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Conserved domains on  [gi|1720375492|ref|XP_030103201|]
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ankyrin repeat domain-containing protein 31 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1148-1297 2.83e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 2.83e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1148 SQGVNttgIGKRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENI 1227
Cdd:COG0666    108 EAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375492 1228 DGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA---DDEKMKELLKSYGAIESTNGEKRNSTDL 1297
Cdd:COG0666    185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaenGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-614 3.53e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 3.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHD 548
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720375492  549 AVMNRHYKVAELLLMSGADPLFRSDHGTCALDEAKDSSMETLLMKYIPQQKKCHLSAQRNSTDPAH 614
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 1683-1785 2.35e-22

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


:

Pssm-ID: 465856  Cd Length: 108  Bit Score: 93.53  E-value: 2.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1683 QHPTKTVPHRNTTPRKKAVQLKDLILRGRINPGNNIL--EFKTQetTHRASVLPSGKLKGENGQIYQNPVTWLKELL--- 1757
Cdd:pfam18755    1 PSSESAPSGGSSRRTGRRVTLQDLLEAGLLQPGEGLLsiEYKGQ--KHRADLLADGKIRLEDGQIFASPSAWAKHVKrgk 78

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720375492 1758 -GGGSYVTWNYAW-NTVTYLGRELVKCVSE 1785
Cdd:pfam18755   79 kSGNGWASWKYSKgKKLDDLRAELLKKVAR 108
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1148-1297 2.83e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 2.83e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1148 SQGVNttgIGKRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENI 1227
Cdd:COG0666    108 EAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375492 1228 DGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA---DDEKMKELLKSYGAIESTNGEKRNSTDL 1297
Cdd:COG0666    185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaenGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-614 3.53e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 3.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHD 548
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720375492  549 AVMNRHYKVAELLLMSGADPLFRSDHGTCALDEAKDSSMETLLMKYIPQQKKCHLSAQRNSTDPAH 614
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 1683-1785 2.35e-22

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


Pssm-ID: 465856  Cd Length: 108  Bit Score: 93.53  E-value: 2.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1683 QHPTKTVPHRNTTPRKKAVQLKDLILRGRINPGNNIL--EFKTQetTHRASVLPSGKLKGENGQIYQNPVTWLKELL--- 1757
Cdd:pfam18755    1 PSSESAPSGGSSRRTGRRVTLQDLLEAGLLQPGEGLLsiEYKGQ--KHRADLLADGKIRLEDGQIFASPSAWAKHVKrgk 78

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720375492 1758 -GGGSYVTWNYAW-NTVTYLGRELVKCVSE 1785
Cdd:pfam18755   79 kSGNGWASWKYSKgKKLDDLRAELLKKVAR 108
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1167-1259 3.47e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 3.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1167 LHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQaGANVNCENiDGIVPLHGASAGNHLKAAE 1246
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1720375492 1247 ILLEHGANPNQKD 1259
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
480-568 2.36e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 2.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  480 LYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKgGADVNVKGKYQiTPLHDAVMNRHYKVAE 559
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVK 78


                   ....*....
gi 1720375492  560 LLLMSGADP 568
Cdd:pfam12796   79 LLLEKGADI 87
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1147-1269 3.96e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 3.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1147 CSQGVNTtgigkRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCEN 1226
Cdd:PHA02874   113 CGIDVNI-----KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720375492 1227 IDGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA 1269
Cdd:PHA02874   188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 468-590 2.48e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.05  E-value: 2.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  468 TINRRNVFGENLLY---KAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELL-KGGADVNVKGKYQI 543
Cdd:PHA03095    39 DVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKAGADVNAKDKVGR 118

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720375492  544 TPLHD--AVMNRHYKVAELLLMSGADPLFRSDHGTCALD---EAKDSSMETL 590
Cdd:PHA03095   119 TPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllKSRNANVELL 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 454-568 1.00e-05

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: 50.40  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  454 KKNGTGEMKKMCLCT---INRRNVFGENLLYKAALHNDVDLVRCCIKNG-ENVNQPS----YDGWTALHEASIGGYYQAV 525
Cdd:cd22192     26 KENDVQAIKKLLKCPscdLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMtsdlYQGETALHIAVVNQNLNLV 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720375492  526 SELLKGGADVN---------VKGK-----YQITPLHDAVMNRHYKVAELLLMSGADP 568
Cdd:cd22192    106 RELIARGADVVspratgtffRPGPknliyYGEHPLSFAACVGNEEIVRLLIEHGADI 162
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1196-1224 1.03e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 1.03e-04
                            10        20
                    ....*....|....*....|....*....
gi 1720375492  1196 GWTPLHKAASGGFDDVIIELLQAGANVNC 1224
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1152-1266 2.92e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1152 NTTGIGKRNKKGESQLHVAARGGNLSRVKVLIEARAD-VNLRDN----AGWTPLHKAASGGFDDVIIELLQAGANVNCEN 1226
Cdd:cd22192     40 PSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPR 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720375492 1227 IDGIV--------------PLHGASAGNHLKAAEILLEHGANPNQKDQKQRTAL 1266
Cdd:cd22192    120 ATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 469-591 7.24e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVrccIKNGENVNQPSYDGWTALHEASIGgYYQAVSELL--------KGGADVNVKGK 540
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENENLEL---TELLLNLSCRGAVGDTLLHAISLE-YVDAVEAILlhllaafrKSGPLELANDQ 120

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720375492  541 YQ------ITPLHDAVMNRHYKVAELLLMSGADPlfrsdHGTCALDEAKDSSMETLL 591
Cdd:TIGR00870  121 YTseftpgITALHLAAHRQNYEIVKLLLERGASV-----PARACGDFFVKSQGVDSF 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 541-568 2.51e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 2.51e-03
                            10        20
                    ....*....|....*....|....*...
gi 1720375492   541 YQITPLHDAVMNRHYKVAELLLMSGADP 568
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1148-1297 2.83e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 2.83e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1148 SQGVNttgIGKRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENI 1227
Cdd:COG0666    108 EAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375492 1228 DGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA---DDEKMKELLKSYGAIESTNGEKRNSTDL 1297
Cdd:COG0666    185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaenGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1156-1283 6.32e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 6.32e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1156 IGKRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHG 1235
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720375492 1236 ASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA---DDEKMKELLKSYGA 1283
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaenGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-614 3.53e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 3.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHD 548
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720375492  549 AVMNRHYKVAELLLMSGADPLFRSDHGTCALDEAKDSSMETLLMKYIPQQKKCHLSAQRNSTDPAH 614
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-582 2.76e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 2.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHD 548
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1720375492  549 AVMNRHYKVAELLLMSGADPLFRSDHGTCALDEA 582
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1159-1279 1.99e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.20  E-value: 1.99e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1159 RNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGASA 1238
Cdd:COG0666    149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720375492 1239 GNHLKAAEILLEHGANPNQKDQKQRTALDEADDEKMKELLK 1279
Cdd:COG0666    229 NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1156-1300 1.26e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.89  E-value: 1.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1156 IGKRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHG 1235
Cdd:COG0666     47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720375492 1236 ASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA---DDEKMKELLKSYGA---IESTNGE-------KRNSTDLVKI 1300
Cdd:COG0666    127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAaanGNLEIVKLLLEAGAdvnARDNDGEtplhlaaENGHLEIVKL 204
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-600 5.04e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.57  E-value: 5.04e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHD 548
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720375492  549 AVMNRHYKVAELLLMSGADPLFRSDHGTCALDEAKDSSMETLLMKYIPQQKK 600
Cdd:COG0666    226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 1683-1785 2.35e-22

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


Pssm-ID: 465856  Cd Length: 108  Bit Score: 93.53  E-value: 2.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1683 QHPTKTVPHRNTTPRKKAVQLKDLILRGRINPGNNIL--EFKTQetTHRASVLPSGKLKGENGQIYQNPVTWLKELL--- 1757
Cdd:pfam18755    1 PSSESAPSGGSSRRTGRRVTLQDLLEAGLLQPGEGLLsiEYKGQ--KHRADLLADGKIRLEDGQIFASPSAWAKHVKrgk 78

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720375492 1758 -GGGSYVTWNYAW-NTVTYLGRELVKCVSE 1785
Cdd:pfam18755   79 kSGNGWASWKYSKgKKLDDLRAELLKKVAR 108
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1167-1259 3.47e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 3.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1167 LHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQaGANVNCENiDGIVPLHGASAGNHLKAAE 1246
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1720375492 1247 ILLEHGANPNQKD 1259
Cdd:pfam12796   79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-582 5.57e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 5.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHD 548
Cdd:COG0666     47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1720375492  549 AVMNRHYKVAELLLMSGADPLFRSDHGTCALDEA 582
Cdd:COG0666    127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
Ank_2 pfam12796
Ankyrin repeats (3 copies);
480-568 2.36e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 2.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  480 LYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKgGADVNVKGKYQiTPLHDAVMNRHYKVAE 559
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVK 78


                   ....*....
gi 1720375492  560 LLLMSGADP 568
Cdd:pfam12796   79 LLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1159-1266 4.17e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 4.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1159 RNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGASA 1238
Cdd:COG0666    182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                           90       100
                   ....*....|....*....|....*...
gi 1720375492 1239 GNHLKAAEILLEHGANPNQKDQKQRTAL 1266
Cdd:COG0666    262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1156-1300 2.38e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 2.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1156 IGKRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHG 1235
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720375492 1236 ASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA---DDEKMKELLKSYGA---IESTNGE-------KRNSTDLVKI 1300
Cdd:COG0666     94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAaynGNLEIVKLLLEAGAdvnAQDNDGNtplhlaaANGNLEIVKL 171
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-576 7.75e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 7.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHD 548
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                           90       100
                   ....*....|....*....|....*...
gi 1720375492  549 AVMNRHYKVAELLLMSGADPLFRSDHGT 576
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLL 286
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1154-1226 3.50e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 3.50e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375492 1154 TGIGKRNKKGESQLHVAARGGNLSRVKVLIEaRADVNLRDNaGWTPLHKAASGGFDDVIIELLQAGANVNCEN 1226
Cdd:pfam12796   21 ADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1147-1269 3.96e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 3.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1147 CSQGVNTtgigkRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCEN 1226
Cdd:PHA02874   113 CGIDVNI-----KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720375492 1227 IDGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA 1269
Cdd:PHA02874   188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1156-1266 1.71e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 1.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1156 IGKRNKKGESQLHVAARGG-NLSRVKVLIEARADVNLRDNAGWTPLHKAAS-GGFDDVIIELLQAGANVNCENIDGIVPL 1233
Cdd:PHA02876   300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPI 379

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1720375492 1234 HGASAGNHLKAAEILLEHGANPNQKDQKQRTAL 1266
Cdd:PHA02876   380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412
PHA03095 PHA03095
ankyrin-like protein; Provisional
 468-590 2.48e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.05  E-value: 2.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  468 TINRRNVFGENLLY---KAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELL-KGGADVNVKGKYQI 543
Cdd:PHA03095    39 DVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKAGADVNAKDKVGR 118

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720375492  544 TPLHD--AVMNRHYKVAELLLMSGADPLFRSDHGTCALD---EAKDSSMETL 590
Cdd:PHA03095   119 TPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllKSRNANVELL 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
469-538 4.49e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 4.49e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGeNVNQPSYdGWTALHEASIGGYYQAVSELLKGGADVNVK 538
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
1167-1216 8.47e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 8.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1167 LHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELL 1216
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1160-1279 8.66e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.12  E-value: 8.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1160 NKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGASAG 1239
Cdd:PLN03192   522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1720375492 1240 NHLKAAEIL--LEHGANPNQKDQKQRTALDEADDEKMKELLK 1279
Cdd:PLN03192   602 KHHKIFRILyhFASISDPHAAGDLLCTAAKRNDLTAMKELLK 643
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1134-1256 1.85e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 1.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1134 QNFRKRKCSLKAPCSQGVNTTGigkRNKKGESQLHVAARGGNLSRVKV--LIEARADVNLRDNAGWTPLHKAASGGFDDV 1211
Cdd:PHA03095   196 QSFKPRARIVRELIRAGCDPAA---TDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRA 272

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720375492 1212 IIELLQAGANVNCENIDGIVPLHGASAGNHLKAAEILLEhgANPN 1256
Cdd:PHA03095   273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA--KNPS 315
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1163-1267 2.48e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 2.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1163 GESQLHVAARGGNLSRVKV---LIEARADVNLRDNAGWTPLHKAASggFDDV--IIELL-QAGANVNCENIDGIVPLHGA 1236
Cdd:PHA03095    47 GKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLY--NATTldVIKLLiKAGADVNAKDKVGRTPLHVY 124

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1720375492 1237 SAGN--HLKAAEILLEHGANPNQKDQKQRTALD 1267
Cdd:PHA03095   125 LSGFniNPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1179-1278 3.39e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 3.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1179 VKVLIEARADVNLRDNAGWTPLHKAASGGF--DDVIIELLQAGANVNCENIDGIVPLHG--ASAGNHLKAAEILLEHGAN 1254
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGAD 179

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720375492 1255 PNQKDQKQRTALD------EADDEKMKELL 1278
Cdd:PHA03095   180 VYAVDDRFRSLLHhhlqsfKPRARIVRELI 209
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1160-1281 3.65e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 3.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1160 NKKGESQLHVAARGGNLS------------------RVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGAN 1221
Cdd:PHA03100   138 NSDGENLLHLYLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720375492 1222 VNCENIDGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQR-TALDEADDEKMKELLKSY 1281
Cdd:PHA03100   218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETLLyFKDKDLNTITKIKMLKKS 278
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1175-1259 5.31e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.45  E-value: 5.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1175 NLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDV-IIE-LLQAGANVNCENIDGIVPLHGASAGNH--LKAAEILLE 1250
Cdd:PHA03100    85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYsIVEyLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLID 164


                   ....*....
gi 1720375492 1251 HGANPNQKD 1259
Cdd:PHA03100   165 KGVDINAKN 173
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-582 9.75e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 9.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHD 548
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1720375492  549 AVMNRHYKVAELLLMSGADPLFRSDHGTCALDEA 582
Cdd:COG0666     94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1158-1291 2.72e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 2.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1158 KRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGAS 1237
Cdd:PHA02878   163 KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1238 AgnHLKAAEI---LLEHGANPNQKDQ-KQRTALDEA-DDEKMKELLKSYGA-IESTNGEK 1291
Cdd:PHA02878   243 G--YCKDYDIlklLLEHGVDVNAKSYiLGLTALHSSiKSERKLKLLLEYGAdINSLNSYK 300
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1176-1266 2.91e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.50  E-value: 2.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1176 LSRVKVLIEARADVNLRDNAGWTPLH---KAASGGFDDVIIELLQAGANVNCENIDGIVPLHG-ASAGNHLKAAEILLEH 1251
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKA 106

                           90
                   ....*....|....*
gi 1720375492 1252 GANPNQKDQKQRTAL 1266
Cdd:PHA03095   107 GADVNAKDKVGRTPL 121
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1167-1269 3.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 3.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1167 LHVAARGGNLSR-VKVLIEARADVNLRDNAGWTPLHKAASGGFD-DVIIELLQAGANVNCENIDGIVPLHGASAGNHLKA 1244
Cdd:PHA02876   277 LHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKD 356

                           90       100
                   ....*....|....*....|....*.
gi 1720375492 1245 AEI-LLEHGANPNQKDQKQRTALDEA 1269
Cdd:PHA02876   357 IVItLLELGANVNARDYCDKTPIHYA 382
Ank_2 pfam12796
Ankyrin repeats (3 copies);
513-582 4.11e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 4.11e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  513 LHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLLMSGAdpLFRSDHGTCALDEA 582
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYA 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
478-529 5.37e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 5.37e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720375492  478 NLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELL 529
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
509-562 1.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 1.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720375492  509 GWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLL 562
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1201-1296 1.03e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1201 HKAASGgfDDVIIE-LLQAGANVNCENIDGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALD---EADDEKMKE 1276
Cdd:PTZ00322    88 QLAASG--DAVGARiLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLElaeENGFREVVQ 165

                           90       100
                   ....*....|....*....|
gi 1720375492 1277 LLKSYgAIESTNGEKRNSTD 1296
Cdd:PTZ00322   166 LLSRH-SQCHFELGANAKPD 184
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1156-1300 1.89e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.83  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1156 IGKRNKKGESQLHVAA--RGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDV-IIELL-QAGANVNCEN----- 1226
Cdd:PHA03100    99 VNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkILKLLiDKGVDINAKNrvnyl 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1227 ------ID-----GIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA----DDEKMKELLKSYGAIESTNG-- 1289
Cdd:PHA03100   179 lsygvpINikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAilnnNKEIFKLLLNNGPSIKTIIEtl 258

                          170
                   ....*....|.
gi 1720375492 1290 EKRNSTDLVKI 1300
Cdd:PHA03100   259 LYFKDKDLNTI 269
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1179-1269 2.56e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 2.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1179 VKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGASAGNHLKAAEILLEHGANPNQK 1258
Cdd:PHA02874   107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                           90
                   ....*....|.
gi 1720375492 1259 DQKQRTALDEA 1269
Cdd:PHA02874   187 DNNGESPLHNA 197
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1160-1269 2.79e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 2.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1160 NKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFD-DVIIELLQAGANVNCEN-IDGIVPLHgaS 1237
Cdd:PHA02878   198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSyILGLTALH--S 275

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720375492 1238 AGNHLKAAEILLEHGANPNQKDQKQRTALDEA 1269
Cdd:PHA02878   276 SIKSERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_5 pfam13857
Ankyrin repeats (many copies);
1159-1203 2.91e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 2.91e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720375492 1159 RNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKA 1203
Cdd:pfam13857   12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1179-1269 2.99e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 2.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1179 VKVLIEARADVNLRDNAGWTPLHKAASGGF--DDVIIELLQAGANVNCENIDGIVPLHGASAGNHLKAAEILLEHGANPN 1256
Cdd:PHA03095   205 VRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                           90
                   ....*....|...
gi 1720375492 1257 QKDQKQRTALDEA 1269
Cdd:PHA03095   285 AVSSDGNTPLSLM 297
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 465-582 5.91e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 5.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  465 CLCTINRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQIT 544
Cdd:PHA02874   113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1720375492  545 PLHDAVMNRHYKVAELLLMSGADPLFRSDHGTCALDEA 582
Cdd:PHA02874   193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
1196-1249 1.34e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720375492 1196 GWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGASAGNHLKAAEILL 1249
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 418-580 1.77e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 1.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  418 KDQINSIFTTDSFSKRKNMHSSGFKNEQIrkseqlrkKNGTGEMKKMCL---CTINRRNVFGENLLYKAALHNDVDLVRC 494
Cdd:PHA02874   104 KDMIKTILDCGIDVNIKDAELKTFLHYAI--------KKGDLESIKMLFeygADVNIEDDNGCYPIHIAIKHNFFDIIKL 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  495 CIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHDAVM-NRhyKVAELLL---------MS 564
Cdd:PHA02874   176 LLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNR--SAIELLInnasindqdID 253

                          170
                   ....*....|....*.
gi 1720375492  565 GADPLFRSDHGTCALD 580
Cdd:PHA02874   254 GSTPLHHAINPPCDID 269
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1161-1256 2.53e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1161 KKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGASAGN 1240
Cdd:PHA02875   100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                           90
                   ....*....|....*.
gi 1720375492 1241 HLKAAEILLEHGANPN 1256
Cdd:PHA02875   180 DIAICKMLLDSGANID 195
PHA03095 PHA03095
ankyrin-like protein; Provisional
 473-579 3.11e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  473 NVFGENLLYK---AALHNDVDLVRCCIKNGENVNQPSYDGWTALH---EASIGGYYQAVSELLKGGADVNVKGKYQITPL 546
Cdd:PHA03095     8 DIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPL 87

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1720375492  547 HDAVMNRH-YKVAELLLMSGADPLFRSDHGTCAL 579
Cdd:PHA03095    88 HLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPL 121
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 469-567 7.67e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 7.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIG-GYYQAVSELLKGGADVNVKGKYQITPLH 547
Cdd:PHA02876   368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGtNPYMSVKTLIDRGANVNSKNKDLSTPLH 447

                           90       100
                   ....*....|....*....|.
gi 1720375492  548 DAVMNR-HYKVAELLLMSGAD 567
Cdd:PHA02876   448 YACKKNcKLDVIEMLLDNGAD 468
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 476-579 7.74e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 7.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  476 GENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHDAVMNRHY 555
Cdd:PHA02875   102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                           90       100
                   ....*....|....*....|....
gi 1720375492  556 KVAELLLMSGADPLFRSDHGTCAL 579
Cdd:PHA02875   182 AICKMLLDSGANIDYFGKNGCVAA 205
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 467-567 8.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 8.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  467 CTINRRNVFGENLLyKAAL---HNDVDLVRCCIKNGENVNQP-------SYD---------GWTALHEASIGGYYQAVSE 527
Cdd:PHA03100   132 ANVNIKNSDGENLL-HLYLesnKIDLKILKLLIDKGVDINAKnrvnyllSYGvpinikdvyGFTPLHYAVYNNNPEFVKY 210

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1720375492  528 LLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLLMSGAD 567
Cdd:PHA03100   211 LLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1167-1283 8.77e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 8.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1167 LHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGF---DDVIIE--LLQAGANVNCENIDGIVPLHGASAG-- 1239
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltDVKEIVklLLEYGANVNAPDNNGITPLLYAISKks 118

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1720375492 1240 NHLKAAEILLEHGANPNQKDQKQRTALDEA-----DDEKMKELLKSYGA 1283
Cdd:PHA03100   119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYlesnkIDLKILKLLIDKGV 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
1182-1236 9.74e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 9.74e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720375492 1182 LIEAR-ADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGA 1236
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 454-568 1.00e-05

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: 50.40  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  454 KKNGTGEMKKMCLCT---INRRNVFGENLLYKAALHNDVDLVRCCIKNG-ENVNQPS----YDGWTALHEASIGGYYQAV 525
Cdd:cd22192     26 KENDVQAIKKLLKCPscdLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMtsdlYQGETALHIAVVNQNLNLV 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720375492  526 SELLKGGADVN---------VKGK-----YQITPLHDAVMNRHYKVAELLLMSGADP 568
Cdd:cd22192    106 RELIARGADVVspratgtffRPGPknliyYGEHPLSFAACVGNEEIVRLLIEHGADI 162
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 479-567 1.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  479 LLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIG--GYYQAVSELLKGGADVNVKGKYQITPLHDAVMNRHY- 555
Cdd:PHA03100    76 SNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKId 155

                           90
                   ....*....|...
gi 1720375492  556 -KVAELLLMSGAD 567
Cdd:PHA03100   156 lKILKLLIDKGVD 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1168-1251 2.70e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1168 HVAARGGNLSrVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGASAGNHLKAAEI 1247
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 1720375492 1248 LLEH 1251
Cdd:PTZ00322   167 LSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 469-567 3.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 3.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHN-DVDLVRCCIKNGENVNQPSYDGWTALHEAS-IGGYYQAVSELLKGGADVNVKGKYQITPL 546
Cdd:PHA02876   300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPI 379

                           90       100
                   ....*....|....*....|.
gi 1720375492  547 HDAVMNRHYKVAELLLMSGAD 567
Cdd:PHA02876   380 HYAAVRNNVVIINTLLDYGAD 400
Ank_5 pfam13857
Ankyrin repeats (many copies);
1215-1269 5.27e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 5.27e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720375492 1215 LLQAG-ANVNCENIDGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA 1269
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 480-594 7.64e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 7.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  480 LYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASigGY---YQAVSELLKGGADVNVKGKYQ-ITPLHDAVmnRHY 555
Cdd:PHA02878   205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYckdYDILKLLLEHGVDVNAKSYILgLTALHSSI--KSE 280

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1720375492  556 KVAELLLMSGADPlfrsdhgtCALDEAKDSSMETLLMKY 594
Cdd:PHA02878   281 RKLKLLLEYGADI--------NSLNSYKLTPLSSAVKQY 311
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1196-1224 1.03e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 1.03e-04
                            10        20
                    ....*....|....*....|....*....
gi 1720375492  1196 GWTPLHKAASGGFDDVIIELLQAGANVNC 1224
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 477-567 1.06e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.31  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  477 ENLLYKAALHNDVDLVRCCIKNgenvnqPSYD-------GWTALHEASIGGYYQAVSELLKGGAD-VNV-------KGKy 541
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKC------PSCDlfqrgalGETALHVAALYDNLEAAVVLMEAAPElVNEpmtsdlyQGE- 90

                           90       100
                   ....*....|....*....|....*.
gi 1720375492  542 qiTPLHDAVMNRHYKVAELLLMSGAD 567
Cdd:cd22192     91 --TALHIAVVNQNLNLVRELIARGAD 114
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 480-567 1.31e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  480 LYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQA-----VSELLKGGADVNVKGKYQITPLHDAVMNR- 553
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKs 118

                           90
                   ....*....|....*
gi 1720375492  554 -HYKVAELLLMSGAD 567
Cdd:PHA03100   119 nSYSIVEYLLDNGAN 133
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1159-1233 1.39e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1159 RNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVI-------IELLQAGANVNCENIDGIV 1231
Cdd:PTZ00322   111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVqllsrhsQCHFELGANAKPDSFTGKP 190


                   ..
gi 1720375492 1232 PL 1233
Cdd:PTZ00322   191 PS 192
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 1175-1299 1.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.81  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1175 NLSRVKVLIEARADVN--LRDNaGWTPLHKAASGGfDDVIIELLQ----AGANVNCENIDGIVPLHGASAGNHLK--AAE 1246
Cdd:PHA02859    65 NVEILKFLIENGADVNfkTRDN-NLSALHHYLSFN-KNVEPEILKilidSGSSITEEDEDGKNLLHMYMCNFNVRinVIK 142

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720375492 1247 ILLEHGANPNQKDQKQRTALDE----ADDEKMKELLKSYGA-IESTNGEKRNSTDLVK 1299
Cdd:PHA02859   143 LLIDSGVSFLNKDFDNNNILYSyilfHSDKKIFDFLTSLGIdINETNKSGYNCYDLIK 200
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1196-1226 1.58e-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: 40.35  E-value: 1.58e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1720375492 1196 GWTPLHKAA-SGGFDDVIIELLQAGANVNCEN 1226
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 492-562 1.64e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.64e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720375492  492 VRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLL 562
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02946 PHA02946
ankyin-like protein; Provisional
 1207-1283 1.68e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1207 GFDDVIIE-LLQAGANVNCENIDGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTA---LDEADDEKMKE--LLKS 1280
Cdd:PHA02946    49 GLDERFVEeLLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlyyLSGTDDEVIERinLLVQ 128


                   ...
gi 1720375492 1281 YGA 1283
Cdd:PHA02946   129 YGA 131
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 528-628 1.94e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  528 LLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLLMSGADPLFRSDHGTCALDEAKDSS---METLLMKYipqqKKCHLS 604
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfreVVQLLSRH----SQCHFE 176

                           90       100
                   ....*....|....*....|....
gi 1720375492  605 AQRNStdpahVEDMFQNKKPKLSS 628
Cdd:PTZ00322   177 LGANA-----KPDSFTGKPPSLED 195
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 508-540 2.34e-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: 39.97  E-value: 2.34e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1720375492  508 DGWTALHEASI-GGYYQAVSELLKGGADVNVKGK 540
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1180-1272 2.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1180 KVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGASAGNHLKAAEILLEHGANPNQKD 1259
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND 241

                           90
                   ....*....|...
gi 1720375492 1260 QKQRTALDEADDE 1272
Cdd:PHA02876   242 LSLLKAIRNEDLE 254
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1152-1266 2.92e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1152 NTTGIGKRNKKGESQLHVAARGGNLSRVKVLIEARAD-VNLRDN----AGWTPLHKAASGGFDDVIIELLQAGANVNCEN 1226
Cdd:cd22192     40 PSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPR 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720375492 1227 IDGIV--------------PLHGASAGNHLKAAEILLEHGANPNQKDQKQRTAL 1266
Cdd:cd22192    120 ATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
469-516 4.16e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 4.16e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEA 516
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 469-591 7.24e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  469 INRRNVFGENLLYKAALHNDVDLVrccIKNGENVNQPSYDGWTALHEASIGgYYQAVSELL--------KGGADVNVKGK 540
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENENLEL---TELLLNLSCRGAVGDTLLHAISLE-YVDAVEAILlhllaafrKSGPLELANDQ 120

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720375492  541 YQ------ITPLHDAVMNRHYKVAELLLMSGADPlfrsdHGTCALDEAKDSSMETLL 591
Cdd:TIGR00870  121 YTseftpgITALHLAAHRQNYEIVKLLLERGASV-----PARACGDFFVKSQGVDSF 172
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 401-567 7.41e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 7.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  401 EAVLKKPERILSNTLSfkdQINSIFTTDSFSKRKNMHSSGFKNEQIRKSEQLRKKNGT----GEMKKMCLCTINRRNVFG 476
Cdd:PHA02878    88 EMIRSINKCSVFYTLV---AIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLSYGADINMKD 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  477 ENLLyKAALH-----NDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHDAVM 551
Cdd:PHA02878   165 RHKG-NTALHyatenKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243

                          170
                   ....*....|....*..
gi 1720375492  552 N-RHYKVAELLLMSGAD 567
Cdd:PHA02878   244 YcKDYDILKLLLEHGVD 260
PHA03095 PHA03095
ankyrin-like protein; Provisional
 490-582 8.05e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 8.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  490 DLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQA--VSELLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLLMSGAD 567
Cdd:PHA03095   203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                           90
                   ....*....|....*
gi 1720375492  568 PLFRSDHGTCALDEA 582
Cdd:PHA03095   283 INAVSSDGNTPLSLM 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 477-562 9.82e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 9.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  477 ENLLYKAALHNDVDLVRCCIKNGENVNQPSY-DGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHDAVMNRHY 555
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148


                   ....*..
gi 1720375492  556 KVAELLL 562
Cdd:PHA02875   149 KGIELLI 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1228-1259 1.13e-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: 38.04  E-value: 1.13e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1720375492 1228 DGIVPLHGASA-GNHLKAAEILLEHGANPNQKD 1259
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 488-579 1.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  488 DVDLVRCCIKNGENVNQPSYD-GWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLLMSGA 566
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90
                   ....*....|...
gi 1720375492  567 DPLFRSDHGTCAL 579
Cdd:PHA02878   226 STDARDKCGNTPL 238
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1196-1224 1.34e-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: 37.62  E-value: 1.34e-03
                           10        20
                   ....*....|....*....|....*....
gi 1720375492 1196 GWTPLHKAASGGFDDVIIELLQAGANVNC 1224
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 468-530 1.58e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 1.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375492  468 TINRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLK 530
Cdd:PHA03095   249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1233-1300 2.03e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 2.03e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720375492 1233 LHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA----DDEKMKELLKSYGAIESTNGE-------KRNSTDLVKI 1300
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAakngHLEIVKLLLEHADVNLKDNGRtalhyaaRSGHLEIVKL 79
Ank_5 pfam13857
Ankyrin repeats (many copies);
531-582 2.19e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 2.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720375492  531 GGADVNVKGKYQITPLHDAVMNRHYKVAELLLMSGADPLFRSDHGTCALDEA 582
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 476-653 2.44e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  476 GENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQ-------------------------------A 524
Cdd:PLN03192   558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKifrilyhfasisdphaagdllctaakrndltA 637

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492  525 VSELLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLLMSGADplfrsdhgtcaLDEAK-DSSMETLLMKYIPQQKKCHL 603
Cdd:PLN03192   638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD-----------VDKANtDDDFSPTELRELLQKRELGH 706

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720375492  604 SAQRNSTDPAHVEDMfqnkkpKLSSNNYTEFICDENFDRQEPGHLEINKG 653
Cdd:PLN03192   707 SITIVDSVPADEPDL------GRDGGSRPGRLQGTSSDNQCRPRVSIYKG 750
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 541-568 2.51e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 2.51e-03
                            10        20
                    ....*....|....*....|....*...
gi 1720375492   541 YQITPLHDAVMNRHYKVAELLLMSGADP 568
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1167-1194 2.68e-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: 36.88  E-value: 2.68e-03
                           10        20
                   ....*....|....*....|....*....
gi 1720375492 1167 LHVAA-RGGNLSRVKVLIEARADVNLRDN 1194
Cdd:pfam00023    6 LHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 528-586 3.20e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 3.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720375492  528 LLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLLMSGADPLFRSDHGTCALDEAKDSS 586
Cdd:PHA02876   164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK 222
Ank_4 pfam13637
Ankyrin repeats (many copies);
1232-1269 3.35e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 3.35e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1720375492 1232 PLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEA 1269
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1162-1269 3.57e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1162 KGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASG-GFDDVIIELLQAGANVNCENIDGIVPLH-GASAG 1239
Cdd:PHA02876   239 KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYlMAKNG 318

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720375492 1240 NHLKAAEILLEHGANPNQKDQKQRTALDEA 1269
Cdd:PHA02876   319 YDTENIRTLIMLGADVNAADRLYITPLHQA 348
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 508-537 6.99e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 6.99e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1720375492   508 DGWTALHEASIGGYYQAVSELLKGGADVNV 537
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
496-547 7.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 7.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720375492  496 IKNG-ENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLH 547
Cdd:pfam13857    2 LEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1160-1253 8.48e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 8.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375492 1160 NKKGESQLHVAARGGN-LSRVKVLIEARADVNLRDNAGWTPLHKAASGGFD-DVIIELLQAGANVNCENIDGIVPLHGAs 1237
Cdd:PHA02876   405 SQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA- 483

                           90
                   ....*....|....*.
gi 1720375492 1238 AGNHlKAAEILLEHGA 1253
Cdd:PHA02876   484 LEYH-GIVNILLHYGA 498
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 508-537 9.50e-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: 35.31  E-value: 9.50e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720375492  508 DGWTALHEASIGGYYQAVSELLKGGADVNV 537
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
 
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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