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Conserved domains on  [gi|68399235|ref|XP_697440|]
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ankyrin repeat and MYND domain-containing protein 1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
7-118 7.21e-40

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 148.95  E-value: 7.21e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   7 KRNGHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYGVQVFS 86
Cdd:COG4642 158 KPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYA 237

                        90       100       110
                ....*....|....*....|....*....|..
gi 68399235  87 DGSTFQGLYHAGERFGPGVMTYPDGRQDLGLW 118
Cdd:COG4642 238 DGDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-782 6.31e-19

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 6.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 516 ILQKSAEILSLTQTLSPTDTQETVRRIALLKTEHRKRWATVELLLERGADPNSSTVP-VPVIFLAIKAAHVNSVRRLLEC 594
Cdd:COG0666  30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGgNTLLHAAARNGDLEIVKLLLEA 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 595 GARTDIPlppEQKGLYPLHIAAGllgAEGPEITELLLHALADPNHKALDqnevfqldqvfedphvcqfsdahvqfsqegG 674
Cdd:COG0666 110 GADVNAR---DKDGETPLHLAAY---NGNLEIVKLLLEAGADVNAQDND------------------------------G 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 675 RTALHVACQRDSEytnarDVVALLLSHCASPNEV-WSGHSPLSLAIASGNHLAVDELLSAGADVNLPLTRHIGSALCALT 753
Cdd:COG0666 154 NTPLHLAAANGNL-----EIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                       250       260
                ....*....|....*....|....*....
gi 68399235 754 NINYDHEQQPRNHVKLLDKLVKAGADVLM 782
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-342 7.72e-11

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 7.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 223 LSIAVPLQQRLNAHIQRHRFEAETLDWDVAAVLNLNRAQFGPKGPLELNSERLIMEASRGECRNVYRILRDGEIHPNVSD 302
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 68399235 303 AKGHTALIAATVYCHDDVINMLLDNGADVNKLNAEGMSAL 342
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
zf-MYND pfam01753
MYND finger;
900-940 8.13e-08

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 49.34  E-value: 8.13e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 68399235   900 CEECGRSVGVhLTACSRCHEVYYCSNTCRGRSWEQrHREKC 940
Cdd:pfam01753   1 CAVCGKEALK-LLRCSRCKSVYYCSKECQKADWPY-HKKEC 39
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
7-118 7.21e-40

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 148.95  E-value: 7.21e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   7 KRNGHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYGVQVFS 86
Cdd:COG4642 158 KPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYA 237

                        90       100       110
                ....*....|....*....|....*....|..
gi 68399235  87 DGSTFQGLYHAGERFGPGVMTYPDGRQDLGLW 118
Cdd:COG4642 238 DGDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 10-118 5.65e-22

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 102.22  E-value: 5.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   10 GHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYGVQVFSDGS 89
Cdd:PLN03185  22 GPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGD 101

                         90       100
                 ....*....|....*....|....*....
gi 68399235   90 TFQGLYHAGERFGPGVMTYPDGRQDLGLW 118
Cdd:PLN03185 102 VFEGSWIQGLQEGPGKYTWANGNVYLGDM 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-782 6.31e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 6.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 516 ILQKSAEILSLTQTLSPTDTQETVRRIALLKTEHRKRWATVELLLERGADPNSSTVP-VPVIFLAIKAAHVNSVRRLLEC 594
Cdd:COG0666  30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGgNTLLHAAARNGDLEIVKLLLEA 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 595 GARTDIPlppEQKGLYPLHIAAGllgAEGPEITELLLHALADPNHKALDqnevfqldqvfedphvcqfsdahvqfsqegG 674
Cdd:COG0666 110 GADVNAR---DKDGETPLHLAAY---NGNLEIVKLLLEAGADVNAQDND------------------------------G 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 675 RTALHVACQRDSEytnarDVVALLLSHCASPNEV-WSGHSPLSLAIASGNHLAVDELLSAGADVNLPLTRHIGSALCALT 753
Cdd:COG0666 154 NTPLHLAAANGNL-----EIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                       250       260
                ....*....|....*....|....*....
gi 68399235 754 NINYDHEQQPRNHVKLLDKLVKAGADVLM 782
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-342 7.72e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 7.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 223 LSIAVPLQQRLNAHIQRHRFEAETLDWDVAAVLNLNRAQFGPKGPLELNSERLIMEASRGECRNVYRILRDGEIHPNVSD 302
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 68399235 303 AKGHTALIAATVYCHDDVINMLLDNGADVNKLNAEGMSAL 342
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
Ank_2 pfam12796
Ankyrin repeats (3 copies);
612-739 1.51e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   612 LHIAAGllgAEGPEITELLLHALADPNHKALDqnevfqldqvfedphvcqfsdahvqfsqegGRTALHVACQRDSEytna 691
Cdd:pfam12796   1 LHLAAK---NGNLELVKLLLENGADANLQDKN------------------------------GRTALHLAAKNGHL---- 43

