718 llpsslklsnepgpsqayysmdtplpDEGGRTALHMACEreddnKCARDIVRLLLSHGANPNL 780
Cdd:pfam12796   58 --------------------------KDNGRTALHYAAR-----SGHLEIVKLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
346-419 1.36e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 1.36e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788675122  346 ERLSTEMILKAEEGNHDwICGILKDNFASADVADAKGYTVLAAAATHCHSAIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:COG0666     85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 79-155 1.67e-09

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 61.77  E-value: 1.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122   79 VQGVQE------WQDGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTM 152
Cdd:PLN03185   108 IQGLQEgpgkytWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF 187


                   ...
gi 1788675122  153 YMK 155
Cdd:PLN03185   188 YPA 190
zf-MYND pfam01753
MYND finger;
969-1009 2.36e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 53.58  E-value: 2.36e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1788675122  969 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWnEFHKKDC 1009
Cdd:pfam01753    1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
350-419 5.99e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 5.99e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  350 TEMILKAEEGNHDWIcGILKDNFASADVADAKGYTVLAAAATHCHSAIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:COG0666    122 TPLHLAAYNGNLEIV-KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
618-703 6.23e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 6.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  618 TIKLLLRRGADPNLCRV-PMQVLFLAVKAGDVDGVRLLLEHGARTDicfppQLGTLTPLHIAAalpgEEG-VQIVELLLH 695
Cdd:pfam12796   12 LVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAA----RSGhLEIVKLLLE 82


                   ....*...
gi 1788675122  696 AITDVDAK 703
Cdd:pfam12796   83 KGADINVK 90
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 87-186 1.58e-08

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 58.69  E-value: 1.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122   87 DGCIYRGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYVWPDGSSFTGTFYLSHREGYGTmYMKTQ--LFQGLYK 164
Cdd:PLN03185     7 NGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGT-YTGTDgtTYKGRWR 85

                           90       100
                   ....*....|....*....|..
gi 1788675122  165 ADQRFGPGVETYPDGSQDVGLW 186
Cdd:PLN03185    86 LNLKHGLGYQRYPNGDVFEGSW 107
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
356-421 5.65e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.73  E-value: 5.65e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1788675122  356 AEEGNHDwICGILKDNFASADVADAKGYTVLAAAATHCHSAIVNLLLDCGADVNKCSDEGLTALSM 421
Cdd:COG0666    161 AANGNLE-IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 619-812 1.57e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  619 IKLLLRRGADPNLC----RVPMQVlFLAVKAGDVDGVRLLLEHGArtDICFPPQLGtLTPLHIAAALPGEEgVQIVELLL 694
Cdd:PHA03095   100 IKLLIKAGADVNAKdkvgRTPLHV-YLSGFNINPKVIRLLLRKGA--DVNALDLYG-MTPLAVLLKSRNAN-VELLRLLI 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  695 HAITDVDAKASDKDGTykpgkLDLLPSSLKLSNEPGPSQAYYSMDTPLPDEGGRTALHMACEReddNKCARDIVRLLLSH 774
Cdd:PHA03095   175 DAGADVYAVDDRFRSL-----LHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATG---SSCKRSLVLPLLIA 246

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1788675122  775 GANPNLL-WSGHSPLSLSIASGNDLVVKELLTHGADPNL 812
Cdd:PHA03095   247 GISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 639-810 1.77e-07

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: 55.02  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  639 LFLAVKAGDVDGVRLLLEHgARTDICfppQLGTL--TPLHIAAALpgeEGVQIVELLLHAITDvdakasdkdgtykpgkl 716
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALY---DNLEAAVVLMEAAPE----------------- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  717 dllpsslkLSNEPGPSQAYYsmdtplpdegGRTALHMACEREDDNkcardIVRLLLSHGA---NP------------NLL 781
Cdd:cd22192     77 --------LVNEPMTSDLYQ----------GETALHIAVVNQNLN-----LVRELIARGAdvvSPratgtffrpgpkNLI 133

                          170       180
                   ....*....|....*....|....*....
gi 1788675122  782 WSGHSPLSLSIASGNDLVVKELLTHGADP 810
Cdd:cd22192    134 YYGEHPLSFAACVGNEEIVRLLIEHGADI 162
Ank_2 pfam12796
Ankyrin repeats (3 copies);
751-853 3.06e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 3.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  751 LHMACEREDdnkcaRDIVRLLLSHGANPNLLWS-GHSPLSLSIASGNDLVVKELLTHgADPNLPlTKGLgSALCVACDLt 829
Cdd:pfam12796    1 LHLAAKNGN-----LELVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGR-TALHYAARS- 71

