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Conserved domains on  [gi|1237937713|ref|NP_001341265|]
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KN motif and ankyrin repeat domain-containing protein 1 isoform e [Homo sapiens]

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];
899-1067 2.17e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.26  E-value: 2.17e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  899 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKASQa 977
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  978 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1057
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 1237937713 1058 KDIAVLLYAH 1067
Cdd:COG0666    232 LEIVKLLLEA 241
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-338 2.50e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  111 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQRAasQINVCGVRKRSYSA--GNASQLEQLSRARRSGGELY 188
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA--ELEELREELEKLEKllQLLPLYQELEALEAELAELP 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  189 IDYEeeemetveQSTQRIKEFRQLTADMQALEQKIQdsscEASSELREngECRSVAVGAEENMNDIVvyhrgsrscKDAa 268
Cdd:COG4717    146 ERLE--------ELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EEL- 201

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  269 vgtlvemrncgvsvtEAMLGVMTEADKEIELQQQTIESLKEKIYRLEVQLRETTHDREMTKLKQELQAAG 338
Cdd:COG4717    202 ---------------EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
899-1067 2.17e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.26  E-value: 2.17e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  899 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKASQa 977
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  978 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1057
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 1237937713 1058 KDIAVLLYAH 1067
Cdd:COG0666    232 LEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
982-1067 1.14e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.14e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  982 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNghlEDNDGSTALSIALEAGHKDIA 1061
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*.
gi 1237937713 1062 VLLYAH 1067
Cdd:pfam12796   78 KLLLEK 83
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 888-1069 1.29e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  888 EAISPDVLRYVINL-ADGNGN-----TALHY-----SVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAAVEAEK 956
Cdd:PHA03100    44 EARNIDVVKILLDNgADINSStknnsTPLHYlsnikYNLTDVKEIVKLLLEYGA-NVNAPDNNGITPLLYAISKKSNSYS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  957 dmrIVEELFGCG-DVNAKASQaGQTALMLAVSHGRIDM------------------VKGLLACGADVNIQDDEGSTALMC 1017
Cdd:PHA03100   123 ---IVEYLLDNGaNVNIKNSD-GENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHY 198

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1237937713 1018 ASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGHKDI-AVLLYAHVN 1069
Cdd:PHA03100   199 AVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIfKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 906-1065 1.53e-06

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: 52.32  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  906 GNTALHYSVSHSNFEIVKLLLDADvcnvdhqnkagytPIMLaalaaveaekDMRIVEELFgcgdvnakasqAGQTALMLA 985
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA-------------PELV----------NEPMTSDLY-----------QGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  986 VSHGRIDMVKGLLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1051
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175

                          170
                   ....*....|....
gi 1237937713 1052 ALEAGHKDIAVLLY 1065
Cdd:cd22192    176 LVLQPNKTFACQMY 189
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 978-1006 3.67e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.67e-05
                            10        20
                    ....*....|....*....|....*....
gi 1237937713   978 GQTALMLAVSHGRIDMVKGLLACGADVNI 1006
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-338 2.50e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  111 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQRAasQINVCGVRKRSYSA--GNASQLEQLSRARRSGGELY 188
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA--ELEELREELEKLEKllQLLPLYQELEALEAELAELP 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  189 IDYEeeemetveQSTQRIKEFRQLTADMQALEQKIQdsscEASSELREngECRSVAVGAEENMNDIVvyhrgsrscKDAa 268
Cdd:COG4717    146 ERLE--------ELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EEL- 201

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  269 vgtlvemrncgvsvtEAMLGVMTEADKEIELQQQTIESLKEKIYRLEVQLRETTHDREMTKLKQELQAAG 338
Cdd:COG4717    202 ---------------EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 107-337 4.93e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  107 EQMAIALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQ--RAASQINVCGVRKRSYSAGNASQLEQLS--RARR 182
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlaRLEAEVEQLEERIAQLSKELTELEAEIEelEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  183 SGGELYIDYEEEEMETVEQSTQRIK-EFRQLTADMQALEQKIQDSSCEASSELRENGECRSVAVGAEENMNDIvvyHRGS 261
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL---EEQI 847

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237937713  262 RSCKDAAVGTLVEMRNCGVSVTEAMLGVmTEADKEIELQQQTIESLKEKIYRLEVQLREttHDREMTKLKQELQAA 337
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRE--LESKRSELRRELEEL 920
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
899-1067 2.17e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.26  E-value: 2.17e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  899 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKASQa 977
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  978 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1057
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 1237937713 1058 KDIAVLLYAH 1067
Cdd:COG0666    232 LEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
899-1064 2.55e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 2.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  899 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKaSQA 977
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAAN-----GNLEIVKLLLEAGaDVNAR-DND 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  978 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1057
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGA 264


                   ....*..
gi 1237937713 1058 KDIAVLL 1064
Cdd:COG0666    265 ALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
884-1067 1.35e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.61  E-value: 1.35e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  884 IAAFEAISPDVLRYVINLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEE 963
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAARN-----GDLEIVKL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  964 LFGCG-DVNAKASQaGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLED 1042
Cdd:COG0666    106 LLEAGaDVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARD 183

                          170       180
                   ....*....|....*....|....*
gi 1237937713 1043 NDGSTALSIALEAGHKDIAVLLYAH 1067
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
888-1079 2.54e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.35  E-value: 2.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  888 EAISPDVLRYVINLADGNGNTALHYSVSHSNFEIVKLLLDADVCNVDHQNKAGYTPIMLAALAAveaeKDMRIVEELFGC 967
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALA----GDLLVALLLLAA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  968 GDVNAKASQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGST 1047
Cdd:COG0666     77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNT 155

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1237937713 1048 ALSIALEAGHKDIAVLL---YAHVNfAKAQSPGTP 1079
Cdd:COG0666    156 PLHLAAANGNLEIVKLLleaGADVN-ARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
982-1067 1.14e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.14e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  982 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNghlEDNDGSTALSIALEAGHKDIA 1061
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*.
gi 1237937713 1062 VLLYAH 1067
Cdd:pfam12796   78 KLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
899-1032 1.50e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 1.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  899 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKaSQA 977
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAEN-----GHLEIVKLLLEAGaDVNAK-DND 218

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1237937713  978 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLA 1032
Cdd:COG0666    219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
Ank_2 pfam12796
Ankyrin repeats (3 copies);
910-1008 6.84e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 6.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  910 LHYSVSHSNFEIVKLLLDADvCNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCGDVNAKASqaGQTALMLAVSHG 989
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN-----GHLEIVKLLLEHADVNLKDN--GRTALHYAARSG 72

                           90
                   ....*....|....*....
gi 1237937713  990 RIDMVKGLLACGADVNIQD 1008
Cdd:pfam12796   73 HLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 888-1069 1.29e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  888 EAISPDVLRYVINL-ADGNGN-----TALHY-----SVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAAVEAEK 956
Cdd:PHA03100    44 EARNIDVVKILLDNgADINSStknnsTPLHYlsnikYNLTDVKEIVKLLLEYGA-NVNAPDNNGITPLLYAISKKSNSYS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  957 dmrIVEELFGCG-DVNAKASQaGQTALMLAVSHGRIDM------------------VKGLLACGADVNIQDDEGSTALMC 1017
Cdd:PHA03100   123 ---IVEYLLDNGaNVNIKNSD-GENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHY 198