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 68399235   692 rDVVALLLSHCASpNEVWSGHSPLSLAIASGNHLAVDELLSAGADVNL 739
Cdd:pfam12796  44 -EIVKLLLEHADV-NLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
zf-MYND pfam01753
MYND finger;
900-940 8.13e-08

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 49.34  E-value: 8.13e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 68399235   900 CEECGRSVGVhLTACSRCHEVYYCSNTCRGRSWEQrHREKC 940
Cdd:pfam01753   1 CAVCGKEALK-LLRCSRCKSVYYCSKECQKADWPY-HKKEC 39
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 548-738 2.83e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235  548 EHRKRwATVELLLERGADPNSSTV--PVPVIFLAIKAAHVNSVRR----LLECGARTDIPlppEQKGLYPLHIAAGLLGA 621
Cdd:PHA03100  44 EARNI-DVVKILLDNGADINSSTKnnSTPLHYLSNIKYNLTDVKEivklLLEYGANVNAP---DNNGITPLLYAISKKSN 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235  622 EgPEITELLLHALADPNHKALDQNEVFQ--LDQVFEDPHVCQF-------------------SDAHVQFSQEGGRTALHV 680
Cdd:PHA03100 120 S-YSIVEYLLDNGANVNIKNSDGENLLHlyLESNKIDLKILKLlidkgvdinaknrvnyllsYGVPINIKDVYGFTPLHY 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 68399235  681 ACqrdseYTNARDVVALLLSHCASPNEV-WSGHSPLSLAIASGNHLAVDELLSAGADVN 738
Cdd:PHA03100 199 AV-----YNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 45-67 2.45e-05

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: 41.62  E-value: 2.45e-05
                          10        20
                  ....*....|....*....|...
gi 68399235    45 YKGSFFKDYRHGKGTYSWPDGSK 67
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-335 2.35e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 2.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   276 IMEASRGECRNVYRILRDgEIHPNVSDaKGHTALIAATVYCHDDVINMLLDNGADVNKLN 335
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
20-41 6.22e-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: 6.22e-04
                           10        20
                   ....*....|....*....|..
gi 68399235     20 CKYEGEFINNLKHGDGVFTWTN 41
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 666-740 2.02e-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: 41.92  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 666 HVQFSQEG--GRTALHVACQRDseytnaRDVVALLLSHCAS-------PNEVWSGHSPLSLAIASGNHLAVDELLSAGAD 736
Cdd:cd22192  41 SCDLFQRGalGETALHVAALYD------NLEAAVVLMEAAPelvnepmTSDLYQGETALHIAVVNQNLNLVRELIARGAD 114


                ....
gi 68399235 737 VNLP 740
Cdd:cd22192 115 VVSP 118
PHA03095 PHA03095
ankyrin-like protein; Provisional
 299-344 2.08e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 2.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 68399235  299 NVSDAKGHTALiaaTVYC-----HDDVINMLLDNGADVNKLNAEGMSALAV 344
Cdd:PHA03095 111 NAKDKVGRTPL---HVYLsgfniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
7-118 7.21e-40