                           90       100
                   ....*....|....*....|....
gi 1788675122  830 yehqrsvdDRLALIDRLIDHGADI 853
Cdd:pfam12796   72 --------GHLEIVKLLLEKGADI 87
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 747-780 1.12e-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: 45.74  E-value: 1.12e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1788675122  747 GRTALHMACEREDDnkcaRDIVRLLLSHGANPNL 780
Cdd:pfam00023    2 GNTPLHLAAGRRGN----LEIVKLLLSKGADVNA 31
PHA03095 PHA03095
ankyrin-like protein; Provisional
 647-853 1.25e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  647 DVDGVRLLLEHGArtDICFPPQLGTlTPLHIAAALPGEEGVQIVELLLHAITDVDAkasdkdgtykpgkldllpsslkls 726
Cdd:PHA03095    26 TVEEVRRLLAAGA--DVNFRGEYGK-TPLHLYLHYSSEKVKDIVRLLLEAGADVNA------------------------ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  727 nepgpsqayysmdtplPDEGGRTALHMACEreddNKCARDIVRLLLSHGANPNL-LWSGHSPLS--LSIASGNDLVVKEL 803
Cdd:PHA03095    79 ----------------PERCGFTPLHLYLY----NATTLDVIKLLIKAGADVNAkDKVGRTPLHvyLSGFNINPKVIRLL 138

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1788675122  804 LTHGADPNlpltkglgsalcvACDLtYEHQ------RSVDDRLALIDRLIDHGADI 853
Cdd:PHA03095   139 LRKGADVN-------------ALDL-YGMTplavllKSRNANVELLRLLIDAGADV 180
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 651-826 1.29e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  651 VRLLLEHGARTDICFPPQLGtlTPLHIAAALPGEEgvqIVELLLhaITDVDAKASDKDGTYKpgkldlLPSSLKLSNEPG 730
Cdd:PHA02878   150 TKLLLSYGADINMKDRHKGN--TALHYATENKDQR---LTELLL--SYGANVNIPDKTNNSP------LHHAVKHYNKPI 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  731 -PSQAYYSMDTPLPDEGGRTALHMACEREDDnkcaRDIVRLLLSHGANPNLLWS--GHSPLSLSIASgnDLVVKELLTHG 807
Cdd:PHA02878   217 vHILLENGASTDARDKCGNTPLHISVGYCKD----YDILKLLLEHGVDVNAKSYilGLTALHSSIKS--ERKLKLLLEYG 290

                          170       180
                   ....*....|....*....|....*.
gi 1788675122  808 ADPNL-------PLTKGLGSALCVAC 826
Cdd:PHA02878   291 ADINSlnsykltPLSSAVKQYLCINI 316
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 604-792 2.40e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 2.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  604 KMALSMIERRKRWQTIKLLLRRGADPN-LCRVPMQVLFLAVKAGDVDGVRLLLEHGARTDIcfPPQLGTlTPLHIAAALP 682
Cdd:PHA02878   169 NTALHYATENKDQRLTELLLSYGANVNiPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA--RDKCGN-TPLHISVGYC 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  683 geEGVQIVELLLHAITDVDAKASDKdgtykpgkldllpsslklsnepgpsqayysmdtplpdegGRTALHMACEREddnk 762
Cdd:PHA02878   246 --KDYDILKLLLEHGVDVNAKSYIL---------------------------------------GLTALHSSIKSE---- 280