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1237937713 1018 ASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGHKDI-AVLLYAHVN 1069
Cdd:PHA03100   199 AVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIfKLLLNNGPS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
980-1031 1.50e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.50e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1237937713  980 TALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1031
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 882-1063 2.49e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 2.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  882 DYIAAFEAISPDVLRYVI------NLADGNGNTALHYSVSHSN---FEIVKLLLDADVcNVDHQNKAGYTPIMLAALAAV 952
Cdd:PHA03095    17 DYLLNASNVTVEEVRRLLaagadvNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  953 EAekdmRIVEELFGCG-DVNAKaSQAGQTALMLAVSHGRID--MVKGLLACGADVNIQDDEGSTALMC--ASEHGHVEIV 1027
Cdd:PHA03095    96 TL----DVIKLLIKAGaDVNAK-DKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELL 170

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1237937713 1028 KLLLAQpGCNGHLEDNDGSTALSIALEAGHKDIAVL 1063
Cdd:PHA03095   171 RLLIDA-GADVYAVDDRFRSLLHHHLQSFKPRARIV 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 956-1078 1.60e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 1.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  956 KDMRIVEELFGCGDVNAKASQAGQtaLMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpG 1035
Cdd:PLN03192   505 HDLNVGDLLGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH-A 581

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1237937713 1036 CNGHLEDNDGSTALSIALEAGHKDIAVLLYahvNFAKAQSPGT 1078
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKIFRILY---HFASISDPHA 621
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 920-1069 4.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 4.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  920 EIVKLLLDADVcnvdhqnKAGYTPImlaalaaVEAEKDMriVEELFGCG-DVNAKASQAgQTALMLAVSHGRIDMVKGLL 998
Cdd:PHA02874    82 DIIKLLIDNGV-------DTSILPI-------PCIEKDM--IKTILDCGiDVNIKDAEL-KTFLHYAIKKGDLESIKMLF 144

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237937713  999 ACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAHVN 1069
Cdd:PHA02874   145 EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
997-1052 4.38e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 4.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237937713  997 LLACG-ADVNIQDDEGSTALMCASEHGHVEIVKLLLAqPGCNGHLEDNDGSTALSIA 1052
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1015-1069 4.42e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 4.42e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1237937713 1015 LMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAHVN 1069
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 899-1031 1.10e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  899 INLADGNGNTALHYSVSHSNFEIVKLLLDaDVCNVDHQNKAGYTPImlaaLAAVEAEKDMRIVEELFGCG-DVNAKASQA 977
Cdd:PHA02878   194 VNIPDKTNNSPLHHAVKHYNKPIVHILLE-NGASTDARDKCGNTPL----HISVGYCKDYDILKLLLEHGvDVNAKSYIL 268

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1237937713  978 GQTALMLAVSHGRIdmVKGLLACGADVNIQDDEGSTAL-MCASEHGHVEIVKLLL 1031
Cdd:PHA02878   269 GLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLsSAVKQYLCINIGRILI 321
Ank_5 pfam13857
Ankyrin repeats (many copies);
969-1015 2.66e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.66e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1237937713  969 DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTAL 1015
Cdd:pfam13857    8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 994-1067 2.71e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 2.71e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237937713  994 VKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAH 1067
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 900-1088 2.93e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 2.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  900 NLADGNGNTALHYSVSHSNFEIVKLLLDaDVCNVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCgdvnAKAS--QA 977
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNVHIRDANGNTALWNAISA-----KHHKIFRILYHF----ASISdpHA 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  978 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAqpgcNG------HLEDNDGSTALSI 1051
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM----NGadvdkaNTDDDFSPTELRE 697

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1237937713 1052 AL---EAGHKdIAVLLYAHVNFAKAQSPGTPRLGRKTSPG 1088
Cdd:PLN03192   698 LLqkrELGHS-ITIVDSVPADEPDLGRDGGSRPGRLQGTS 736
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 905-1033 1.20e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 1.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  905 NGNTALHYSVSHSNFEIVKLLL----DADVCNVDHqnkagYTPImlaalAAVEAEKDMRIVEELF---GCGDVNakaSQA 977
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIargaDPDIPNTDK-----FSPL-----HLAVMMGDIKGIELLIdhkACLDIE---DCC 167

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237937713  978 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMC-ASEHGHVEIVKLLLAQ 1033
Cdd:PHA02875   168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 906-1065 1.53e-06

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: 52.32  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  906 GNTALHYSVSHSNFEIVKLLLDADvcnvdhqnkagytPIMLaalaaveaekDMRIVEELFgcgdvnakasqAGQTALMLA 985
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA-------------PELV----------NEPMTSDLY-----------QGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  986 VSHGRIDMVKGLLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1051
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175

                          170
                   ....*....|....
gi 1237937713 1052 ALEAGHKDIAVLLY 1065
Cdd:cd22192    176 LVLQPNKTFACQMY 189
Ank_4 pfam13637
Ankyrin repeats (many copies);
1011-1064 2.99e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.99e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1237937713 1011 GSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1064
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 978-1009 3.82e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.59  E-value: 3.82e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1237937713  978 GQTALMLAVSH-GRIDMVKGLLACGADVNIQDD 1009
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
891-937 1.14e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 1.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1237937713  891 SPDVLRYVINLADGN----GNTALHYSVSHSNFEIVKLLLDADvCNVDHQN 937
Cdd:pfam12796   42 HLEIVKLLLEHADVNlkdnGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 899-1059 1.47e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  899 INLADGNGNTALHYSVSHSNFEIVKLLLDADV-CNVDHQNkaGYTPImlaalAAVEAEKDMRIVEELFGCGDVNAKASQA 977
Cdd:PHA02874   150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyANVKDNN--GESPL-----HNAAEYGDYACIKLLIDHGNHIMNKCKN 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  978 GQTALMLAVSHGRidMVKGLLACGADVNIQDDEGSTALMCASEHG-HVEIVKLLLAQPGcNGHLEDNDGSTALSIALEAG 1056
Cdd:PHA02874   223 GFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFKYI 299


                   ...
gi 1237937713 1057 HKD 1059
Cdd:PHA02874   300 NKD 302
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 978-1043 2.86e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.86e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237937713  978 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGHLEDN 1043
Cdd:PTZ00322   115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAN 180
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 910-1064 2.89e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  910 LHYSVSHSNFEIVKLLLDADVCNVDHQNKAGYTPImlaalAAVEAEKDMRIVEELFGCGDVNAKASQAGQTALMLAVSHG 989
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPL-----HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237937713  990 RIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1064
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 978-1006 3.67e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.67e-05
                            10        20
                    ....*....|....*....|....*....
gi 1237937713   978 GQTALMLAVSHGRIDMVKGLLACGADVNI 1006
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
899-926 4.72e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.72e-05
                           10        20
                   ....*....|....*....|....*...
gi 1237937713  899 INLADGNGNTALHYSVSHSNFEIVKLLL 926
Cdd:pfam13637   27 INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 908-1006 5.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 5.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  908 TALHYSVSHSNFEIVKLLLDADVCnVDHQNKAGYTPIMLAALAaveaeKDMRIVEELFGCG-DVNAKASQAGQTALMLAV 986
Cdd:PHA02875   137 SPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAK-----GDIAICKMLLDSGaNIDYFGKNGCVAALCYAI 210

                           90       100
                   ....*....|....*....|
gi 1237937713  987 SHGRIDMVKGLLACGADVNI 1006
Cdd:PHA02875   211 ENNKIDIVRLFIKRGADCNI 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 890-1033 1.03e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  890 ISPDVLRYVINL------ADGNGNTALHY--SVSHSNFEIVKLLLDADvCNVDHQNKAGYTPIMLAALAAVEAEKDMR-- 959
Cdd:PHA03095   165 ANVELLRLLIDAgadvyaVDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGSSCKRSLVLpl 243

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237937713  960 IVEELfgcgDVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQ 1033
Cdd:PHA03095   244 LIAGI----SINAR-NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 978-1006 1.65e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 1.65e-04
                           10        20
                   ....*....|....*....|....*....
gi 1237937713  978 GQTALMLAVSHGRIDMVKGLLACGADVNI 1006
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 905-938 1.88e-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: 39.58  E-value: 1.88e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1237937713  905 NGNTALHYSVSHS-NFEIVKLLLDADvCNVDHQNK 938
Cdd:pfam00023    1 DGNTPLHLAAGRRgNLEIVKLLLSKG-ADVNARDK 34
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-338 2.50e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  111 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQRAasQINVCGVRKRSYSA--GNASQLEQLSRARRSGGELY 188
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA--ELEELREELEKLEKllQLLPLYQELEALEAELAELP 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  189 IDYEeeemetveQSTQRIKEFRQLTADMQALEQKIQdsscEASSELREngECRSVAVGAEENMNDIVvyhrgsrscKDAa 268
Cdd:COG4717    146 ERLE--------ELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EEL- 201

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  269 vgtlvemrncgvsvtEAMLGVMTEADKEIELQQQTIESLKEKIYRLEVQLRETTHDREMTKLKQELQAAG 338
Cdd:COG4717    202 ---------------EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 907-1052 2.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  907 NTALHYSvshsNFEIVKLLLdadvcnVDHQNKAGYTPIMLAALAAVEAEKDMRIVEELFGCG-DVNAKASQAGQTALMLA 985
Cdd:PHA02878   106 KDAFNNR----NVEIFKIIL------TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGaDINMKDRHKGNTALHYA 175

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237937713  986 VSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIA 1052
Cdd:PHA02878   176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHIS 241
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 978-1049 4.36e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.36  E-value: 4.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  978 GQTALMLAVSHGRIDMVKGLLACGADVNIQ----------DDE----GSTALMCASEHGHVEIVKLLLAQPGCNGHLEDN 1043
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220


                   ....*.
gi 1237937713 1044 DGSTAL 1049
Cdd:cd22194    221 RGNTVL 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
899-944 6.04e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.04e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1237937713  899 INLADGNGNTALHYSVSHSNFEIVKLLLDADV-CNVdhQNKAGYTPI 944
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNL--KDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 905-930 7.78e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 7.78e-04
                            10        20
                    ....*....|....*....|....*.
gi 1237937713   905 NGNTALHYSVSHSNFEIVKLLLDADV 930
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 982-1067 8.35e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 8.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  982 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHV-----EIVKLLLaQPGCNGHLEDNDGSTALSIALEA- 1055
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLL-EYGANVNAPDNNGITPLLYAISKk 117

                           90
                   ....*....|...
gi 1237937713 1056 -GHKDIAVLLYAH 1067
Cdd:PHA03100   118 sNSYSIVEYLLDN 130
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 899-1053 8.95e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 8.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  899 INLADGNGNTALHYSVSHSNFEIVKLLLD--ADVcNVDHQNkaGYTPImlaalaaveaekdmriveelfgcgdvnakasq 976
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEygADV-NIEDDN--GCYPI-------------------------------- 161

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237937713  977 agqtalMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIAL 1053
Cdd:PHA02874   162 ------HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH-GNHIMNKCKNGFTPLHNAI 231
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1010-1031 1.79e-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: 36.80  E-value: 1.79e-03
                            10        20
                    ....*....|....*....|..
gi 1237937713  1010 EGSTALMCASEHGHVEIVKLLL 1031
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLL 22
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 957-1031 2.64e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 2.64e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237937713  957 DMRIVEELFGCG-DVNAKASQAgQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1031
Cdd:PHA02876   157 ELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 920-1069 3.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  920 EIVKLLLD--ADVCNVDHQNkaGYTPImlaalAAVEAEKDMRIVEELFGCG-DVNAkASQAGQTALMLAVSHGRIDMVKG 996
Cdd:PHA02878   148 EITKLLLSygADINMKDRHK--GNTAL-----HYATENKDQRLTELLLSYGaNVNI-PDKTNNSPLHHAVKHYNKPIVHI 219

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237937713  997 LLACGADVNIQDDEGSTALMCASEH-GHVEIVKLLLAQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLY-AHVN 1069
Cdd:PHA02878   220 LLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLKLLLEYgADIN 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
906-944 3.42e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 3.42e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1237937713  906 GNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPI 944
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETAL 38
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 107-337 4.93e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  107 EQMAIALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQ--RAASQINVCGVRKRSYSAGNASQLEQLS--RARR 182
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlaRLEAEVEQLEERIAQLSKELTELEAEIEelEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  183 SGGELYIDYEEEEMETVEQSTQRIK-EFRQLTADMQALEQKIQDSSCEASSELRENGECRSVAVGAEENMNDIvvyHRGS 261
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL---EEQI 847

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237937713  262 RSCKDAAVGTLVEMRNCGVSVTEAMLGVmTEADKEIELQQQTIESLKEKIYRLEVQLREttHDREMTKLKQELQAA 337
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRE--LESKRSELRRELEEL 920
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
107-337 5.29e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 5.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  107 EQMAIALKRLKELEEQVRTIPVLQVKISVLQEEKRQLVSQLKNQRAAsqinvcgVRKRSYSAGNASQLEQLSRARRSGGE 186
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE-------LEKLEKLLQLLPLYQELEALEAELAE 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  187 LYIDYeeeemetvEQSTQRIKEFRQLTADMQALEQKIQdsscEASSELREngECRSVAVGAEENMNDIVvyhrgsrscKD 266
Cdd:COG4717    144 LPERL--------EELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EE 200

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237937713  267 AAvgtlvemrncgvsvteamlgvmtEADKEIELQQQTIESLKEKIYRLEVQLRETTHDREMTKLKQELQAA 337
Cdd:COG4717    201 LE-----------------------ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-349 5.93e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 5.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  102 LQHIREQMAIALKRLKELEEQVRTIpvlQVKISVLQEEKRQLVSQLKN-QRAASQINVCGVRKRSYSAGNASQLEQLSRA 180
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASRKIGEI---EKEIEQLEQEEEKLKERLEElEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  181 ----RRSGGELYIDYEEEEMETVEQSTQRIKEFRQ-LTADMQALEQKIQDSSCEASSelrengecrsvavgAEENMNDIV 255
Cdd:TIGR02169  774 lhklEEALNDLEARLSHSRIPEIQAELSKLEEEVSrIEARLREIEQKLNRLTLEKEY--------------LEKEIQELQ 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237937713  256 VYhrgSRSCKD--AAVGTLVEMRNCGVSVTEAMLgvmteadKEIELQQQTIES----LKEKIYRLEVQLRETthDREMTK 329
Cdd:TIGR02169  840 EQ---RIDLKEqiKSIEKEIENLNGKKEELEEEL-------EELEAALRDLESrlgdLKKERDELEAQLREL--ERKIEE 907

                          250       260
                   ....*....|....*....|
gi 1237937713  330 LKQELQAAGSRKKVDKATMA 349
Cdd:TIGR02169  908 LEAQIEKKRKRLSELKAKLE 927
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1010-1043 5.94e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 5.94e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1237937713 1010 EGSTALMCASEH-GHVEIVKLLLaQPGCNGHLEDN 1043
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLL-SKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 905-930 8.76e-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: 34.93  E-value: 8.76e-03
                           10        20
                   ....*....|....*....|....*.
gi 1237937713  905 NGNTALHYSVSHSNFEIVKLLLDADV 930
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PHA02798 PHA02798
ankyrin-like protein; Provisional
 991-1063 9.55e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 9.55e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237937713  991 IDMVKGLLACGADVNIQDDEGSTALMCASEHGHV---EIVkLLLAQPGCNGHLEDNDGSTALSIALEAGHK-DIAVL 1063
Cdd:PHA02798    89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEIL-LFMIENGADTTLLDKDGFTMLQVYLQSNHHiDIEII 164
 
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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