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 148.95  E-value: 7.21e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   7 KRNGHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYGVQVFS 86
Cdd:COG4642 158 KPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYA 237

                        90       100       110
                ....*....|....*....|....*....|..
gi 68399235  87 DGSTFQGLYHAGERFGPGVMTYPDGRQDLGLW 118
Cdd:COG4642 238 DGDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
7-111 1.11e-33

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 130.85  E-value: 1.11e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   7 KRNGHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYGVQVFS 86
Cdd:COG4642 135 GRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYA 214

                        90       100
                ....*....|....*....|....*
gi 68399235  87 DGSTFQGLYHAGERFGPGVMTYPDG 111
Cdd:COG4642 215 DGDRYEGEFKNGKRHGQGTLTYADG 239
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
7-113 1.15e-28

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 116.21  E-value: 1.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   7 KRNGHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYGVQVFS 86
Cdd:COG4642 112 GGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYA 191

                        90       100
                ....*....|....*....|....*..
gi 68399235  87 DGSTFQGLYHAGERFGPGVMTYPDGRQ 113
Cdd:COG4642 192 NGDVYEGEFKNGQRHGQGTYTYADGDR 218
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 10-118 5.65e-22

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 102.22  E-value: 5.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   10 GHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYGVQVFSDGS 89
Cdd:PLN03185  22 GPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGD 101

                         90       100
                 ....*....|....*....|....*....
gi 68399235   90 TFQGLYHAGERFGPGVMTYPDGRQDLGLW 118
Cdd:PLN03185 102 VFEGSWIQGLQEGPGKYTWANGNVYLGDM 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-782 6.31e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 6.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 516 ILQKSAEILSLTQTLSPTDTQETVRRIALLKTEHRKRWATVELLLERGADPNSSTVP-VPVIFLAIKAAHVNSVRRLLEC 594
Cdd:COG0666  30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGgNTLLHAAARNGDLEIVKLLLEA 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 595 GARTDIPlppEQKGLYPLHIAAGllgAEGPEITELLLHALADPNHKALDqnevfqldqvfedphvcqfsdahvqfsqegG 674
Cdd:COG0666 110 GADVNAR---DKDGETPLHLAAY---NGNLEIVKLLLEAGADVNAQDND------------------------------G 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 675 RTALHVACQRDSEytnarDVVALLLSHCASPNEV-WSGHSPLSLAIASGNHLAVDELLSAGADVNLPLTRHIGSALCALT 753
Cdd:COG0666 154 NTPLHLAAANGNL-----EIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                       250       260
                ....*....|....*....|....*....
gi 68399235 754 NINYDHEQQPRNHVKLLDKLVKAGADVLM 782
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAKDKDGLTALL 257
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
16-113 6.72e-17

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 81.93  E-value: 6.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235  16 WPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYGVQVFSDGSTFQGLY 95
Cdd:COG4642  98 FGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEF 177

                        90
                ....*....|....*...
gi 68399235  96 HAGERFGPGVMTYPDGRQ 113
Cdd:COG4642 178 KNGKRHGQGTLTYANGDV 195
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 7-118 2.54e-16

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 84.11  E-value: 2.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235    7 KRNGHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYGVQVFS 86
Cdd:PLN03185  42 MRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWA 121

                         90       100       110
                 ....*....|....*....|....*....|..
gi 68399235   87 DGSTFQGLYHAGERFGPGVMTYPDGRQDLGLW 118
Cdd:PLN03185 122 NGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQW 153
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 2-111 4.38e-14

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 76.80  E-value: 4.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235    2 WDISCKrNGHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYG 81
Cdd:PLN03185  84 WRLNLK-HGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFG 162

                         90       100       110
                 ....*....|....*....|....*....|
gi 68399235   82 VQVFSDGSTFQGLYHAGERFGPGVMtYPDG 111
Cdd:PLN03185 163 VYTWSDGGCYVGTWTRGLKDGKGVF-YPAG 191
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 10-113 2.73e-12