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1788675122  763 carDIVRLLLSHGANPNLL-WSGHSPLSLSI 792
Cdd:PHA02878   281 ---RKLKLLLEYGADINSLnSYKLTPLSSAV 308
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 376-428 1.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 1.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1788675122  376 DVADAKGYTVLAAAATHCHSAIVNLLLDCGADVNKCSDEGLTALSMCFLVYYP 428
Cdd:PHA03100   186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 747-780 5.42e-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: 41.03  E-value: 5.42e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1788675122   747 GRTALHMACEREDdnkcaRDIVRLLLSHGANPNL 780
Cdd:smart00248    2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
356-419 7.33e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 7.33e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788675122  356 AEEGNHDwICGILKDNFASADVADAKGYTVLAAAATHCHSAIVNLLLDCgADVNKCsDEGLTAL 419
Cdd:pfam12796    5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTAL 65
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 114-136 1.34e-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: 39.70  E-value: 1.34e-04
                           10        20
                   ....*....|....*....|...
gi 1788675122  114 YHGQFYRDHCHGLGTYVWPDGSS 136
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 607-781 1.77e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  607 LSMIERRKRWQTIKLLLRRGADPNLCRVP-MQVLFLAVKAGDVDGVRLLLEHGARTDI--CFppqlgTLTPLHIAAAlpg 683
Cdd:PHA02875   106 LHLATILKKLDIMKLLIARGADPDIPNTDkFSPLHLAVMMGDIKGIELLIDHKACLDIedCC-----GCTPLIIAMA--- 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  684 EEGVQIVELLLHAITDVDakasdkdgtykpgkldllpsslklsnepgpsqaYYsmdtplpdeGGRTALHMACEREDDNKC 763
Cdd:PHA02875   178 KGDIAICKMLLDSGANID---------------------------------YF---------GKNGCVAALCYAIENNKI 215

                          170
                   ....*....|....*...
gi 1788675122  764 arDIVRLLLSHGANPNLL 781
Cdd:PHA02875   216 --DIVRLFIKRGADCNIM 231
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 747-862 2.13e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.26  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  747 GRTALHMACEREDDNkcardIVRLLLSHGAN--------------PNLLWSGHSPLSLSIASGNDLVVKELLTHGADP-N 811
Cdd:cd21882     73 GQTALHIAIENRNLN-----LVRLLVENGADvsaratgrffrkspGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPaA 147

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1788675122  812 LPLTKGLGS----ALCVACDLTYEHQR---SVDDRLALIDRLIDHGADiLKPVTLRQG 862
Cdd:cd21882    148 LEAQDSLGNtvlhALVLQADNTPENSAfvcQMYNLLLSYGAHLDPTQQ-LEEIPNHQG 204
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
113-133 7.45e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 37.71  E-value: 7.45e-04
                            10        20
                    ....*....|....*....|.
gi 1788675122   113 SYHGQFYRDHCHGLGTYVWPD 133
Cdd:smart00698    2 RYEGEWRNGKRHGRGVYTYAN 22
Ank_4 pfam13637
Ankyrin repeats (many copies);
382-419 7.46e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 7.46e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1788675122  382 GYTVLAAAATHCHSAIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 747-779 2.18e-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: 36.47  E-value: 2.18e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1788675122  747 GRTALHMACEREDdnkcaRDIVRLLLSHGANPN 779
Cdd:pfam13606    2 GNTPLHLAARNGR-----LEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
636-694 2.34e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.34e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788675122  636 MQVLFLAVKAGDVDGVRLLLEHGA---RTDICFppqlgtLTPLHIAAAlpgEEGVQIVELLL 694
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAdinAVDGNG------ETALHFAAS---NGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 619-726 2.36e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  619 IKLLLRRGADPNlCR--VPMQVLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAaalpGEEGV-QIVELLL- 694
Cdd:PTZ00322    98 ARILLTGGADPN-CRdyDGRTPLHIACANGHVQVVRVLLEFGA--DPTLLDKDGK-TPLELA----EENGFrEVVQLLSr 169

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1788675122  695 HAITDVDAKASDkdgtyKPGKLDLLPSSLKLS 726
Cdd:PTZ00322   170 HSQCHFELGANA-----KPDSFTGKPPSLEDS 196
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 766-811 3.10e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 3.10e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1788675122  766 DIVRLLLSHGANPNL-LWSGHSPLSLSIASGNDLVVKELLTHGADPN 811
Cdd:PHA02875    16 DIARRLLDIGINPNFeIYDGISPIKLAMKFRDSEAIKLLMKHGAIPD 62
Ank_2 pfam12796
Ankyrin repeats (3 copies);
356-409 4.35e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.40  E-value: 4.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1788675122  356 AEEGNHDwICGILKDNFASADVADakGYTVLAAAATHCHSAIVNLLLDCGADVN 409
Cdd:pfam12796   38 AKNGHLE-IVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLLLEKGADIN 88
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
356-419 4.41e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 4.41e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788675122  356 AEEGNHDwICGILKDNFASADVADAKGYTVLAAAATHCHSAIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:COG0666    194 AENGHLE-IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 381-413 4.81e-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: 35.73  E-value: 4.81e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1788675122  381 KGYTVL-AAAATHCHSAIVNLLLDCGADVNKCSD 413
Cdd:pfam00023    1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
733-780 5.30e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1788675122  733 QAYYSMDTPLPDEGGRTALHMACEREddnkcARDIVRLLLSHGANPNL 780
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYG-----ALEIVRVLLAYGVDLNL 44
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 632-812 6.78e-03