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 71.02  E-value: 2.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   10 GHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYGVqVFSDGS 89
Cdd:PLN03185 114 GPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGV-FYPAGS 192

                         90       100
                 ....*....|....*....|....*..
gi 68399235   90 TF---QGLYHAGERfGPGVMtyPDGRQ 113
Cdd:PLN03185 193 RVpavQEFYLNALR-KRGVL--PDLRR 216
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-342 7.72e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 7.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 223 LSIAVPLQQRLNAHIQRHRFEAETLDWDVAAVLNLNRAQFGPKGPLELNSERLIMEASRGECRNVYRILRDGEIHPNVSD 302
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 68399235 303 AKGHTALIAATVYCHDDVINMLLDNGADVNKLNAEGMSAL 342
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
Ank_2 pfam12796
Ankyrin repeats (3 copies);
612-739 1.51e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   612 LHIAAGllgAEGPEITELLLHALADPNHKALDqnevfqldqvfedphvcqfsdahvqfsqegGRTALHVACQRDSEytna 691
Cdd:pfam12796   1 LHLAAK---NGNLELVKLLLENGADANLQDKN------------------------------GRTALHLAAKNGHL---- 43

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 68399235   692 rDVVALLLSHCASpNEVWSGHSPLSLAIASGNHLAVDELLSAGADVNL 739
Cdd:pfam12796  44 -EIVKLLLEHADV-NLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 7-82 2.36e-10

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 64.47  E-value: 2.36e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68399235    7 KRNGHGIQEWPDGCKYEGEFINNLKHGDGVFTWTNGESYKGSFFKDYRHGKGTYsWPDGSKY--TGKFYLNRKEGYGV 82
Cdd:PLN03185 134 KMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF-YPAGSRVpaVQEFYLNALRKRGV 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
275-342 9.16e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 9.16e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68399235 275 LIMEASRGECRNVYRILRDGEIHPNVSDAKGHTALIAATVYCHDDVINMLLDNGADVNKLNAEGMSAL 342
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
275-367 5.96e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 5.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 275 LIMEASRGECRNVYRILRDGEIHPNVSDAKGHTALIAATVYCHDDVINMLLDNGADVNKLNAEGMSAL--AVCMLLYYPL 352
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALdlAAENGNLEIV 235

                        90
                ....*....|....*
gi 68399235 353 QSLHETLAEKVPRNI 367
Cdd:COG0666 236 KLLLEAGADLNAKDK 250
zf-MYND pfam01753
MYND finger;
900-940 8.13e-08

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 49.34  E-value: 8.13e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 68399235   900 CEECGRSVGVhLTACSRCHEVYYCSNTCRGRSWEQrHREKC 940
Cdd:pfam01753   1 CAVCGKEALK-LLRCSRCKSVYYCSKECQKADWPY-HKKEC 39
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
2-118 1.03e-07

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 54.58  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   2 WDISCKRNGHGIQEWPDGCKYEGEFINNlkhgdgvftwtNGESYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKEGYG 81
Cdd:COG4642  72 VTAAGGGGGGGGGKGDGGDGGGGEGGFG-----------GGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGG 140

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 68399235  82 VQVFSDGSTFQGLYHAGERFGPGVMTYPDGRQDLGLW 118
Cdd:COG4642 141 IYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEF 177
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 548-738 2.83e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235  548 EHRKRwATVELLLERGADPNSSTV--PVPVIFLAIKAAHVNSVRR----LLECGARTDIPlppEQKGLYPLHIAAGLLGA 621
Cdd:PHA03100  44 EARNI-DVVKILLDNGADINSSTKnnSTPLHYLSNIKYNLTDVKEivklLLEYGANVNAP---DNNGITPLLYAISKKSN 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235  622 EgPEITELLLHALADPNHKALDQNEVFQ--LDQVFEDPHVCQF-------------------SDAHVQFSQEGGRTALHV 680
Cdd:PHA03100 120 S-YSIVEYLLDNGANVNIKNSDGENLLHlyLESNKIDLKILKLlidkgvdinaknrvnyllsYGVPINIKDVYGFTPLHY 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 68399235  681 ACqrdseYTNARDVVALLLSHCASPNEV-WSGHSPLSLAIASGNHLAVDELLSAGADVN 738
Cdd:PHA03100 199 AV-----YNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
252-342 6.57e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.26  E-value: 6.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 252 AAVLNLNRAQFGPKGPLELNSERLIMEASRGECRNVYRILRDGEIHPNVSDAKGHTALIAATVYCHDDVINMLLDNGADV 331
Cdd:COG0666  34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                        90
                ....*....|.
gi 68399235 332 NKLNAEGMSAL 342
Cdd:COG0666 114 NARDKDGETPL 124
Ank_2 pfam12796
Ankyrin repeats (3 copies);
576-706 8.07e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 8.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   576 IFLAIKAAHVNSVRRLLECGARTDIPlppEQKGLYPLHIAAGllgAEGPEITELLLhaladpNHKALDqnevfqldqvfe 655
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ---DKNGRTALHLAAK---NGHLEIVKLLL------EHADVN------------ 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 68399235   656 dphvcqfsdahvqfSQEGGRTALHVACQRdseytNARDVVALLLSHCASPN 706
Cdd:pfam12796  57 --------------LKDNGRTALHYAARS-----GHLEIVKLLLEKGADIN 88
PHA03095 PHA03095
ankyrin-like protein; Provisional
 543-739 9.49e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 9.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235  543 ALLKTEHRKRWATVELLLERGADPNSSTV--PVPVIFLAIKAAHVNSVRRLLECGARTdiplppEQKGLY---PLHIAAG 617
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAPERcgFTPLHLYLYNATTLDVIKLLIKAGADV------NAKDKVgrtPLHVYLS 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235  618 LLGAEgPEITELLLHALADPNhkALDQNEVFQLDqVF------------------EDP------------HVCQFSDAHV 667
Cdd:PHA03095 127 GFNIN-PKVIRLLLRKGADVN--ALDLYGMTPLA-VLlksrnanvellrllidagADVyavddrfrsllhHHLQSFKPRA 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235  668 QFSQE-------------GGRTALHVACQRDSeytNARDVVALLLSHCASPNEV-WSGHSPLSLAIASGNHLAVDELLSA 733
Cdd:PHA03095 203 RIVREliragcdpaatdmLGNTPLHSMATGSS---CKRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIAL 279


                 ....*.
gi 68399235  734 GADVNL 739
Cdd:PHA03095 280 GADINA 285
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 45-67 2.45e-05

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: 41.62  E-value: 2.45e-05
                          10        20
                  ....*....|....*....|...
gi 68399235    45 YKGSFFKDYRHGKGTYSWPDGSK 67
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
Ank_2 pfam12796
Ankyrin repeats (3 copies);
555-640 3.60e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   555 TVELLLERGADPNSSTV-PVPVIFLAIKAAHVNSVRRLLECGARTDIPlppeqKGLYPLHIAAgLLGAEgpEITELLLHA 633
Cdd:pfam12796  12 LVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEHADVNLKD-----NGRTALHYAA-RSGHL--EIVKLLLEK 83


                  ....*..
gi 68399235   634 LADPNHK 640
Cdd:pfam12796  84 GADINVK 90
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
7-78 6.29e-05

Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 44.29  E-value: 6.29e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68399235   7 KRNGHGIQEWPDGC-KYEGEFINNLKHGDGVFTWTNGE-SYKGSFFKDYRHGKGTYSWPDGSKYTGKFYLNRKE 78
Cdd:COG2849  89 KLEGEWKEYYENGKlKSEGNYKNGKLHGEWKEYYENGKlKEEGNYKNGKKDGVWKYYDENGKLVKEEEYKNGKK 162
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
12-112 6.53e-05

Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 44.29  E-value: 6.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235  12 GIQEWPDGCKYEGEFINNLKHGDGVFTWTNGE-SYKGSFFKDYRHGKGTYSWPDGS-KYTGKFYLNRKEGYGVQVFSDGS 89
Cdd:COG2849  47 GGKLIKKKLGKGLGKYKKGKLGEWKTYYPNGQlKSEGTYKNGKLEGEWKEYYENGKlKSEGNYKNGKLHGEWKEYYENGK 126

                        90       100
                ....*....|....*....|....
gi 68399235  90 -TFQGLYHAGERFGPGVMTYPDGR 112
Cdd:COG2849 127 lKEEGNYKNGKKDGVWKYYDENGK 150
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 22-42 1.07e-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: 40.08  E-value: 1.07e-04
                          10        20
                  ....*....|....*....|.
gi 68399235    22 YEGEFINNLKHGDGVFTWTNG 42
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-335 2.35e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 2.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   276 IMEASRGECRNVYRILRDgEIHPNVSDaKGHTALIAATVYCHDDVINMLLDNGADVNKLN 335
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
305-342 3.69e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 3.69e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 68399235   305 GHTALIAATVYCHDDVINMLLDNGADVNKLNAEGMSAL 342
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
20-41 6.22e-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: 6.22e-04
                           10        20
                   ....*....|....*....|..
gi 68399235     20 CKYEGEFINNLKHGDGVFTWTN 41
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 304-335 7.45e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 7.45e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 68399235   304 KGHTAL-IAATVYCHDDVINMLLDNGADVNKLN 335
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
Ank_2 pfam12796
Ankyrin repeats (3 copies);
678-780 1.55e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   678 LHVACQRdseytNARDVVALLLSHCASPNEVWS-GHSPLSLAIASGNHLAVDELLSaGADVNLPLTRHigSAL-CALTNi 755
Cdd:pfam12796   1 LHLAAKN-----GNLELVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR--TALhYAARS- 71

                          90       100
                  ....*....|....*....|....*
gi 68399235   756 nydheqqprNHVKLLDKLVKAGADV 780
Cdd:pfam12796  72 ---------GHLEIVKLLLEKGADI 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-345 1.98e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 1.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235   276 IMEASRGECRNVYRILRDGEIHPNVSDAKGHTALIAATVYCHDDVINMLLDNgADVNKLNaEGMSALAVC 345
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYA 68
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 666-740 2.02e-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: 41.92  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68399235 666 HVQFSQEG--GRTALHVACQRDseytnaRDVVALLLSHCAS-------PNEVWSGHSPLSLAIASGNHLAVDELLSAGAD 736
Cdd:cd22192  41 SCDLFQRGalGETALHVAALYD------NLEAAVVLMEAAPelvnepmTSDLYQGETALHIAVVNQNLNLVRELIARGAD 114


                ....
gi 68399235 737 VNLP 740
Cdd:cd22192 115 VVSP 118
PHA03095 PHA03095
ankyrin-like protein; Provisional
 299-344 2.08e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 2.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 68399235  299 NVSDAKGHTALiaaTVYC-----HDDVINMLLDNGADVNKLNAEGMSALAV 344
Cdd:PHA03095 111 NAKDKVGRTPL---HVYLsgfniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 674-706 2.43e-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: 36.50  E-value: 2.43e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 68399235   674 GRTALHVACQRdseyTNARDVVALLLSHCASPN 706
Cdd:pfam00023   2 GNTPLHLAAGR----RGNLEIVKLLLSKGADVN 30
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 58-111 5.12e-03

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 40.59  E-value: 5.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68399235   58 GTYSWPDGSKYTGKFYLNRKEGYGVQVFSDGSTFQGLYHAGERFGPGVMTYPDG 111
Cdd:PLN03185   1 GELVLSNGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSG 54
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
44-64 6.05e-03

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 35.01  E-value: 6.05e-03
                           10        20
                   ....*....|....*....|.
gi 68399235     44 SYKGSFFKDYRHGKGTYSWPD 64
Cdd:smart00698   2 RYEGEWRNGKRHGRGVYTYAN 22
 
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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