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: 40.45  E-value: 6.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  632 CRVPM--QVLFLAVKAGDV-DGVRLLLEHGARTDIcfppqlGTlTPLHIAAalpgEEGVQIVELLLhaitdVDAKASDKD 708
Cdd:TIGR00870   47 CPDRLgrSALFVAAIENENlELTELLLNLSCRGAV------GD-TLLHAIS----LEYVDAVEAIL-----LHLLAAFRK 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  709 GTykpgkldllpsSLKLSNEPgpsqayySMDTPLPDEggrTALHMACEREDDNkcardIVRLLLSHGAN----------- 777
Cdd:TIGR00870  111 SG-----------PLELANDQ-------YTSEFTPGI---TALHLAAHRQNYE-----IVKLLLERGASvparacgdffv 164

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1788675122  778 ----PNLLWSGHSPLSLSIASGNDLVVKELLTHGADPNL 812
Cdd:TIGR00870  165 ksqgVDSFYHGESPLNAAACLGSPSIVALLSEDPADILT 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
386-419 7.45e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.63  E-value: 7.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1788675122  386 LAAAATHCHSAIVNLLLDCGADVNKCSDEGLTAL 419
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 622-809 7.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 7.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  622 LLRRGADPNLCRVPMQV-LFLAVKAG-DVDGVRLLLEHGArtDICFPPQLgTLTPLHIAAALPGEEGVQIVELLLHAitD 699
Cdd:PHA02876   293 LLERGADVNAKNIKGETpLYLMAKNGyDTENIRTLIMLGA--DVNAADRL-YITPLHQASTLDRNKDIVITLLELGA--N 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  700 VDAKA-SDKDGTYKPGK----------LDLLPSSLKLSNEPGP--------SQAYYSMDTpLPDEGGR---------TAL 751
Cdd:PHA02876   368 VNARDyCDKTPIHYAAVrnnvviintlLDYGADIEALSQKIGTalhfalcgTNPYMSVKT-LIDRGANvnsknkdlsTPL 446

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1788675122  752 HMACEreddNKCARDIVRLLLSHGANPNLLwSGHSPLSLSIASGNDLVVKELLTHGAD 809
Cdd:PHA02876   447 HYACK----KNCKLDVIEMLLDNGADVNAI-NIQNQYPLLIALEYHGIVNILLHYGAE 499
PHA03095 PHA03095
ankyrin-like protein; Provisional
 766-855 9.34e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 9.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  766 DIVRLLLSHGANPNllWSGH---SPLSLSIASGNDL---VVKELLTHGADPNLPLTKGLGSALCVACDltyehqrsvDDR 839
Cdd:PHA03095    28 EEVRRLLAAGADVN--FRGEygkTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYN---------ATT 96

                           90
                   ....*....|....*.
gi 1788675122  840 LALIDRLIDHGADILK 855
Cdd:PHA03095    97 LDVIKLLIKAGADVNA 112
Ank_5 pfam13857
Ankyrin repeats (many copies);
367-422 9.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 9.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1788675122  367 ILKDNFASADVADAKGYTVLAAAATHCHSAIVNLLLDCGADVNKCSDEGLTALSMC 422
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 619-720 9.61e-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: 9.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788675122  619 IKLLLRRGADP---------------NLCRVPMQVLFLAVKAGDVDGVRLLLEHGArtDICFPPQLGTlTPLHIAAALPG 683
Cdd:cd22192    105 VRELIARGADVvspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGA--DIRAQDSLGN-TVLHILVLQPN 181

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1788675122  684 EEGV-QIVELLLhaitdvdakASDKDGTYKPgkLDLLP 720
Cdd:cd22192    182 KTFAcQMYDLIL---------SYDKEDDLQP--LDLVP 208
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH