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Conserved domains on  [gi|2462596386|ref|XP_054205612|]
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ankyrin repeat domain-containing protein 17 isoform X7 [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];
272-553 8.62e-60

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 208.27  E-value: 8.62e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  272 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 351
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  352 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 431
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  432 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 508
Cdd:COG0666    164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2462596386  509 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 553
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
738-1026 1.13e-56

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.02  E-value: 1.13e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  738 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 817
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  818 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 897
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  898 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 977
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462596386  978 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1026
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-352 2.02e-56

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.64  E-value: 2.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386   71 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 150
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  151 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 230
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  231 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 310
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462596386  311 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 352
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
1362-1432 7.58e-41

type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 (ANKRD17) and similar proteins; ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


:

Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 145.28  E-value: 7.58e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462596386 1362 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1432
Cdd:cd22502      1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
Ank_2 pfam12796
Ankyrin repeats (3 copies);
521-606 4.49e-15

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 4.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  521 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 600
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 2462596386  601 CYLLDY 606
Cdd:pfam12796   78 KLLLEK 83
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1718-1973 1.11e-08

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.55  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1718 PPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMT-------VPPLATSSAPVAVPSTAP 1790
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTpqssqsqVPPGPSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1791 VTYPMPQTPMGCP---QPTPK--METPAIRPPPhgtTAPHKNSASVQNssvavlsvnHIKRPH-SVPSSVQLPSTLSTQS 1864
Cdd:pfam03154  327 TPPSQSQLQSQQPpreQPLPPapLSMPHIKPPP---TTPIPQLPNPQS---------HKHPPHlSGPSPFQMNSNLPPPP 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1865 ACQN----------SVHPANKPIAPNfSAPLPFGPFS----TLFENSPTSAhafwggsvvsSQSTPESMLSGKSSYLPNs 1930
Cdd:pfam03154  395 ALKPlsslsthhppSAHPPPLQLMPQ-SQQLPPPPAQppvlTQSQSLPPPA----------ASHPPTSGLHQVPSQSPF- 462
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462596386 1931 dPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDSPyGSVTPSST 1973
Cdd:pfam03154  463 -PQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPP-SSASVSSS 503
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
718-746 1.11e-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: 38.34  E-value: 1.11e-03
                            10        20
                    ....*....|....*....|....*....
gi 2462596386   718 NHDTALTLACAGGHEELVQTLLERGASIE 746
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
272-553 8.62e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 208.27  E-value: 8.62e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  272 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 351
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  352 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 431
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  432 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 508
Cdd:COG0666    164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2462596386  509 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 553
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
738-1026 1.13e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.02  E-value: 1.13e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  738 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 817
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  818 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 897
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  898 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 977
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462596386  978 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1026
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-352 2.02e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.64  E-value: 2.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386   71 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 150
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  151 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 230
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  231 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 310
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462596386  311 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 352
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
1362-1432 7.58e-41

type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 (ANKRD17) and similar proteins; ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 145.28  E-value: 7.58e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462596386 1362 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1432
Cdd:cd22502      1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
733-1039 1.03e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 116.28  E-value: 1.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  733 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVG--VVEILLDNGADIEAQsERTKDTPL-SLACSGGRQEVVELLLAR 808
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  809 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPL--MLAAMNGHTAAVKLLLDMGSDINAqI 884
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLavLLKSRNANVELLRLLIDAGADVYA-V 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  885 ETNRNTALTLAC--FQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssrdtal 960
Cdd:PHA03095   184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA----------- 252
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386  961 tiaadkghykfcelligrgahidvRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVR 1039
Cdd:PHA03095   253 ------------------------RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
127-447 1.58e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.73  E-value: 1.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  127 EACSEGDVNAVRKLLIEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGIKGDiTPLMA-AANGGHVK 202
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  203 IVKLLLAHKADVNAQSSTGNTALtYACAGGY---VDVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLLLEN 276
Cdd:PHA03095    99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  277 GAGI-----------NTHSNEFKESAltlacykghlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 343
Cdd:PHA03095   177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  344 GAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQgaNINAQT-EETQE 422
Cdd:PHA03095   247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK--NPSAETvAATLN 324
                          330       340
                   ....*....|....*....|....*....
gi 2462596386  423 TA----LTLACCGGFLEVADFLIKAGADI 447
Cdd:PHA03095   325 TAsvagGDIPSDATRLCVAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
192-282 2.45e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 2.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  192 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASieDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 2462596386  272 LLLENGAGINT 282
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
455-546 4.02e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.26  E-value: 4.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  455 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHVCTVQ 534
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 2462596386  535 FLISKGANVNRT 546
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
858-949 5.35e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 5.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  858 LMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 937
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 2462596386  938 RVLLDKGADVNA 949
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
137-350 1.28e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  137 VRKLLIEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVeDRGIKGDITPLMAAANG--GHVKIVKLLLA 209
Cdd:PHA03100    51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV-NAPDNNGITPLLYAISKksNSYSIVEYLLD 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  210 HKADVNAQSSTGNTALTYACAGGYVDV------------------VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:PHA03100   130 NGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  272 LLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 343
Cdd:PHA03100   210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287

                   ....*..
gi 2462596386  344 GAQVNMP 350
Cdd:PHA03100   288 GFYKNRK 294
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1363-1427 4.39e-17

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 77.32  E-value: 4.39e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1427
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
521-606 4.49e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 4.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  521 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 600
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 2462596386  601 CYLLDY 606
Cdd:pfam12796   78 KLLLEK 83
KH smart00322
K homology RNA-binding domain;
1365-1429 2.89e-13

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 66.55  E-value: 2.89e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386  1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIP--GPGSEERVVEITGPPENVEKAAELILEIL 68
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
452-630 1.54e-11

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: 69.66  E-value: 1.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  452 STPLMEAAQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 525
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  526 RAGHVCTVQFLISKGANVN--RTTAN------------NDHtVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 591
Cdd:cd22192     98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462596386  592 AKGGHTSVVCYLLDYpnnLLSAPPPDvtQLTPPSHDLNR 630
Cdd:cd22192    177 VLQPNKTFACQMYDL---ILSYDKED--DLQPLDLVPNN 210
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
781-1010 1.99e-09

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: 62.72  E-value: 1.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  781 QSERTKDTPLSLACSGGRQEVVELLL--------ARGANKEhrnvsdyTPLSLAASGGYVNIIKILLNAGAE-INSRTGS 851
Cdd:cd22192     12 QQKRISESPLLLAAKENDVQAIKKLLkcpscdlfQRGALGE-------TALHVAALYDNLEAAVVLMEAAPElVNEPMTS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  852 KL--GISPLMLAAMNGHTAAVKLLLDMGSDINaqieTNRNTALtlaCFqgrtevvsllLDRKANV----EHraktgltPL 925
Cdd:cd22192     85 DLyqGETALHIAVVNQNLNLVRELIARGADVV----SPRATGT---FF----------RPGPKNLiyygEH-------PL 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  926 MEAASGGYAEVGRVLLDKGADVNAppvpssRD----TALTIAADKGHYKF-CE---LLIGRGAHID------VRNKKGNT 991
Cdd:cd22192    141 SFAACVGNEEIVRLLIEHGADIRA------QDslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLT 214
                          250
                   ....*....|....*....
gi 2462596386  992 PLWLAANGGHLDVVQLLVQ 1010
Cdd:cd22192    215 PFKLAAKEGNIVMFQHLVQ 233
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1718-1973 1.11e-08

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.55  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1718 PPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMT-------VPPLATSSAPVAVPSTAP 1790
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTpqssqsqVPPGPSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1791 VTYPMPQTPMGCP---QPTPK--METPAIRPPPhgtTAPHKNSASVQNssvavlsvnHIKRPH-SVPSSVQLPSTLSTQS 1864
Cdd:pfam03154  327 TPPSQSQLQSQQPpreQPLPPapLSMPHIKPPP---TTPIPQLPNPQS---------HKHPPHlSGPSPFQMNSNLPPPP 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1865 ACQN----------SVHPANKPIAPNfSAPLPFGPFS----TLFENSPTSAhafwggsvvsSQSTPESMLSGKSSYLPNs 1930
Cdd:pfam03154  395 ALKPlsslsthhppSAHPPPLQLMPQ-SQQLPPPPAQppvlTQSQSLPPPA----------ASHPPTSGLHQVPSQSPF- 462
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462596386 1931 dPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDSPyGSVTPSST 1973
Cdd:pfam03154  463 -PQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPP-SSASVSSS 503
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
125-308 2.34e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.17  E-value: 2.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  125 LAEACSEGDVNAVRKLLiEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDI----TPLMAAANG 198
Cdd:cd22192     21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLyqgeTALHIAVVN 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  199 GHVKIVKLLLAHKADVNAQSST--------------GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL----ME 260
Cdd:cd22192    100 QNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvLQ 179
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462596386  261 AGSAGHVEVARLLLENGAGINTHS-----NEFKESALTLACYKGHLEMVRFLL 308
Cdd:cd22192    180 PNKTFACQMYDLILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
705-941 9.15e-07

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: 54.32  E-value: 9.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  705 IYPAIDIDaqtESNHDTALTLACAGGHEELVQTLLERGAS--IEHRDKKGFTPLILAATAG-HVGVVEILLDNGADIEaq 781
Cdd:TIGR00870    6 IVPAEESP---LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  782 serTKDTPLsLACSGGRQEVVELLLA-------RGANKEHRNVS-------DYTPLSLAASGGYVNIIKILLNAGAEINS 847
Cdd:TIGR00870   81 ---VGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  848 R------------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIE---------------TNRNTALTLACFQgr 900
Cdd:TIGR00870  157 RacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSlgntllhllvmenefKAEYEELSCQMYN-- 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2462596386  901 tEVVSLL--LDRKANVEH-RAKTGLTPLMEAASGGYAEVGRVLL 941
Cdd:TIGR00870  235 -FALSLLdkLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
521-625 1.93e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  521 LMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVV 600
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                           90       100
                   ....*....|....*....|....*...
gi 2462596386  601 CYLLDYPNNLLSA---PPPDVTQLTPPS 625
Cdd:PTZ00322   165 QLLSRHSQCHFELganAKPDSFTGKPPS 192
PHA03247 PHA03247
large tegument protein UL36; Provisional
1661-2093 2.53e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1661 TNATYPMPTAKEHYPVSSPSSPSPPAQPGGVSRNSPLDcGSASPNKVASSSeqeaGSPPVVETTNTRPPNSSSSSGSSSA 1740
Cdd:PHA03247  2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRL----GRAAQASSPPQRPRRRAARPTVGSL 2695
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1741 HSNQQQPPGSVSQEPRPPLQQSQVPPPEV----RMTVPPLATSSAPVAVPST-----APVTYPMPQTPMGCPQPTPKMET 1811
Cdd:PHA03247  2696 TSLADPPPPPPTPEPAPHALVSATPLPPGpaaaRQASPALPAAPAPPAVPAGpatpgGPARPARPPTTAGPPAPAPPAAP 2775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1812 PAirPPPHGTTAPHKNSASVQNSSVAVLSvnhikRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIAPNfSAPLPFGPFS 1891
Cdd:PHA03247  2776 AA--GPPRRLTRPAVASLSESRESLPSPW-----DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT-APPPPPGPPP 2847
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1892 TlfensPTSAhafwGGSVVssqstPESMLSGKSsylpnsdPLHQSDTSKAPGFRPP---LQRPAPSPSGIVNMDSPYGSV 1968
Cdd:PHA03247  2848 P-----SLPL----GGSVA-----PGGDVRRRP-------PSRSPAAKPAAPARPPvrrLARPAVSRSTESFALPPDQPE 2906
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1969 TPssthlgnfasnisggqmygpgaplggapaaanfnRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSP-APSSVPLGS 2047
Cdd:PHA03247  2907 RP----------------------------------PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPlAPTTDPAGA 2952
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2462596386 2048 EKPSNVSQDRKVPVPIGTERSARIRQTGTSAPSVIGSNLSTSVGHS 2093
Cdd:PHA03247  2953 GEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTG 2998
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
988-1017 1.04e-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: 44.12  E-value: 1.04e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2462596386   988 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1017
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
386-415 1.08e-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: 44.12  E-value: 1.08e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2462596386   386 EGYTPLMEAAREGHEEMVALLLGQGANINA 415
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
123-376 2.66e-05

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: 49.69  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  123 RSLAEACSEGDVNAVRKLLIEGRSVNEHTEE--GESLLCLACSAG-YYELAQVLLamhaNVEDRGIKGDiTPLMAAANGg 199
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLL----NLSCRGAVGD-TLLHAISLE- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  200 HVKIVKLLLAHKADvnAQSSTGNTALTYACAGG--YVDvvkvllesgasiedhnengHTPLMEAGSAGHVEVARLLLENG 277
Cdd:TIGR00870   93 YVDAVEAILLHLLA--AFRKSGPLELANDQYTSefTPG-------------------ITALHLAAHRQNYEIVKLLLERG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  278 AGINT--HSNEFKESALT---------LACYK--GHLEMVRFLLEAGADQEhKTDEM-----HTALMEA----------- 328
Cdd:TIGR00870  152 ASVPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelsc 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462596386  329 -CMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 376
Cdd:TIGR00870  231 qMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
228-381 4.61e-05

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: 48.54  E-value: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  228 ACAGGYVDVVKVLLESGAS--IEDHNENGHTPLMEAGSAG-HVEVARLLLENGAGINThsnefKESALTLAC--YKGHLE 302
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV-----GDTLLHAISleYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  303 MVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ESP 357
Cdd:TIGR00870   99 AILLHLLAAFRKsgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgESP 178
                          170       180
                   ....*....|....*....|....
gi 2462596386  358 LTLAACGGHVELAALLIERGASLE 381
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADIL 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
221-249 1.74e-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: 40.65  E-value: 1.74e-04
                            10        20
                    ....*....|....*....|....*....
gi 2462596386   221 GNTALTYACAGGYVDVVKVLLESGASIED 249
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
1362-1438 2.91e-04

Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 46.15  E-value: 2.91e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386 1362 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqkDktgDRIITIrGGT--ESTRQATQLINALIKDPdkEIDE 1438
Cdd:COG1185    549 RIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIE---D---DGTVKI-AATdgEAAEKAIERIEGITAEP--EVGE 618
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
1362-1438 3.88e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.81  E-value: 3.88e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386 1362 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDPdkEIDE 1438
Cdd:PRK11824   554 RIETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIED------DGTVKIAATDgEAAEAAKERIEGITAEP--EVGE 623
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
718-746 1.11e-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: 38.34  E-value: 1.11e-03
                            10        20
                    ....*....|....*....|....*....
gi 2462596386   718 NHDTALTLACAGGHEELVQTLLERGASIE 746
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
718-750 1.44e-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: 1.44e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462596386  718 NHDTALTLACA-GGHEELVQTLLERGASIEHRDK 750
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
SCS2 COG5066
VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and ...
1712-1818 8.15e-03

VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and secretion];


Pssm-ID: 227398 [Multi-domain]  Cd Length: 242  Bit Score: 40.33  E-value: 8.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1712 EQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPV 1791
Cdd:COG5066    121 SEEEISKNVHECSEDRGAAVLLVEMPTLLNILYLEVRFFVNQKEVPAEPETQPPVQVKKEEVPPVTQKTVPHENEKQTSV 200
                           90       100
                   ....*....|....*....|....*..
gi 2462596386 1792 TYPMPQTPMGCPQPTPKmETPAIRPPP 1818
Cdd:COG5066    201 STPKPQNQIKEAATVPA-ENEPSSMPI 226
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
272-553 8.62e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 208.27  E-value: 8.62e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  272 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 351
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  352 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 431
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  432 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 508
Cdd:COG0666    164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2462596386  509 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 553
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
301-586 2.51e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 206.73  E-value: 2.51e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  301 LEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASL 380
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  381 EEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLIKAGADIEL---GCSTPLME 457
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAqdnDGNTPLHL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  458 AAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLI 537
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462596386  538 SKGANVNRtTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGST 586
Cdd:COG0666    240 EAGADLNA-KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
738-1026 1.13e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.02  E-value: 1.13e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  738 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 817
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  818 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 897
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  898 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 977
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462596386  978 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1026
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-352 2.02e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.64  E-value: 2.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386   71 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 150
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  151 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 230
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  231 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 310
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462596386  311 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 352
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
234-521 2.44e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.25  E-value: 2.44e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  234 VDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFkESALTLACYKGHLEMVRFLLEAGAD 313
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALG-ALLLLAAALAGDLLVALLLLAAGAD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  314 QEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLME 393
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  394 AAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYL 470
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNdgkTALDLAAENGNLEIVKLL 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462596386  471 LAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPL 521
Cdd:COG0666    239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
201-488 2.11e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.56  E-value: 2.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  201 VKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGI 280
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  281 NThSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 360
Cdd:COG0666     81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  361 AACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFL 440
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462596386  441 IKAGADIELGC---STPLMEAAQEGHLELVKYLLAAGANVHATTATGDTAL 488
Cdd:COG0666    239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
701-949 2.10e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.48  E-value: 2.10e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  701 AMLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEA 780
Cdd:COG0666     36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  781 QSERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLML 860
Cdd:COG0666    116 RDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR--DNDGETPLHL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  861 AAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVL 940
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271

                   ....*....
gi 2462596386  941 LDKGADVNA 949
Cdd:COG0666    272 LLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
702-993 8.73e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.94  E-value: 8.73e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  702 MLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQ 781
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  782 SERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLA 861
Cdd:COG0666     84 DDG-GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  862 AMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 941
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  942 DKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPL 993
Cdd:COG0666    240 EAGADLNAK--DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
40-325 1.96e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.53  E-value: 1.96e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386   40 LLLSGTADGADLRTVDPETQARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQ 119
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  120 SDNRSLAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGG 199
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  200 HVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAG 279
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2462596386  280 INtHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTAL 325
Cdd:COG0666    245 LN-AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
834-1043 1.28e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.36  E-value: 1.28e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  834 IIKILLNAGAEINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKAN 913
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADA-LGALLLLAAALAGDLLVALLLLAAGAD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  914 VEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPL 993
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA--RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462596386  994 WLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVK 1043
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
433-846 5.65e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.73  E-value: 5.65e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  433 FLEVADFLIKAGADIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEH 512
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  513 ESEGGRTPLMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGstmlieaa 592
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG-------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  593 kgghtsvvcylldypnnllsapppdvtqltppshdlnraprvpvqalpmvvppqepdkppanvattlpirnkavsgrasa 672
Cdd:COG0666        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  673 msntpthsiaasisqpqtptpspiispsamlpiypaididaqtesnhDTALTLACAGGHEELVQTLLERGASIEHRDKKG 752
Cdd:COG0666    154 -----------------------------------------------NTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  753 FTPLILAATAGHVGVVEILLDNGADIEAQSERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYV 832
Cdd:COG0666    187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
                          410
                   ....*....|....
gi 2462596386  833 NIIKILLNAGAEIN 846
Cdd:COG0666    266 LIVKLLLLALLLLA 279
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
1362-1432 7.58e-41

type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 (ANKRD17) and similar proteins; ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 145.28  E-value: 7.58e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462596386 1362 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1432
Cdd:cd22502      1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
KH-I_ANKHD1 cd22503
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ...
1362-1443 1.58e-37

type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing protein 1 (ANKHD1) and similar proteins; ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. It acts as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. It may play might have a role in MM cell proliferation and cell cycle progression by regulating expression of p21. It also regulates cell cycle progression and proliferation in multiple myeloma cells. ANKHD1 is a component of Hippo signaling pathway. It functions as a positive regulator of YAP1 and promotes cell growth and cell cycle progression through Cyclin A upregulation in prostate cancer cells.


Pssm-ID: 411931  Cd Length: 83  Bit Score: 136.42  E-value: 1.58e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1362 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDKEIDELIP 1441
Cdd:cd22503      1 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIP 80

                   ..
gi 2462596386 1442 KN 1443
Cdd:cd22503     81 RN 82
KH-I_MASK cd22404
type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family ...
1362-1432 4.40e-37

type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family includes Drosophila melanogaster ankyrin repeat and KH domain-containing protein Mask, and its mammalian homologues Mask1/ANKHD1 and Mask2/ANKRD17. Mask, also called multiple ankyrin repeat single KH domain-containing protein, is a large ankyrin repeat and KH domain-containing protein involved in Drosophila receptor tyrosine kinase signaling. It acts as a mediator of receptor tyrosine kinase (RTK) signaling and may act either downstream of MAPK or transduce signaling through a parallel branch of the RTK pathway. Mask is required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere. Mask1/ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. Mask2/ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411832 [Multi-domain]  Cd Length: 71  Bit Score: 134.65  E-value: 4.40e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462596386 1362 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1432
Cdd:cd22404      1 KSKKVTVPNSAISRVIGRGGCNINAIREVSGAHIEIDKQKGEQGDRRITIKGSADATRQAAQLINALIKDP 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
733-1039 1.03e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 116.28  E-value: 1.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  733 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVG--VVEILLDNGADIEAQsERTKDTPL-SLACSGGRQEVVELLLAR 808
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  809 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPL--MLAAMNGHTAAVKLLLDMGSDINAqI 884
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLavLLKSRNANVELLRLLIDAGADVYA-V 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  885 ETNRNTALTLAC--FQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssrdtal 960
Cdd:PHA03095   184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA----------- 252
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386  961 tiaadkghykfcelligrgahidvRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVR 1039
Cdd:PHA03095   253 ------------------------RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
788-1074 2.82e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.38  E-value: 2.82e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  788 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYV-----NIIKILLNAGAEINSrtGSKLGISPLMLAA 862
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA--PDNNGITPLLYAI 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  863 MN--GHTAAVKLLLDMGSDINAqietnrntaltlacfqgrtevvsllldrkanvehRAKTGLTPLMEAASGGYA--EVGR 938
Cdd:PHA03100   115 SKksNSYSIVEYLLDNGANVNI----------------------------------KNSDGENLLHLYLESNKIdlKILK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  939 VLLDKGADVNAppvpssrdtaltiaADKghykfCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAA 1018
Cdd:PHA03100   161 LLIDKGVDINA--------------KNR-----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462596386 1019 DNRKITPLMAAFRKGHVKVVRYLvkeVNQFPSDS---ECMRY-----IATITDKEMLKKCHLCM 1074
Cdd:PHA03100   222 NKYGDTPLHIAILNNNKEIFKLL---LNNGPSIKtiiETLLYfkdkdLNTITKIKMLKKSIMYM 282
PHA03095 PHA03095
ankyrin-like protein; Provisional
127-447 1.58e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.73  E-value: 1.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  127 EACSEGDVNAVRKLLIEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGIKGDiTPLMA-AANGGHVK 202
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  203 IVKLLLAHKADVNAQSSTGNTALtYACAGGY---VDVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLLLEN 276
Cdd:PHA03095    99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  277 GAGI-----------NTHSNEFKESAltlacykghlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 343
Cdd:PHA03095   177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  344 GAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQgaNINAQT-EETQE 422
Cdd:PHA03095   247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK--NPSAETvAATLN 324
                          330       340
                   ....*....|....*....|....*....
gi 2462596386  423 TA----LTLACCGGFLEVADFLIKAGADI 447
Cdd:PHA03095   325 TAsvagGDIPSDATRLCVAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
192-282 2.45e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 2.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  192 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASieDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 2462596386  272 LLLENGAGINT 282
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
455-546 4.02e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.26  E-value: 4.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  455 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHVCTVQ 534
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 2462596386  535 FLISKGANVNRT 546
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
334-512 6.10e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 107.06  E-value: 6.10e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  334 VEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-----ELAALLIERGASLEEVNDEGYTPLMEAARE--GHEEMVALL 406
Cdd:PHA03100    48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  407 LGQGANINAQTEeTQETALTLA--CCGGFLEVADFLIKAGADI----------ELGC---------STPLMEAAQEGHLE 465
Cdd:PHA03100   128 LDNGANVNIKNS-DGENLLHLYleSNKIDLKILKLLIDKGVDInaknrvnyllSYGVpinikdvygFTPLHYAVYNNNPE 206
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462596386  466 LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEH 512
Cdd:PHA03100   207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
325-416 5.10e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 5.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  325 LMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASleEVNDEGYTPLMEAAREGHEEMVA 404
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 2462596386  405 LLLGQGANINAQ 416
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
858-949 5.35e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 5.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  858 LMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 937
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 2462596386  938 RVLLDKGADVNA 949
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
283-591 6.81e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 101.64  E-value: 6.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  283 HSNEFKESAL---TLACYKGHLEMVRFLLEAGADQEHK----TDEMHTALMEACMDGhVEVARLLLDSGAQVNMPADSFE 355
Cdd:PHA03095     6 SVDIIMEAALydyLLNASNVTVEEVRRLLAAGADVNFRgeygKTPLHLYLHYSSEKV-KDIVRLLLEAGADVNAPERCGF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  356 SPLTLAACGGHVE-LAALLIERGASLEEVNDEGYTPLMEAAR--EGHEEMVALLLGQGANINAqTEETQETALtlaccgg 432
Cdd:PHA03095    85 TPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNA-LDLYGMTPL------- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  433 flevADFLIKAGADIELgcstplmeaaqeghlelVKYLLAAGANVHATTATGDTALTYACENGHTDVADV--LLQAGADL 510
Cdd:PHA03095   157 ----AVLLKSRNANVEL-----------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDP 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  511 EHESEGGRTPLMKAArAGHVCT---VQFLISKGANVNRTTaNNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTM 587
Cdd:PHA03095   216 AATDMLGNTPLHSMA-TGSSCKrslVLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                   ....
gi 2462596386  588 LIEA 591
Cdd:PHA03095   294 LSLM 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
125-510 1.06e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 102.83  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  125 LAEACSEGDV--NAVRKLLIEGRSVNEHTEEGESLLclacsagyyelAQVLLAMHANVEDRGIKGdITPLMAAANGGHVK 202
Cdd:PHA02876   125 LKEAISGNDIhyDKINESIEYMKLIKERIQQDELLI-----------AEMLLEGGADVNAKDIYC-ITPIHYAAERGNAK 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  203 IVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIedhNENGHTpLMEAGSAGHVEVARLLLENGAGINT 282
Cdd:PHA02876   193 MVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI---NKNDLS-LLKAIRNEDLETSLLLYDAGFSVNS 268
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  283 hSNEFKESALTLACYKGHL-EMVRFLLEAGADQEHKTDEMHTALMEACMDGH-VEVARLLLDSGAQVNMPADSFESPLTL 360
Cdd:PHA02876   269 -IDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQ 347
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  361 AAC-GGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQeTALTLACCGG--FLEVA 437
Cdd:PHA02876   348 ASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTnpYMSVK 426
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386  438 DfLIKAGADIELG---CSTPLMEAAQEG-HLELVKYLLAAGANVHATTATGDTALTYACenGHTDVADVLLQAGADL 510
Cdd:PHA02876   427 T-LIDRGANVNSKnkdLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
225-317 4.09e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 4.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  225 LTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENgagINTHSNEFKESALTLACYKGHLEMV 304
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 2462596386  305 RFLLEAGADQEHK 317
Cdd:pfam12796   78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
258-348 6.98e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 6.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  258 LMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEaGADQEHKTDEMhTALMEACMDGHVEVA 337
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIV 77
                           90
                   ....*....|.
gi 2462596386  338 RLLLDSGAQVN 348
Cdd:pfam12796   78 KLLLEKGADIN 88
PHA03100 PHA03100
ankyrin repeat protein; Provisional
176-415 9.45e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 9.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  176 MHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYV-----DVVKVLLESGASIEDH 250
Cdd:PHA03100    23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  251 NENGHTPLMEAGSA--GHVEVARLLLENGAGINTHSNEFKES-ALTLACYKGHLEMVRFLLEAGADQEHKTDemhtalme 327
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLlHLYLESNKIDLKILKLLIDKGVDINAKNR-------- 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  328 acmdghVEvarLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLL 407
Cdd:PHA03100   175 ------VN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245

                   ....*...
gi 2462596386  408 GQGANINA 415
Cdd:PHA03100   246 NNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
734-1030 1.30e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 98.98  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  734 LVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIE------------AQSERTKDT------------- 788
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvlecAVDSKNIDTikaiidnrsnink 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  789 -PLSL--ACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVN-IIKILLNAGAEINSRTGSklGISPLMLAAMN 864
Cdd:PHA02876   240 nDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK--GETPLYLMAKN 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  865 GH-TAAVKLLLDMGSDINAQiETNRNTALTLACFQGR-TEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLD 942
Cdd:PHA02876   318 GYdTENIRTLIMLGADVNAA-DRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  943 KGADVNAppVPSSRDTALTIA-ADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAA-NGGHLDVVQLLVQAGADVDAADN 1020
Cdd:PHA02876   397 YGADIEA--LSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINI 474
                          330
                   ....*....|
gi 2462596386 1021 RKITPLMAAF 1030
Cdd:PHA02876   475 QNQYPLLIAL 484
Ank_2 pfam12796
Ankyrin repeats (3 copies);
823-917 2.18e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 2.18e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  823 LSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHTAAVKLLLDMgsdINAQIETNRNTALTLACFQGRTE 902
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*
gi 2462596386  903 VVSLLLDRKANVEHR 917
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
732-916 2.47e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 2.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  732 EELVQTLLERGASIEHRDKKGFTPLILAATAGHV-----GVVEILLDNGADIEAQSERTkDTPLSLACSGGRQ--EVVEL 804
Cdd:PHA03100    48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG-ITPLLYAISKKSNsySIVEY 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  805 LLARGANKEHRNVSDYTPLSLAASGGYV--NIIKILLNAGAEINSRT--------GSKL------GISPLMLAAMNGHTA 868
Cdd:PHA03100   127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNrvnyllsyGVPInikdvyGFTPLHYAVYNNNPE 206
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462596386  869 AVKLLLDMGSDINAqIETNRNTALTLACFQGRTEVVSLLLDRKANVEH 916
Cdd:PHA03100   207 FVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
391-480 5.60e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 5.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  391 LMEAAREGHEEMVALLLGQGANINAQTEETQeTALTLACCGGFLEVADFLI-KAGADIELGCSTPLMEAAQEGHLELVKY 469
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLLeHADVNLKDNGRTALHYAARSGHLEIVKL 79
                           90
                   ....*....|.
gi 2462596386  470 LLAAGANVHAT 480
Cdd:pfam12796   80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
488-580 6.41e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 6.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  488 LTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKgANVNRTtaNNDHTVLSLACAGGHLAVV 567
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK--DNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 2462596386  568 ELLLAHGADPTHR 580
Cdd:pfam12796   78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
790-883 1.51e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  790 LSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNaGAEINSRTGsklGISPLMLAAMNGHTAA 869
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN---GRTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 2462596386  870 VKLLLDMGSDINAQ 883
Cdd:pfam12796   77 VKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
733-886 1.54e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.96  E-value: 1.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  733 ELVQTLLERGASIEHRDKKGFTPLILAATA--GHVGVVEILLDNGADIEAQSERTKdTPLSLACSGGRQ--EVVELLLAR 808
Cdd:PHA03100    87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKIdlKILKLLIDK 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  809 GA--NKEHR--------------NVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHTAAVKL 872
Cdd:PHA03100   166 GVdiNAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN--KYGDTPLHIAILNNNKEIFKL 243
                          170
                   ....*....|....
gi 2462596386  873 LLDMGSDINAQIET 886
Cdd:PHA03100   244 LLNNGPSIKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
199-521 1.69e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.87  E-value: 1.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  199 GHVKIVKLLLAHKAD-VNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENG 277
Cdd:PHA02874    12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  278 agINThsnefkeSALTLACYKGhlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 357
Cdd:PHA02874    92 --VDT-------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  358 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQteetqetaltlaCCGGFleva 437
Cdd:PHA02874   161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK------------CKNGF---- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  438 dflikagadielgcsTPLMEAAQegHLELVKYLLAAGANVHATTATGDTALTYA----CEnghTDVADVLLQAGADLEHE 513
Cdd:PHA02874   225 ---------------TPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADISIK 284

                   ....*...
gi 2462596386  514 SEGGRTPL 521
Cdd:PHA02874   285 DNKGENPI 292
Ank_2 pfam12796
Ankyrin repeats (3 copies);
723-816 1.83e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  723 LTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNgADIEAQSErtKDTPLSLACSGGRQEVV 802
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 2462596386  803 ELLLARGANKEHRN 816
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
233-539 1.94e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 1.94e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  233 YVDVVKVLLESGASIEDHNENGHTPL---MEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLE 309
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  310 AGADQEHKTDEMHTALmEACMDG---HVEVARLLLDSGAQVNmpaDSFESPLTLAAC-----GGHVELAALLIERGASLE 381
Cdd:PHA03095   106 AGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVN---ALDLYGMTPLAVllksrNANVELLRLLIDAGADVY 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  382 EVNDEGYTPLmeaaregheemvalllgqgaNINAQTEETQETaltlaccggfleVADFLIKAGAD---IELGCSTPLMEA 458
Cdd:PHA03095   182 AVDDRFRSLL--------------------HHHLQSFKPRAR------------IVRELIRAGCDpaaTDMLGNTPLHSM 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  459 AQEGHLE--LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFL 536
Cdd:PHA03095   230 ATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309

                   ...
gi 2462596386  537 ISK 539
Cdd:PHA03095   310 LAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
358-449 4.85e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 4.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  358 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLgQGANINAQTEetQETALTLACCGGFLEVA 437
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN--GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 2462596386  438 DFLIKAGADIEL 449
Cdd:pfam12796   78 KLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
960-1043 9.32e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 9.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  960 LTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQaGADVDAADNRKiTPLMAAFRKGHVKVVR 1039
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVK 78

                   ....
gi 2462596386 1040 YLVK 1043
Cdd:pfam12796   79 LLLE 82
PHA02876 PHA02876
ankyrin repeat protein; Provisional
236-606 9.83e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 93.20  E-value: 9.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  236 VVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEfKESALTLACYKGHLEMVRFLLeagaDQE 315
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAII----DNR 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  316 HKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-ELAALLIERGASLEEVNDEGYTPLMEA 394
Cdd:PHA02876   235 SNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLM 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  395 AREGHE-EMVALLLGQGANINAqteetqetaltlaccggflevADFLIkagadielgcSTPLMEAAQ-EGHLELVKYLLA 472
Cdd:PHA02876   315 AKNGYDtENIRTLIMLGADVNA---------------------ADRLY----------ITPLHQASTlDRNKDIVITLLE 363
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  473 AGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGH-VCTVQFLISKGANVNrtTANND 551
Cdd:PHA02876   364 LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVN--SKNKD 441
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  552 -HTVLSLACAGG-HLAVVELLLAHGADPTH-RLKDGSTMLIEAakgGHTSVVCYLLDY 606
Cdd:PHA02876   442 lSTPLHYACKKNcKLDVIEMLLDNGADVNAiNIQNQYPLLIAL---EYHGIVNILLHY 496
PHA03100 PHA03100
ankyrin repeat protein; Provisional
137-350 1.28e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  137 VRKLLIEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVeDRGIKGDITPLMAAANG--GHVKIVKLLLA 209
Cdd:PHA03100    51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV-NAPDNNGITPLLYAISKksNSYSIVEYLLD 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  210 HKADVNAQSSTGNTALTYACAGGYVDV------------------VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:PHA03100   130 NGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  272 LLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 343
Cdd:PHA03100   210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287

                   ....*..
gi 2462596386  344 GAQVNMP 350
Cdd:PHA03100   288 GFYKNRK 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
440-793 1.43e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 1.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  440 LIKAGADI----ELGCsTPL---MEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHT-DVADVLLQAGADLE 511
Cdd:PHA03095    33 LLAAGADVnfrgEYGK-TPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVN 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  512 HESEGGRTPLmkaaragHVC---------TVQFLISKGANVNrttANNDHTVLSLAC----AGGHLAVVELLLAHGADPT 578
Cdd:PHA03095   112 AKDKVGRTPL-------HVYlsgfninpkVIRLLLRKGADVN---ALDLYGMTPLAVllksRNANVELLRLLIDAGADVY 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  579 HRLKDGSTMLieaakggHtsvvcYLLDYPnnllsapppdvtqltppshdlnraprvpvqalpmvvppqepdKPPANVATT 658
Cdd:PHA03095   182 AVDDRFRSLL-------H-----HHLQSF------------------------------------------KPRARIVRE 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  659 LPIRNKAVSGRaSAMSNTPTHSIAASISqpqtptpspiispsamlpiypaididaqtesnhdtaltlaCAGGheeLVQTL 738
Cdd:PHA03095   208 LIRAGCDPAAT-DMLGNTPLHSMATGSS----------------------------------------CKRS---LVLPL 243
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386  739 LERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSErTKDTPLSLA 793
Cdd:PHA03095   244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
925-1019 1.99e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 1.99e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  925 LMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIgrgAHIDVRNK-KGNTPLWLAANGGHLD 1003
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANL--QDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKdNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 2462596386 1004 VVQLLVQAGADVDAAD 1019
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-258 3.84e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 3.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386    5 AAEMEAYVLEDILEVESFILDQDDLENPMLETAS--------KLLLsgtADGADLRTVDPETQArleALLEAAGIGklst 76
Cdd:COG0666     62 ALAGDLLVALLLLAAGADINAKDDGGNTLLHAAArngdleivKLLL---EAGADVNARDKDGET---PLHLAAYNG---- 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386   77 adgkafaDPEVLRRLtssvscaLDEAAAALTRMRAESTAnagqsdnrsLAEACSEGDVNAVRKLLIEGRSVNEHTEEGES 156
Cdd:COG0666    132 -------NLEIVKLL-------LEAGADVNAQDNDGNTP---------LHLAAANGNLEIVKLLLEAGADVNARDNDGET 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  157 LLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDV 236
Cdd:COG0666    189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
                          250       260
                   ....*....|....*....|..
gi 2462596386  237 VKVLLESGASIEDHNENGHTPL 258
Cdd:COG0666    268 VKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
709-952 4.88e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.70  E-value: 4.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  709 IDIDAqTESNHDTAL-TLACAGGHEELVQTLLERGASIEHRDKKGFTPL--ILAATAGHVGVVEILLDNGADIEAQSERT 785
Cdd:PHA03095    74 ADVNA-PERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYG 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  786 KdTPLS--------------LACSGG-----------------------RQEVVELLLARGANKEHRNVSDYTPLSLAAS 828
Cdd:PHA03095   153 M-TPLAvllksrnanvellrLLIDAGadvyavddrfrsllhhhlqsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMAT 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  829 GGYVNIIKI--LLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrNTALTLACFQGRTEVVSL 906
Cdd:PHA03095   232 GSSCKRSLVlpLLIAGISINAR--NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG-NTPLSLMVRNNNGRAVRA 308
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462596386  907 LLDRKANVEHRAKTgLTPLMEAASGGYAEVGR-----VLLDKGADVNAPPV 952
Cdd:PHA03095   309 ALAKNPSAETVAAT-LNTASVAGGDIPSDATRlcvakVVLRGAFSLLPEPI 358
PHA02874 PHA02874
ankyrin repeat protein; Provisional
762-1091 1.65e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 87.71  E-value: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  762 AGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNA 841
Cdd:PHA02874    11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  842 GAEinsrtgsklgISPLMLAAMNGHTaaVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTG 921
Cdd:PHA02874    91 GVD----------TSILPIPCIEKDM--IKTILDCGIDVNIK-DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  922 LTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLA----- 996
Cdd:PHA02874   158 CYPIHIAIKHNFFDIIKLLLEKGAYANVK--DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiihnr 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  997 ----------------ANGG-----------HLDVVQLLVQAGADVDAADNRKITPLMAAFRK-GHVKVVR------YLV 1042
Cdd:PHA02874   236 saiellinnasindqdIDGStplhhainppcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKdiianaVLI 315
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2462596386 1043 KEVNQFPsDSECMRYIATITDKEMLKKCHLCMESIVQAKdRQAAEANKN 1091
Cdd:PHA02874   316 KEADKLK-DSDFLEHIEIKDNKEFSDFIKECNEEIEDMK-KTKCGCDKN 362
PHA03095 PHA03095
ankyrin-like protein; Provisional
401-614 1.90e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.77  E-value: 1.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  401 EMVALLLGQGANINaQTEETQETALT--LAC-CGGFLEVADFLIKAGADIEL----GCsTPL---MEAAQEghLELVKYL 470
Cdd:PHA03095    28 EEVRRLLAAGADVN-FRGEYGKTPLHlyLHYsSEKVKDIVRLLLEAGADVNApercGF-TPLhlyLYNATT--LDVIKLL 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  471 LAAGANVHATTATGDTAL-TYAC-ENGHTDVADVLLQAGADLEHESEGGRTPL---MKAARAgHVCTVQFLISKGANVnR 545
Cdd:PHA03095   104 IKAGADVNAKDKVGRTPLhVYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDAGADV-Y 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  546 TTANNDHTVLSLacaggHL-------AVVELLLAHGADPTHRLKDGSTMLIEAAKGG--HTSVVCYLL------DYPNNL 610
Cdd:PHA03095   182 AVDDRFRSLLHH-----HLqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLiagisiNARNRY 256

                   ....
gi 2462596386  611 LSAP 614
Cdd:PHA03095   257 GQTP 260
PHA02875 PHA02875
ankyrin repeat protein; Provisional
721-913 1.90e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.35  E-value: 1.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  721 TALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQE 800
Cdd:PHA02875    37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  801 VVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGskLGISPLMLAAMNGHTAAVKLLLDMGSDI 880
Cdd:PHA02875   117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC--CGCTPLIIAMAKGDIAICKMLLDSGANI 194
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462596386  881 NAqieTNRNTALTLACF---QGRTEVVSLLLDRKAN 913
Cdd:PHA02875   195 DY---FGKNGCVAALCYaieNNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-217 2.06e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 2.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  125 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGikgdITPLMAAANGGHVKI 203
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNG----RTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 2462596386  204 VKLLLAHKADVNAQ 217
Cdd:pfam12796   77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
892-986 2.68e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 2.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  892 LTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKgADVNappVPSSRDTALTIAADKGHYKF 971
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN---LKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 2462596386  972 CELLIGRGAHIDVRN 986
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1363-1427 4.39e-17

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 77.32  E-value: 4.39e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1427
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
PHA02876 PHA02876
ankyrin repeat protein; Provisional
499-880 1.27e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 86.27  E-value: 1.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  499 VADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANnDHTVLSLACAGGHLAVVELLLahgaDPT 578
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAII----DNR 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  579 HRLKDGSTMLIEAAKGG--HTSVVCYLLDYPNNLLsapppDVTQLTPpshdLNRAPRVPvqALPMVVPP---QEPDKPPA 653
Cdd:PHA02876   235 SNINKNDLSLLKAIRNEdlETSLLLYDAGFSVNSI-----DDCKNTP----LHHASQAP--SLSRLVPKlleRGADVNAK 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  654 NVATTLPIRNKAVSGrasamsnTPTHSIAASISQpqtptpspiispsamlpiypAIDIDAqTESNHDTALTLACA-GGHE 732
Cdd:PHA02876   304 NIKGETPLYLMAKNG-------YDTENIRTLIML--------------------GADVNA-ADRLYITPLHQASTlDRNK 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  733 ELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTkDTPLSLACSGGRQEV-VELLLARGAN 811
Cdd:PHA02876   356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKI-GTALHFALCGTNPYMsVKTLIDRGAN 434
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386  812 KEHRNVSDYTPLSLAASGG-YVNIIKILLNAGAEINSrtgskLGIS---PLMLAAmnGHTAAVKLLLDMGSDI 880
Cdd:PHA02876   435 VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA-----INIQnqyPLLIAL--EYHGIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
902-1043 6.51e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 6.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  902 EVVSLLLDRKANVEHR---AKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALtiaadkgHYKFC------ 972
Cdd:PHA03095    28 EEVRRLLAAGADVNFRgeyGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAP--ERCGFTPL-------HLYLYnattld 98
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  973 --ELLIGRGAHIDVRNKKGNTPL--WLAANGGHLDVVQLLVQAGADVDAADNRKITPLmAAFRKGH---VKVVRYLVK 1043
Cdd:PHA03095    99 viKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPL-AVLLKSRnanVELLRLLID 175
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
1364-1426 7.22e-16

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 73.87  E-value: 7.22e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1364 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLIN 1426
Cdd:cd00105      1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGERVVTITGTPEAVEKAKELIE 63
PHA02876 PHA02876
ankyrin repeat protein; Provisional
457-947 7.48e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.96  E-value: 7.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  457 EAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFL 536
Cdd:PHA02876   151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  537 ISKGANVNRttanNDhtvLSLacagghlavvelllahgadpthrLKDGSTMLIEaakgghTSVVCYLLDYPNNLLsappp 616
Cdd:PHA02876   231 IDNRSNINK----ND---LSL-----------------------LKAIRNEDLE------TSLLLYDAGFSVNSI----- 269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  617 DVTQltppshdlnraprvpvqalpmvvppqepdkppanvattlpirnkavsgrasamsNTPTHSIAasisqpQTPTPSpi 696
Cdd:PHA02876   270 DDCK------------------------------------------------------NTPLHHAS------QAPSLS-- 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  697 ispsamlpiypaididaqtesnhdtaltlacaggheELVQTLLERGASIEHRDKKGFTPLILAATAGH-VGVVEILLDNG 775
Cdd:PHA02876   288 ------------------------------------RLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLG 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  776 ADIEAqSERTKDTPLSLACSGGR-QEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgSKLG 854
Cdd:PHA02876   332 ADVNA-ADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS-QKIG 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  855 IS-PLMLAAMNGHTaAVKLLLDMGSDINAQiETNRNTALTLACFQG-RTEVVSLLLDRKANVEHRAKTGLTPLMEAAsgG 932
Cdd:PHA02876   410 TAlHFALCGTNPYM-SVKTLIDRGANVNSK-NKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--E 485
                          490
                   ....*....|....*
gi 2462596386  933 YAEVGRVLLDKGADV 947
Cdd:PHA02876   486 YHGIVNILLHYGAEL 500
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
192-360 1.04e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 83.38  E-value: 1.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  192 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:PLN03192   529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  272 LLLENGAGINTHSNefkESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVN-MP 350
Cdd:PLN03192   609 ILYHFASISDPHAA---GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkAN 685
                          170
                   ....*....|
gi 2462596386  351 ADSFESPLTL 360
Cdd:PLN03192   686 TDDDFSPTEL 695
PHA02875 PHA02875
ankyrin repeat protein; Provisional
224-446 3.94e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 3.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  224 ALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFkESALTLACYKGHLEM 303
Cdd:PHA02875     5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  304 VRFLLEAG--ADQEHKTDEMhTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLE 381
Cdd:PHA02875    84 VEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386  382 EVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTLACCGGFLEVADFLIKAGAD 446
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
521-606 4.49e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 4.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  521 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 600
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 2462596386  601 CYLLDY 606
Cdd:pfam12796   78 KLLLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
133-329 7.29e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.26  E-value: 7.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  133 DVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKA 212
Cdd:PHA02875    47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  213 DVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKESAL 292
Cdd:PHA02875   127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2462596386  293 TLACYKGHLEMVRFLLEAGADQEHKT---DEMHTALMEAC 329
Cdd:PHA02875   207 CYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDMIC 246
PHA02875 PHA02875
ankyrin repeat protein; Provisional
324-576 9.87e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.88  E-value: 9.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  324 ALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAsLEEVNDEGY-TPLMEAAREGHEEM 402
Cdd:PHA02875     5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  403 VALLLGQGANINaqteetqetaltlaccggflevaDFLIKAGadielgcSTPLMEAAQEGHLELVKYLLAAGANVHATTA 482
Cdd:PHA02875    84 VEELLDLGKFAD-----------------------DVFYKDG-------MTPLHLATILKKLDIMKLLIARGADPDIPNT 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  483 TGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGG 562
Cdd:PHA02875   134 DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENN 213
                          250
                   ....*....|....
gi 2462596386  563 HLAVVELLLAHGAD 576
Cdd:PHA02875   214 KIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
365-629 1.55e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 1.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  365 GHVELAALLIE-RGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTlACCGGFLEVADFLIKA 443
Cdd:PHA02874    12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLT-AIKIGAHDIIKLLIDN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  444 GADIELgCSTPLMEAaqeghlELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMK 523
Cdd:PHA02874    91 GVDTSI-LPIPCIEK------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  524 AARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLiEAAKGGHTSVVCYL 603
Cdd:PHA02874   164 AIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL-HNAIIHNRSAIELL 241
                          250       260
                   ....*....|....*....|....*.
gi 2462596386  604 LdypnNLLSAPPPDVTQLTPPSHDLN 629
Cdd:PHA02874   242 I----NNASINDQDIDGSTPLHHAIN 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
733-1032 1.80e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.38  E-value: 1.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  733 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVGVVEILLDNGADIEAQSERTkdtpLSLACSGGRQEVVELLLARGAN 811
Cdd:PHA02878    51 DVVKSLLTRGHNVNQPDHRDLTPLhIICKEPNKLGMKEMIRSINKCSVFYTLVA----IKDAFNNRNVEIFKIILTNRYK 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  812 KEHrnVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRTGSKLGiSPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrN 889
Cdd:PHA02878   127 NIQ--TIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTN-N 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  890 TALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMeaASGGYA---EVGRVLLDKGADVNAppvpssRDTALTIAAdk 966
Cdd:PHA02878   203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH--ISVGYCkdyDILKLLLEHGVDVNA------KSYILGLTA-- 272
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386  967 ghykfcelligrgAHIDVRNKkgntplwlaangghlDVVQLLVQAGADVDAADNRKITPLMAAFRK 1032
Cdd:PHA02878   273 -------------LHSSIKSE---------------RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
788-980 3.62e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.95  E-value: 3.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  788 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSrTGSKLGISPLMLAAMNGHT 867
Cdd:PHA02875    37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADD-VFYKDGMTPLHLATILKKL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  868 AAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADV 947
Cdd:PHA02875   116 DIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462596386  948 N----APPVpssrdTALTIAADKGHYKFCELLIGRGA 980
Cdd:PHA02875   195 DyfgkNGCV-----AALCYAIENNKIDIVRLFIKRGA 226
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
1363-1428 5.13e-14

third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411867 [Multi-domain]  Cd Length: 68  Bit Score: 68.80  E-value: 5.13e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINAL 1428
Cdd:cd22439      3 TQEITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEDGSTERSVTITGTPEAVSLAQYLINAR 68
PHA02875 PHA02875
ankyrin repeat protein; Provisional
793-1014 5.26e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 5.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  793 ACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGsklGI-SPLMLAAMNGHTAAVK 871
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIeSELHDAVEEGDVKAVE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  872 LLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPP 951
Cdd:PHA02875    86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  952 VPSSrdTALTIAADKGHYKFCELLIGRGAHIDVRNKKGN-TPLWLAANGGHLDVVQLLVQAGAD 1014
Cdd:PHA02875   166 CCGC--TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
1365-1429 1.88e-13

fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH domain-containing protein HEN4 and similar protein; HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. HEN4 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of HEN4.


Pssm-ID: 411890 [Multi-domain]  Cd Length: 66  Bit Score: 66.89  E-value: 1.88e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386 1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22462      2 EILIPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDSATGERIVLISGTPDQARHAQNLIEAFI 66
PHA02875 PHA02875
ankyrin repeat protein; Provisional
158-378 2.49e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.64  E-value: 2.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  158 LCLACSAGYYELAQVLLAMHANvEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVV 237
Cdd:PHA02875     6 LCDAILFGELDIARRLLDIGIN-PNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  238 KVLLESGASIED-HNENGHTPLMEAGSAGHVEVARLLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH 316
Cdd:PHA02875    85 EELLDLGKFADDvFYKDGMTPLHLATILKKLDIMKLLIARGADPDI-PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386  317 KTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAdsfESPLTLAACGG----HVELAALLIERGA 378
Cdd:PHA02875   164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFG---KNGCVAALCYAiennKIDIVRLFIKRGA 226
KH smart00322
K homology RNA-binding domain;
1365-1429 2.89e-13

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 66.55  E-value: 2.89e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386  1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIP--GPGSEERVVEITGPPENVEKAAELILEIL 68
PHA02875 PHA02875
ankyrin repeat protein; Provisional
826-1043 3.39e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 3.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  826 AASGGYVNIIKILLNAGaeINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRnTALTLACFQGRTEVVS 905
Cdd:PHA02875     9 AILFGELDIARRLLDIG--INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDVKAVE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  906 LLLDRKANVEHRA-KTGLTPLMEAASGGYAEVGRVLLDKGADvnaPPVPSS-RDTALTIAADKGHYKFCELLIGRGAHID 983
Cdd:PHA02875    86 ELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGAD---PDIPNTdKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462596386  984 VRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRK-ITPLMAAFRKGHVKVVRYLVK 1043
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA02875 PHA02875
ankyrin repeat protein; Provisional
199-427 4.50e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.87  E-value: 4.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  199 GHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGAsIEDHNENG-HTPLMEAGSAGHVEVARLLLENG 277
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  278 AGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 357
Cdd:PHA02875    92 KFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462596386  358 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHE-EMVALLLGQGANINAQTEETQETALTL 427
Cdd:PHA02875   172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNIMFMIEGEECTIL 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
705-781 5.16e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 5.16e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386  705 IYPAIDIDAQTEsNHDTALTLACAGGHEELVQTLLERgASIEHRDkKGFTPLILAATAGHVGVVEILLDNGADIEAQ 781
Cdd:pfam12796   17 LENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
336-571 2.21e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 2.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  336 VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGAN--I 413
Cdd:PHA02874    17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsI 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  414 NAQTEETQETALTLACCGGFLEVADFLIKagadielgcsTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACE 493
Cdd:PHA02874    97 LPIPCIEKDMIKTILDCGIDVNIKDAELK----------TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  494 NGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHlAVVELLL 571
Cdd:PHA02874   167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM-NKCKNGFTPLHNAIIHNR-SAIELLI 242
PHA02876 PHA02876
ankyrin repeat protein; Provisional
801-1042 2.24e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 2.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  801 VVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDI 880
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD--DLSVLECAVDSKNIDTIKAIIDNRSNI 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  881 NAQ----IETNRNTALtlacfqgrtEVVSLLLDRKANVEHRAKTGLTPLMEAASG-GYAEVGRVLLDKGADVNAPPVPSs 955
Cdd:PHA02876   238 NKNdlslLKAIRNEDL---------ETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKG- 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  956 rDTALTIAADKGH-YKFCELLIGRGAHIDVRNKKGNTPLWLAAN-GGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKG 1033
Cdd:PHA02876   308 -ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                   ....*....
gi 2462596386 1034 HVKVVRYLV 1042
Cdd:PHA02876   387 NVVIINTLL 395
PHA02878 PHA02878
ankyrin repeat protein; Provisional
767-941 2.35e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 2.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  767 VVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 846
Cdd:PHA02878   149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  847 SRtgSKLGISPLMLAAMNGHTAAV-KLLLDMGSDINAQIETNRNTALTLACFQGRteVVSLLLDRKANVEHRAKTGLTPL 925
Cdd:PHA02878   229 AR--DKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPL 304
                          170
                   ....*....|....*..
gi 2462596386  926 MEAASGGYA-EVGRVLL 941
Cdd:PHA02878   305 SSAVKQYLCiNIGRILI 321
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
369-636 2.71e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.59  E-value: 2.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  369 LAALLIERGASLEE---VNDEGYTPLMEAAREGHEEMVALLLGQ--GANINAQTEETQET-ALTLACCG--GFLEVadfL 440
Cdd:PLN03192   468 LSQLLRLKTSTLIEamqTRQEDNVVILKNFLQHHKELHDLNVGDllGDNGGEHDDPNMASnLLTVASTGnaALLEE---L 544
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  441 IKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAgADLEHESEGG 517
Cdd:PLN03192   545 LKAKLDPDIGDSkgrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAG 623
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  518 RTpLMKAARAGHVCTVQFLISKGANVNrttaNNDH---TVLSLACAGGHLAVVELLLAHGADPTHRLKD---GSTMLIEA 591
Cdd:PLN03192   624 DL-LCTAAKRNDLTAMKELLKQGLNVD----SEDHqgaTALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELREL 698
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462596386  592 AK----GGHTSVVCYLLDYPNNLLSAPPPDVTQLTPPSHDLNRAPRVPV 636
Cdd:PLN03192   699 LQkrelGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSI 747
PHA02878 PHA02878
ankyrin repeat protein; Provisional
123-313 2.79e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 2.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  123 RSLAEACSEGDVNAVRKLLIegrsvNEHTEEGESLLCLACSAGY-----YELAQVLLAMHANVEDRGIKGDITPLMAAAN 197
Cdd:PHA02878   103 VAIKDAFNNRNVEIFKIILT-----NRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  198 GGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL-MEAGSAGHVEVARLLLEN 276
Cdd:PHA02878   178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462596386  277 GAGINTHSNEFKESALTLACYKGhlEMVRFLLEAGAD 313
Cdd:PHA02878   258 GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGAD 292
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
334-514 4.87e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.44  E-value: 4.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  334 VEVARLLLDSGAQVNMPADSFeSPLTLAACGGHVELAALLieRGASLEEVND-EGYTPLMEAAREGHEEMVALLLGQGAN 412
Cdd:PLN03192   507 LNVGDLLGDNGGEHDDPNMAS-NLLTVASTGNAALLEELL--KAKLDPDIGDsKGRTPLHIAASKGYEDCVLVLLKHACN 583
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  413 INAQtEETQETALTLACCGGFLEVADFLIK--------AGADIelgcstpLMEAAQEGHLELVKYLLAAGANVHATTATG 484
Cdd:PLN03192   584 VHIR-DANGNTALWNAISAKHHKIFRILYHfasisdphAAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655
                          170       180       190
                   ....*....|....*....|....*....|
gi 2462596386  485 DTALTYACENGHTDVADVLLQAGADLEHES 514
Cdd:PLN03192   656 ATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
190-241 5.10e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.68  E-value: 5.10e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  190 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLL 241
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
1363-1432 7.65e-12

third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411862 [Multi-domain]  Cd Length: 74  Bit Score: 62.72  E-value: 7.65e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1432
Cdd:cd22434      3 TTQVTIPKDLAGSIIGKGGQRIRQIRHESGASIKIDEPLPGSEDRIITITGTQDQIQNAQYLLQNSVKQY 72
Ank_2 pfam12796
Ankyrin repeats (3 copies);
993-1047 8.62e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 8.62e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386  993 LWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVKEVNQ 1047
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV 55
PHA02875 PHA02875
ankyrin repeat protein; Provisional
887-1043 9.75e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 9.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  887 NRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGA--DVNAPPVPSSrdtaLTIAA 964
Cdd:PHA02875     1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIESE----LHDAV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  965 DKGHYKFCELLIGRGAHI-DVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVK 1043
Cdd:PHA02875    77 EEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
Ank_4 pfam13637
Ankyrin repeats (many copies);
451-504 1.01e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 1.01e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  451 CSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLL 504
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
452-630 1.54e-11

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: 69.66  E-value: 1.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  452 STPLMEAAQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 525
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  526 RAGHVCTVQFLISKGANVN--RTTAN------------NDHtVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 591
Cdd:cd22192     98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462596386  592 AKGGHTSVVCYLLDYpnnLLSAPPPDvtQLTPPSHDLNR 630
Cdd:cd22192    177 VLQPNKTFACQMYDL---ILSYDKED--DLQPLDLVPNN 210
PHA02878 PHA02878
ankyrin repeat protein; Provisional
234-526 2.48e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 2.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  234 VDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLengAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGAD 313
Cdd:PHA02878    50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYK 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  314 QEHKTDEMHtaLMEACMDGHVE--VARLLLDSGAQVNM-PADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTP 390
Cdd:PHA02878   127 NIQTIDLVY--IDKKSKDDIIEaeITKLLLSYGADINMkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  391 LMEAAREGHEEMVALLLGQGANINAQTEetqetaltlacCGgflevadflikagadielgcSTPL-MEAAQEGHLELVKY 469
Cdd:PHA02878   205 LHHAVKHYNKPIVHILLENGASTDARDK-----------CG--------------------NTPLhISVGYCKDYDILKL 253
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  470 LLAAGANVHA-TTATGDTALTYACENghTDVADVLLQAGADLEHESEGGRTPLMKAAR 526
Cdd:PHA02878   254 LLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02878 PHA02878
ankyrin repeat protein; Provisional
191-447 5.41e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 5.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  191 PLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESgaSIEDHNENGHTPLMEAGSAGHVEVA 270
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  271 RLLLengagINTHSNEfKESALTLACYKGH-----LEMVRFLLEAGADQEHKT-DEMHTALMEACMDGHVEVARLLLDSG 344
Cdd:PHA02878   118 KIIL-----TNRYKNI-QTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  345 AQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPL-MEAAREGHEEMVALLLGQGANINAQTEETQET 423
Cdd:PHA02878   192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLT 271
                          250       260
                   ....*....|....*....|....
gi 2462596386  424 ALTLACCGGflEVADFLIKAGADI 447
Cdd:PHA02878   272 ALHSSIKSE--RKLKLLLEYGADI 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
256-471 8.84e-11

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: 67.35  E-value: 8.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  256 TPLMEAGSAGHVE-VARLLLENGAGINTHSnEFKESALTLACYKGHLEMVRFLLEAGAD--QEHKTDEMH---TALMEAC 329
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRG-ALGETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTALHIAV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  330 MDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPL---- 391
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilv 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  392 MEAAREGHEEMVALLLGQGANINAQTEETQETALTLaccggflevadflikagadielgcsTPLMEAAQEGHLELVKYLL 471
Cdd:cd22192    178 LQPNKTFACQMYDLILSYDKEDDLQPLDLVPNNQGL-------------------------TPFKLAAKEGNIVMFQHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
989-1042 1.61e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.61e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  989 GNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLV 1042
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
856-1019 1.82e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.43  E-value: 1.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  856 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRnTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAE 935
Cdd:PLN03192   527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  936 VGRVLLDKGADVNappvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADV 1015
Cdd:PLN03192   606 IFRILYHFASISD----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681

                   ....
gi 2462596386 1016 DAAD 1019
Cdd:PLN03192   682 DKAN 685
KH-I_NOVA_rpt3 cd09031
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
1364-1425 2.15e-10

third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411807 [Multi-domain]  Cd Length: 71  Bit Score: 58.36  E-value: 2.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386 1364 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1425
Cdd:cd09031      3 IELEVPENLVGAILGKGGKTLVEIQELTGARIQISKKGEfvpGTRNRKVTITGTPAAVQAAQYLI 67
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
116-294 3.41e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 3.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  116 NAGQSDNRSLAE----ACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTP 191
Cdd:PLN03192   516 NGGEHDDPNMASnlltVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN-TA 594
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  192 LMAAANGGHVKIVKLLLAHKADVNAQssTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 271
Cdd:PLN03192   595 LWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
                          170       180
                   ....*....|....*....|....
gi 2462596386  272 LLLENGAGInTHSNEFKE-SALTL 294
Cdd:PLN03192   673 LLIMNGADV-DKANTDDDfSPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
719-772 4.07e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 4.07e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  719 HDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL 772
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
190-316 5.49e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 5.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  190 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESgASIEDHNENGHTpLMEAGSAGHVEV 269
Cdd:PLN03192   560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDLTA 637
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462596386  270 ARLLLENGAGINTHSNEFKeSALTLACYKGHLEMVRFLLEAGADQEH 316
Cdd:PLN03192   638 MKELLKQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA03100 PHA03100
ankyrin repeat protein; Provisional
132-253 5.89e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 5.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  132 GDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR-------GIKGDI------TPLMA 194
Cdd:PHA03100   119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsyGVPINIkdvygfTPLHY 198
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386  195 AANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNEN 253
Cdd:PHA03100   199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
812-1026 6.33e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 6.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  812 KEHR----NVSDYTPLSLAASGGYVNIIKILLNAGAEINsRTGSKlGISPLMLAAMNGHTAAVKLLLdmgSDINAQIETN 887
Cdd:PHA02878    26 TENYstsaSLIPFIPLHQAVEARNLDVVKSLLTRGHNVN-QPDHR-DLTPLHIICKEPNKLGMKEMI---RSINKCSVFY 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  888 RNTALTLACFQGRTEVV-SLLLDRKANVEhraKTGLTPLMEAASGGY--AEVGRVLLDKGADVNAPPvPSSRDTALTIAA 964
Cdd:PHA02878   101 TLVAIKDAFNNRNVEIFkIILTNRYKNIQ---TIDLVYIDKKSKDDIieAEITKLLLSYGADINMKD-RHKGNTALHYAT 176
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  965 DKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1026
Cdd:PHA02878   177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1373-1427 7.47e-10

second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the second one.


Pssm-ID: 411829 [Multi-domain]  Cd Length: 72  Bit Score: 56.85  E-value: 7.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386 1373 ISRVIGRGGCNINAIREFTGAHIDIDKQKDKT---GDRIITIRGGTESTRQATQLINA 1427
Cdd:cd22401     11 CGRLIGKDGRNIKKIMEDTNTKITISSLQDLTsynPERTITIKGSLEAMSEAESLISE 68
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
1364-1429 9.44e-10

first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one.


Pssm-ID: 411856 [Multi-domain]  Cd Length: 74  Bit Score: 56.57  E-value: 9.44e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386 1364 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKT--GDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22428      7 IEMKVPREAVGLIIGRQGATIKQIQKETGARIDFKDEGSGGelPERVLLIQGNPVQAQRAEEAIHQII 74
KH-I_PCBP4_rpt3 cd22523
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
1363-1427 1.13e-09

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) and similar proteins; PCBP4, also called alpha-CP4, or heterogeneous nuclear ribonucleoprotein E4, or hnRNP E4, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It regulates both basal and stress-induced p21 expression through binding p21 3'-UTR and modulating p21 mRNA stability. It also plays a role in the cell cycle and is implicated in lung tumor suppression. PCBP4 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411951  Cd Length: 68  Bit Score: 56.44  E-value: 1.13e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1427
Cdd:cd22523      3 SQEFLIPNDLIGCVIGRQGSKISEIRQMSGAHIKIGNQTEGTSERHVTITGSPVSITLAQYLITT 67
Ank_4 pfam13637
Ankyrin repeats (many copies);
956-1009 1.24e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.24e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  956 RDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLV 1009
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
555-608 1.41e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 1.41e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  555 LSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPN 608
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
125-285 1.64e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 1.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  125 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLL----------------AMHANVEDRGIKGD 188
Cdd:PHA02874    39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekDMIKTILDCGIDVN 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  189 I------TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAG 262
Cdd:PHA02874   119 IkdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
                          170       180
                   ....*....|....*....|...
gi 2462596386  263 SAGHVEVARLLLENGAGINTHSN 285
Cdd:PHA02874   199 EYGDYACIKLLIDHGNHIMNKCK 221
Ank_4 pfam13637
Ankyrin repeats (many copies);
221-274 1.93e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.93e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  221 GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLL 274
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
781-1010 1.99e-09

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: 62.72  E-value: 1.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  781 QSERTKDTPLSLACSGGRQEVVELLL--------ARGANKEhrnvsdyTPLSLAASGGYVNIIKILLNAGAE-INSRTGS 851
Cdd:cd22192     12 QQKRISESPLLLAAKENDVQAIKKLLkcpscdlfQRGALGE-------TALHVAALYDNLEAAVVLMEAAPElVNEPMTS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  852 KL--GISPLMLAAMNGHTAAVKLLLDMGSDINaqieTNRNTALtlaCFqgrtevvsllLDRKANV----EHraktgltPL 925
Cdd:cd22192     85 DLyqGETALHIAVVNQNLNLVRELIARGADVV----SPRATGT---FF----------RPGPKNLiyygEH-------PL 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  926 MEAASGGYAEVGRVLLDKGADVNAppvpssRD----TALTIAADKGHYKF-CE---LLIGRGAHID------VRNKKGNT 991
Cdd:cd22192    141 SFAACVGNEEIVRLLIEHGADIRA------QDslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLT 214
                          250
                   ....*....|....*....
gi 2462596386  992 PLWLAANGGHLDVVQLLVQ 1010
Cdd:cd22192    215 PFKLAAKEGNIVMFQHLVQ 233
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
728-806 1.99e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.99e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386  728 AGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAqSERTKDTPLSLACSGGRQEVVELLL 806
Cdd:PTZ00322    91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
254-308 1.99e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.99e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386  254 GHTPLMEAGSAGHVEVARLLLENGAGINtHSNEFKESALTLACYKGHLEMVRFLL 308
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
1364-1425 1.99e-09

third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding protein Rnc1 and similar proteins; Rnc1, also called RNA-binding protein that suppresses calcineurin deletion 1, is an RNA-binding protein that acts as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. It binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression of Rnc1 suppresses the Cl(-) sensitivity of calcineurin deletion. The nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. Rnc1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411885 [Multi-domain]  Cd Length: 64  Bit Score: 55.54  E-value: 1.99e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1364 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQK-DKTGDRIITIRGGTESTRQATQLI 1425
Cdd:cd22457      1 QNISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAKAPhDETGERMFTITGTPEANDRALRLL 63
Ank_4 pfam13637
Ankyrin repeats (many copies);
484-537 2.13e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.13e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  484 GDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLI 537
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
553-604 2.13e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.13e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  553 TVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLL 604
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
125-397 2.31e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 2.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  125 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSA----GYYELAQVLLAMHANVEDRGIKgditplmAAANGGH 200
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIK-------DAFNNRN 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  201 VKIVKLLLAHKADVNAQSStgntaLTYACAGGYVD-----VVKVLLESGASIEDHNEN-GHTPLMEAGSAGHVEVARLLL 274
Cdd:PHA02878   114 VEIFKIILTNRYKNIQTID-----LVYIDKKSKDDiieaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLL 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  275 ENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEA---CMDghVEVARLLLDSGAQVNmpA 351
Cdd:PHA02878   189 SYGANVNI-PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVN--A 263
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2462596386  352 DSFESPLTLAACGGHVE-LAALLIERGASLEEVNDEGYTPLMEAARE 397
Cdd:PHA02878   264 KSYILGLTALHSSIKSErKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
KH-I_TDRKH_rpt2 cd22429
second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
1363-1425 3.65e-09

second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the second one.


Pssm-ID: 411857 [Multi-domain]  Cd Length: 82  Bit Score: 55.42  E-value: 3.65e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGD--RIITIRGGTESTRQATQLI 1425
Cdd:cd22429      3 TEELHVPQRAVGRIIGRGGETIRSICRTSGAKVKCDRESDDTLDlvRLITITGTKKEVDAAKSLI 67
PHA02798 PHA02798
ankyrin-like protein; Provisional
201-418 4.34e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 61.39  E-value: 4.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  201 VKIVKLLLAHKADVNAQSSTGNTALT--------YACAggyVDVVKVLLESGASIEDHNENGHTP---LMEAGSAGHVEV 269
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLCtilsnikdYKHM---LDIVKILIENGADINKKNSDGETPlycLLSNGYINNLEI 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  270 ARLLLENGAGINTHSNeFKESALTLACYKGH---LEMVRFLLEAGAD-----QEHKTDEMHTALME--ACMDghVEVARL 339
Cdd:PHA02798   128 LLFMIENGADTTLLDK-DGFTMLQVYLQSNHhidIEIIKLLLEKGVDinthnNKEKYDTLHCYFKYniDRID--ADILKL 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  340 LLDSGAQVNMPADSFESPL-----TLAACGGHVELAAL-LIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANI 413
Cdd:PHA02798   205 FVDNGFIINKENKSHKKKFmeylnSLLYDNKRFKKNILdFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDI 284

                   ....*
gi 2462596386  414 NAQTE 418
Cdd:PHA02798   285 NIITE 289
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
1362-1432 4.78e-09

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 54.40  E-value: 4.78e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386 1362 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDP 1432
Cdd:cd02393      4 RITTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIED------DGTVTIFATDkESAEAAKAMIEDIVAEP 69
KH-I_NOVA_rpt2 cd22436
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
1365-1425 5.69e-09

second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411864 [Multi-domain]  Cd Length: 70  Bit Score: 54.55  E-value: 5.69e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD--KTGDRIITIRGGTESTRQATQLI 1425
Cdd:cd22436      4 KILVPNSTAGMIIGKGGATIKAIMEQSGARVQISQKPEsiNLQERVVTVTGEPEANRKAVSLI 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
356-407 9.24e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 9.24e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  356 SPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLL 407
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
321-374 9.61e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 9.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  321 MHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLI 374
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
721-840 1.04e-08

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: 60.41  E-value: 1.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  721 TALTLACAGGHEELVQTLLERGASIE---------HRDKK-----GFTPLILAATAGHVGVVEILLDNGADIEAQsERTK 786
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLG 169
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386  787 DTPL---------SLACsggrqEVVELLLARGANK-----EH-RNVSDYTPLSLAASGGYVNIIKILLN 840
Cdd:cd22192    170 NTVLhilvlqpnkTFAC-----QMYDLILSYDKEDdlqplDLvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1718-1973 1.11e-08

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.55  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1718 PPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMT-------VPPLATSSAPVAVPSTAP 1790
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTpqssqsqVPPGPSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1791 VTYPMPQTPMGCP---QPTPK--METPAIRPPPhgtTAPHKNSASVQNssvavlsvnHIKRPH-SVPSSVQLPSTLSTQS 1864
Cdd:pfam03154  327 TPPSQSQLQSQQPpreQPLPPapLSMPHIKPPP---TTPIPQLPNPQS---------HKHPPHlSGPSPFQMNSNLPPPP 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1865 ACQN----------SVHPANKPIAPNfSAPLPFGPFS----TLFENSPTSAhafwggsvvsSQSTPESMLSGKSSYLPNs 1930
Cdd:pfam03154  395 ALKPlsslsthhppSAHPPPLQLMPQ-SQQLPPPPAQppvlTQSQSLPPPA----------ASHPPTSGLHQVPSQSPF- 462
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462596386 1931 dPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDSPyGSVTPSST 1973
Cdd:pfam03154  463 -PQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPP-SSASVSSS 503
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
877-1042 1.16e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  877 GSDINAQIETNRNTALTLacfqGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSsr 956
Cdd:PLN03192   518 GEHDDPNMASNLLTVAST----GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG-- 591
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  957 DTALTIAADKGHYKFCELLIgRGAHIDVRNKKGNTpLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVK 1036
Cdd:PLN03192   592 NTALWNAISAKHHKIFRILY-HFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669

                   ....*.
gi 2462596386 1037 VVRYLV 1042
Cdd:PLN03192   670 MVRLLI 675
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1366-1427 1.43e-08

seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 53.09  E-value: 1.43e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386 1366 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqKDKTGDrIITIRGGTESTRQATQLINA 1427
Cdd:cd22452      6 IKVSPRYFGRIIGPGGSNINQIREKSGCFINVPK-KNKESD-VITLRGTKEGVEKAEEMIKK 65
PHA02878 PHA02878
ankyrin repeat protein; Provisional
233-618 2.42e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 2.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  233 YVDVVKVLLESGASIeDHNENGHT--------PLMEAGSAGHVEVARLLLENGAGINTHSNEFKeSALTLACYK----GH 300
Cdd:PHA02878     9 YTDNYETILKYIEYI-DHTENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDL-TPLHIICKEpnklGM 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  301 LEMVRFLLEAGADQEHKtdemhtALMEACMDGHVEVARLLLdsgaqvnmpADSFESpltlaacgghvelaalliERGASL 380
Cdd:PHA02878    87 KEMIRSINKCSVFYTLV------AIKDAFNNRNVEIFKIIL---------TNRYKN------------------IQTIDL 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  381 EEVNDEGYTPLMEAaregheEMVALLLGQGANINAQTEETQetaltlaccggflevadflikagadielgcSTPLMEAAQ 460
Cdd:PHA02878   134 VYIDKKSKDDIIEA------EITKLLLSYGADINMKDRHKG------------------------------NTALHYATE 177
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  461 EGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPL-MKAARAGHVCTVQFLISK 539
Cdd:PHA02878   178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386  540 GANVNRTTANNDHTVLSLACAGGHlaVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPNNLLSAPPPDV 618
Cdd:PHA02878   258 GVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334
Ank_4 pfam13637
Ankyrin repeats (many copies);
387-441 3.20e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 3.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386  387 GYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLI 441
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
550-811 4.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 4.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  550 NDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYpNNLLSAPPPDVTQltpPSHD-L 628
Cdd:PHA02875     1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKH-GAIPDVKYPDIES---ELHDaV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  629 NRAPRVPVQALPMVvppqepdkppanvattlpirNKAVSGRASAMSNTPTHsiAASISQPqtptpspiISPSAMLPIYPA 708
Cdd:PHA02875    77 EEGDVKAVEELLDL--------------------GKFADDVFYKDGMTPLH--LATILKK--------LDIMKLLIARGA 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  709 iDIDAqTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDT 788
Cdd:PHA02875   127 -DPDI-PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
                          250       260
                   ....*....|....*....|...
gi 2462596386  789 PLSLACSGGRQEVVELLLARGAN 811
Cdd:PHA02875   205 ALCYAIENNKIDIVRLFIKRGAD 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
517-571 4.60e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 4.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386  517 GRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDhTVLSLACAGGHLAVVELLL 571
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
KH-I_PCBP1_2_rpt3 cd22521
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
1363-1427 4.82e-08

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411949  Cd Length: 76  Bit Score: 51.98  E-value: 4.82e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1427
Cdd:cd22521      6 SHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINA 70
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
825-908 5.45e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 5.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  825 LAASGGYVNIiKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDINAqIETNRNTALTLACFQGRTEVV 904
Cdd:PTZ00322    89 LAASGDAVGA-RILLTGGADPNCRDYD--GRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVV 164

                   ....
gi 2462596386  905 SLLL 908
Cdd:PTZ00322   165 QLLS 168
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1361-1431 5.52e-08

first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 52.02  E-value: 5.52e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386 1361 RRSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRI--------ITIRGGTESTRQATQLINALIKD 1431
Cdd:cd22446      6 KVTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGNYDEddddetveISIEGDAEGVELAKKEIEAIVKE 84
Ank_4 pfam13637
Ankyrin repeats (many copies);
290-341 6.88e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 6.88e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  290 SALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLL 341
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
201-505 7.17e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 57.44  E-value: 7.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  201 VKIVKLLLAHKADVNAQS--STGNTAL---TYACAGGYVDVVKVLLESGASIEDHNENGHTPLM---EAGSAGHVEVARL 272
Cdd:PHA02989    50 IKIVKLLIDNGADVNYKGyiETPLCAVlrnREITSNKIKKIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRF 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  273 LLENGAGINTHSNE--FKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVArllldsgaqvnmp 350
Cdd:PHA02989   130 LLSKGINVNDVKNSrgYNLLHMYLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMNIYLRNDIDVI------------- 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  351 adsfespltlaacggHVELAALLIERGASLEEvNDEGYTPLMEAAREGHEEMValllgqganinaqteeTQEtaltlacc 430
Cdd:PHA02989   197 ---------------SIKVIKYLIKKGVNIET-NNNGSESVLESFLDNNKILS----------------KKE-------- 236
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  431 ggfLEVADFL---IKAGADIELGCsTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQ 505
Cdd:PHA02989   237 ---FKVLNFIlkyIKINKKDKKGF-NPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1366-1430 8.70e-08

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 51.26  E-value: 8.70e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1366 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRI--------ITIRGGTESTRQATQLINALIK 1430
Cdd:cd22447      8 VPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPADedddtmveVTITGDEFNVQHAKQRIEEIIS 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
498-887 1.09e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.60  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  498 DVADVLLQAGADLEHESEGGRTPLMKAARAGHVCT-----VQFLISKGANVNRTTANNDHTVLSLACAG-GHLAVVELLL 571
Cdd:PHA03100    49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  572 AHGADPTHRLKDGSTMLIEAAKGGHTsvvcylldypnnllsapppdvtqltppshDLNraprvpvqalpmvvppqepdkp 651
Cdd:PHA03100   129 DNGANVNIKNSDGENLLHLYLESNKI-----------------------------DLK---------------------- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  652 panvattlpirnkavsgrasamsntpthsiaasisqpqtptpspIISpsamLPIYPAIDIDAQTEsnhdtaltlacaggh 731
Cdd:PHA03100   158 --------------------------------------------ILK----LLIDKGVDINAKNR--------------- 174
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  732 eelVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERtKDTPLSLACSGGRQEVVELLLARGAN 811
Cdd:PHA03100   175 ---VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY-GDTPLHIAILNNNKEIFKLLLNNGPS 250
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  812 kehrnvsdytplslaasggyVNIIK--ILLNAGAEINSRTGSKLGISPLMLAamnghtaavkLLLDMGSDINAQIETN 887
Cdd:PHA03100   251 --------------------IKTIIetLLYFKDKDLNTITKIKMLKKSIMYM----------FLLDPGFYKNRKLIEN 298
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1368-1429 1.26e-07

first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411824 [Multi-domain]  Cd Length: 68  Bit Score: 50.72  E-value: 1.26e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386 1368 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22396      7 VPDKMVGLIIGRGGEQINRLQAESGAKIQIAPDSGGLPERPCTLTGTPDAIETAKRLIDQIV 68
KH-I_IGF2BP_rpt1 cd22400
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1368-1425 1.31e-07

first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the first one.


Pssm-ID: 411828 [Multi-domain]  Cd Length: 68  Bit Score: 50.35  E-value: 1.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386 1368 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTG-DRIITIRGGTESTRQATQLI 1425
Cdd:cd22400      6 VPSEFVGAIIGKGGATIRQITQQTGARIDIHRKENAGAaEKAITIYGTPEGCSSACKQI 64
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1365-1430 1.53e-07

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 50.35  E-value: 1.53e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386 1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqkDKTGDRIITIRGGTESTRQATQLINALIK 1430
Cdd:cd22449      7 KFDVPAKYVPHIIGKKGANINKLREEYGVKIDFE---DKTGEGNVEIKGSKKNVEEAKKRILSQID 69
PHA02878 PHA02878
ankyrin repeat protein; Provisional
710-898 1.56e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  710 DIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSeRTKDTP 789
Cdd:PHA02878   159 DINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD-KCGNTP 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  790 LSLACSggrqevvelllargankehrNVSDYtplslaasggyvNIIKILLNAGAEINSRTgSKLGISPLMLAAMNghTAA 869
Cdd:PHA02878   238 LHISVG--------------------YCKDY------------DILKLLLEHGVDVNAKS-YILGLTALHSSIKS--ERK 282
                          170       180
                   ....*....|....*....|....*....
gi 2462596386  870 VKLLLDMGSDINAqIETNRNTALTLACFQ 898
Cdd:PHA02878   283 LKLLLEYGADINS-LNSYKLTPLSSAVKQ 310
PHA02989 PHA02989
ankyrin repeat protein; Provisional
800-1038 1.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 56.29  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  800 EVVELLLARGANKEHRNVSDyTPL------SLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAV--- 870
Cdd:PHA02989    51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFN--GVSPIVCFIYNSNINNCdml 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  871 KLLLDMGSDINAQIETNRNTAL--TLACFQGRTEVVSLLLDRKANV-EHRAKTGLTP----LMEAASGGYAEVGRVLLDK 943
Cdd:PHA02989   128 RFLLSKGINVNDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKK 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  944 GADVNAPPVPSSRDTALTIAADKGHYKFC-ELL--IGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADN 1020
Cdd:PHA02989   208 GVNIETNNNGSESVLESFLDNNKILSKKEfKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSK 287
                          250
                   ....*....|....*...
gi 2462596386 1021 RKITPLMAAFRKGHVKVV 1038
Cdd:PHA02989   288 DGDTVLTYAIKHGNIDML 305
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
988-1020 1.60e-07

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: 49.21  E-value: 1.60e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462596386  988 KGNTPLWLAA-NGGHLDVVQLLVQAGADVDAADN 1020
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
195-274 1.79e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  195 AANGGHVKIvKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLL 274
Cdd:PTZ00322    90 AASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
738-793 1.99e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.99e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386  738 LLERG-ASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKdTPLSLA 793
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
856-908 2.08e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 2.08e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462596386  856 SPLMLAAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLL 908
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1363-1426 2.20e-07

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 49.51  E-value: 2.20e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLIN 1426
Cdd:cd22411      1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDL--PEENSDSDVITITGKKEDVEKARERIL 62
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
125-308 2.34e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.17  E-value: 2.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  125 LAEACSEGDVNAVRKLLiEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDI----TPLMAAANG 198
Cdd:cd22192     21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLyqgeTALHIAVVN 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  199 GHVKIVKLLLAHKADVNAQSST--------------GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL----ME 260
Cdd:cd22192    100 QNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvLQ 179
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462596386  261 AGSAGHVEVARLLLENGAGINTHS-----NEFKESALTLACYKGHLEMVRFLL 308
Cdd:cd22192    180 PNKTFACQMYDLILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
KH-I_BTR1_rpt3 cd22514
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ...
1363-1425 3.02e-07

third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411942 [Multi-domain]  Cd Length: 71  Bit Score: 49.73  E-value: 3.02e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1425
Cdd:cd22514      2 SVTIGVPDEHIGAILGRGGRTINEIQQHSGARIKISDRGDfvsGTRNRKVTITGPQDAVQMAQYLL 67
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
856-1043 3.65e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.40  E-value: 3.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  856 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKT-----GLTPLMEAAS 930
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVV 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  931 GGYAEVGRVLLDKGADVNAPPV------PSSR------DTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLwlaan 998
Cdd:cd22192     99 NQNLNLVRELIARGADVVSPRAtgtffrPGPKnliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL----- 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  999 ggHLDVVQ------------LLVQAGADVDAA-----DNRKITPLMAAFRKGHVKVVRYLVK 1043
Cdd:cd22192    174 --HILVLQpnktfacqmydlILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1431-1858 3.69e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.54  E-value: 3.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1431 DPdKEIDElipKNRLKSSSANSKIGSSAPTTTAANTSLMGIKMTTVALSSTSQTATALTVPAISSASTH-KTIKNPVNNV 1509
Cdd:pfam03154  133 DP-KDIDQ---DNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAgPTPSAPSVPP 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1510 RPGFPVSLPLAYPPPQFAHALLAAQTfQQIRPPRLPMTHfggtfPPAQSTwgpfpvrPLSPARATNSPKPHMVPRHSNQN 1589
Cdd:pfam03154  209 QGSPATSQPPNQTQSTAAPHTLIQQT-PTLHPQRLPSPH-----PPLQPM-------TQPPPPSQVSPQPLPQPSLHGQM 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1590 SSGSQVNSAGSLTSSPTTTTSSSASTVPGTSTNGSPS-SPSVRRQLFVTVVKTSNATTTTVTTTASNNNTAPtnATYPMP 1668
Cdd:pfam03154  276 PPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGpSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPP--APLSMP 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1669 TAKehypvsSPSSPSPPAQPGGVSRNSPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPP 1748
Cdd:pfam03154  354 HIK------PPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPP 427
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1749 GS----VSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPvtypmPQTPMGCPQPTPKMETPAIRPPphgTTAP 1824
Cdd:pfam03154  428 PAqppvLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPP-----PITPPSGPPTSTSSAMPGIQPP---SSAS 499
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2462596386 1825 HKNSASVQNSSVAVLSVNHIK--------RPHSVPSSVQLPS 1858
Cdd:pfam03154  500 VSSSGPVPAAVSCPLPPVQIKeealdeaeEPESPPPPPRSPS 541
KH-I_PCBP3_rpt3 cd22522
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
1363-1427 4.63e-07

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) and similar proteins; PCBP3, also called alpha-CP3, or PCBP3-overlapping transcript, or PCBP3-overlapping transcript 1, or heterogeneous nuclear ribonucleoprotein E3, or hnRNP E3, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It can function as a repressor dependent on binding to single-strand and double-stranded poly(C) sequences. PCBP3 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411950 [Multi-domain]  Cd Length: 75  Bit Score: 49.34  E-value: 4.63e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1427
Cdd:cd22522     10 THELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGSPANISLAQYLINA 74
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
715-894 5.22e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 5.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  715 TESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQsERTKDTPLSLAC 794
Cdd:PLN03192   521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR-DANGNTALWNAI 599
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  795 SGGRQEVVELLLARGANKEHRNVSDYtpLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLL 874
Cdd:PLN03192   600 SAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSE--DHQGATALQVAMAEDHVDMVRLLI 675
                          170       180
                   ....*....|....*....|
gi 2462596386  875 DMGSDINAQIETNRNTALTL 894
Cdd:PLN03192   676 MNGADVDKANTDDDFSPTEL 695
KH-I_FUBP_rpt4 cd22399
fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1367-1426 5.53e-07

fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411827 [Multi-domain]  Cd Length: 67  Bit Score: 48.76  E-value: 5.53e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462596386 1367 SVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD-KTGDRIITIRGGTESTRQATQLIN 1426
Cdd:cd22399      5 LVPANKCGLVIGKGGETIRQINQQSGAHVELDRNPPpNPNEKLFIIRGNPQQIEHAKQLIR 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
908-1043 6.67e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 6.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  908 LDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCE---LLIGRGAHIDV 984
Cdd:PHA03095     1 DEEDESVDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNA 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386  985 RNKKGNTPLWL-AANGGHLDVVQLLVQAGADVDAADNRKITPL---MAAFRKgHVKVVRYLVK 1043
Cdd:PHA03095    79 PERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvyLSGFNI-NPKVIRLLLR 140
KH-I_FUBP2_rpt4 cd22488
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1367-1425 7.96e-07

fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 2 (FUBP2) and similar proteins; FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP2 contains four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411916  Cd Length: 69  Bit Score: 48.56  E-value: 7.96e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386 1367 SVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGD---RIITIRGGTESTRQATQLI 1425
Cdd:cd22488      5 SIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQPPPNGDpnfKLFIIRGSPQQIDHAKQLI 66
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
705-941 9.15e-07

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: 54.32  E-value: 9.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  705 IYPAIDIDaqtESNHDTALTLACAGGHEELVQTLLERGAS--IEHRDKKGFTPLILAATAG-HVGVVEILLDNGADIEaq 781
Cdd:TIGR00870    6 IVPAEESP---LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  782 serTKDTPLsLACSGGRQEVVELLLA-------RGANKEHRNVS-------DYTPLSLAASGGYVNIIKILLNAGAEINS 847
Cdd:TIGR00870   81 ---VGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  848 R------------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIE---------------TNRNTALTLACFQgr 900
Cdd:TIGR00870  157 RacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSlgntllhllvmenefKAEYEELSCQMYN-- 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2462596386  901 tEVVSLL--LDRKANVEH-RAKTGLTPLMEAASGGYAEVGRVLL 941
Cdd:TIGR00870  235 -FALSLLdkLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
Ank_4 pfam13637
Ankyrin repeats (many copies);
820-874 1.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386  820 YTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLL 874
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGN--GETALHFAASNGNVEVLKLLL 54
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1368-1411 1.29e-06

first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH1 domain of PEPPER and FLK, as well as KH1 and KH3 domains of RCF3 and HEN4.


Pssm-ID: 411887 [Multi-domain]  Cd Length: 69  Bit Score: 47.60  E-value: 1.29e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462596386 1368 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITI 1411
Cdd:cd22459      8 CPVSKAGSVIGKGGEIIKQLRQETGARIKVEDGVPGTEERVITI 51
PHA03100 PHA03100
ankyrin repeat protein; Provisional
465-780 1.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  465 ELVKYLLAAGANVHATTATGDTALTYACENGHT-----DVADVLLQAGADLEHESEGGRTPLMKAA--RAGHVCTVQFLI 537
Cdd:PHA03100    49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  538 SKGANVNRTTANNdHTVLSLACAGGH--LAVVELLLAHGADpthrlkdgstmlIEAakgghTSVVCYLLDYPnnllsapp 615
Cdd:PHA03100   129 DNGANVNIKNSDG-ENLLHLYLESNKidLKILKLLIDKGVD------------INA-----KNRVNYLLSYG-------- 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  616 pdvtqltppshdlnraprvpvqalpmvVPPQEPDKppanvattlpirnkavsgrasaMSNTPTHSiaasisqpqtptpsp 695
Cdd:PHA03100   183 ---------------------------VPINIKDV----------------------YGFTPLHY--------------- 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  696 iispsamlpiypaididaqtesnhdtaltlACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNG 775
Cdd:PHA03100   199 ------------------------------AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248

                   ....*
gi 2462596386  776 ADIEA 780
Cdd:PHA03100   249 PSIKT 253
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
521-625 1.93e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  521 LMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVV 600
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                           90       100
                   ....*....|....*....|....*...
gi 2462596386  601 CYLLDYPNNLLSA---PPPDVTQLTPPS 625
Cdd:PTZ00322   165 QLLSRHSQCHFELganAKPDSFTGKPPS 192
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1366-1429 1.99e-06

third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411826 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 1.99e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462596386 1366 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22398      4 VPVPRFAVGVVIGKGGEMIKKIQNETGARVQFKPDDGNSPDRICVITGPPDQVQHAARMIQELI 67
PHA02989 PHA02989
ankyrin repeat protein; Provisional
869-1070 1.99e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.82  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  869 AVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRA--KTGLTPLM---EAASGGYAEVGRVLLDK 943
Cdd:PHA02989    18 ALEFLLRTGFDVNEEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGyiETPLCAVLrnrEITSNKIKKIVKLLLKF 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  944 GADVNAPPVPSSRDTALTIAadKGHYKFCE---LLIGRGAHI-DVRNKKGNTPL--WLAANGGHLDVVQLLVQAGADV-D 1016
Cdd:PHA02989    98 GADINLKTFNGVSPIVCFIY--NSNINNCDmlrFLLSKGINVnDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfE 175
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1017 AADNRKITPLMAAFRKG----HVKVVRYLVK-----EVNQFPSDSECMRYIAtiTDKEMLKKC 1070
Cdd:PHA02989   176 KTSLYGLTPMNIYLRNDidviSIKVIKYLIKkgvniETNNNGSESVLESFLD--NNKILSKKE 236
PHA03247 PHA03247
large tegument protein UL36; Provisional
1661-2093 2.53e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1661 TNATYPMPTAKEHYPVSSPSSPSPPAQPGGVSRNSPLDcGSASPNKVASSSeqeaGSPPVVETTNTRPPNSSSSSGSSSA 1740
Cdd:PHA03247  2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRL----GRAAQASSPPQRPRRRAARPTVGSL 2695
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1741 HSNQQQPPGSVSQEPRPPLQQSQVPPPEV----RMTVPPLATSSAPVAVPST-----APVTYPMPQTPMGCPQPTPKMET 1811
Cdd:PHA03247  2696 TSLADPPPPPPTPEPAPHALVSATPLPPGpaaaRQASPALPAAPAPPAVPAGpatpgGPARPARPPTTAGPPAPAPPAAP 2775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1812 PAirPPPHGTTAPHKNSASVQNSSVAVLSvnhikRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIAPNfSAPLPFGPFS 1891
Cdd:PHA03247  2776 AA--GPPRRLTRPAVASLSESRESLPSPW-----DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT-APPPPPGPPP 2847
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1892 TlfensPTSAhafwGGSVVssqstPESMLSGKSsylpnsdPLHQSDTSKAPGFRPP---LQRPAPSPSGIVNMDSPYGSV 1968
Cdd:PHA03247  2848 P-----SLPL----GGSVA-----PGGDVRRRP-------PSRSPAAKPAAPARPPvrrLARPAVSRSTESFALPPDQPE 2906
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1969 TPssthlgnfasnisggqmygpgaplggapaaanfnRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSP-APSSVPLGS 2047
Cdd:PHA03247  2907 RP----------------------------------PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPlAPTTDPAGA 2952
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2462596386 2048 EKPSNVSQDRKVPVPIGTERSARIRQTGTSAPSVIGSNLSTSVGHS 2093
Cdd:PHA03247  2953 GEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTG 2998
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
1368-1425 3.13e-06

type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa, or AKAP 149, or dual specificity A-kinase-anchoring protein 1, or D-AKAP-1, or protein kinase A-anchoring protein 1 (PRKA1), or spermatid A-kinase anchor protein 84, or S-AKAP84, is a novel developmentally regulated A kinase anchor protein of male germ cells. It binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.


Pssm-ID: 411823 [Multi-domain]  Cd Length: 68  Bit Score: 46.75  E-value: 3.13e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386 1368 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLI 1425
Cdd:cd22395      6 VPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYTQNFQICSIEGTQQQIDKALKLI 63
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
1368-1429 4.14e-06

second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411806 [Multi-domain]  Cd Length: 72  Bit Score: 46.49  E-value: 4.14e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1368 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQK-DKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd02396      8 VPASQCGSLIGKGGSKIKEIRESTGASVQVASEMlPNSTERAVTISGSPEAITKCVEQICCVM 70
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
323-539 4.18e-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: 51.94  E-value: 4.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  323 TALMEACMDGHVE-VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIErgASLEEVND-------EGYTPLMEA 394
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  395 AREGHEEMVALLLGQGANInaqteetqetaLTLACCGGFlevadFLIKAGADIELGcSTPLMEAAQEGHLELVKYLLAAG 474
Cdd:cd22192     97 VVNQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNLIYYG-EHPLSFAACVGNEEIVRLLIEHG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  475 ANVHATTATGDTAL---------TYACEnghtdVADVLL-----QAGADLEHESEG-GRTPLMKAARAGHVCTVQFLISK 539
Cdd:cd22192    160 ADIRAQDSLGNTVLhilvlqpnkTFACQ-----MYDLILsydkeDDLQPLDLVPNNqGLTPFKLAAKEGNIVMFQHLVQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
767-949 4.19e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 4.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  767 VVEILLDNGadiEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 846
Cdd:PLN03192   509 VGDLLGDNG---GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  847 SRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrntALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLM 926
Cdd:PLN03192   586 IRDAN--GNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
                          170       180
                   ....*....|....*....|...
gi 2462596386  927 EAASGGYAEVGRVLLDKGADVNA 949
Cdd:PLN03192   661 VAMAEDHVDMVRLLIMNGADVDK 683
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
1368-1425 4.77e-06

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411865 [Multi-domain]  Cd Length: 69  Bit Score: 46.06  E-value: 4.77e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462596386 1368 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDK---TGDRIITIRGGTESTRQATQLI 1425
Cdd:cd22437      5 VPNSSCGLIIGKGGSTIKELREDSNANIKISPKDQLlpgSSERIVTITGSFDQVVKAVALI 65
KH-I_PCBP_rpt1 cd22438
first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
1373-1425 5.00e-06

first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411866 [Multi-domain]  Cd Length: 67  Bit Score: 46.10  E-value: 5.00e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1373 ISRVIGRGGCNINAIREFTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLI 1425
Cdd:cd22438     10 VGSIIGKKGETIKKFREESGARINI--SDGSCPERIVTVTGTTDAVFKAFELI 60
KH-I_FUBP3_rpt4 cd22489
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1367-1426 5.18e-06

fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411917 [Multi-domain]  Cd Length: 69  Bit Score: 46.08  E-value: 5.18e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1367 SVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGD---RIITIRGGTESTRQATQLIN 1426
Cdd:cd22489      5 TIPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNTDpnvRIFTIRGVPQQIEHARQLID 67
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
386-418 5.74e-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: 44.97  E-value: 5.74e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462596386  386 EGYTPLMEAA-REGHEEMVALLLGQGANINAQTE 418
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1744-1953 5.84e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 51.69  E-value: 5.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1744 QQQPPgsVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPVTYPMPQTPMGCPQP-TPKMETPAIRPP----P 1818
Cdd:pfam03154  168 QTQPP--VLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPhTLIQQTPTLHPQrlpsP 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1819 HGTTAPhknsasvqnssvavlsvnhikRPHSVPssvqlPSTLSTQSACQNSVHPANKPIA-------PNFSAPLPFGPFS 1891
Cdd:pfam03154  246 HPPLQP---------------------MTQPPP-----PSQVSPQPLPQPSLHGQMPPMPhslqtgpSHMQHPVPPQPFP 299
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386 1892 TLFENS----PTSAHAFWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSkAPGFRPPLQRPAP 1953
Cdd:pfam03154  300 LTPQSSqsqvPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLS-MPHIKPPPTTPIP 364
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1368-1429 6.13e-06

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH2 domain of PEPPER and FLK, as well as KH2 and KH4 domains of RCF3 and HEN4.


Pssm-ID: 411888 [Multi-domain]  Cd Length: 73  Bit Score: 46.07  E-value: 6.13e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386 1368 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDK-----TGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22460      6 VASSQAGSLIGKGGAIIKQIREESGASVRILPEEELppcasPDDRVVQISGEAQAVKKALELVSSRL 72
Ank_4 pfam13637
Ankyrin repeats (many copies);
788-839 6.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 6.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  788 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILL 839
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1364-1430 6.50e-06

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 45.64  E-value: 6.50e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386 1364 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDriITIRGGTESTRQATQLINALIK 1430
Cdd:cd02394      4 TTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDE--IRIEGSPEGVKKAKAEILELVD 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
754-806 7.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 7.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462596386  754 TPLILAATAGHVGVVEILLDNGADIEAQSERtKDTPLSLACSGGRQEVVELLL 806
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
854-1010 7.75e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 51.03  E-value: 7.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  854 GISPLMLAAMN---GHTAAVKLLLDMGSD-------INAQIETNR---NTALTLACFQGRTEVVSLLLDRKANVEHRA-- 918
Cdd:cd21882     26 GKTCLHKAALNlndGVNEAIMLLLEAAPDsgnpkelVNAPCTDEFyqgQTALHIAIENRNLNLVRLLVENGADVSARAtg 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  919 ----KTGLT-------PLMEAASGGYAEVGRVLLDKGADvnaPPVPSSRDT-------ALTIAADK--GHYKFC----EL 974
Cdd:cd21882    106 rffrKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQ---PAALEAQDSlgntvlhALVLQADNtpENSAFVcqmyNL 182
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2462596386  975 LIGRGAHID-------VRNKKGNTPLWLAANGGHLDVVQLLVQ 1010
Cdd:cd21882    183 LLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
PRK11633 PRK11633
cell division protein DedD; Provisional
1746-1855 8.50e-06

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 49.23  E-value: 8.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1746 QPPGSVSQEPR------PPLQQSQVPPPEVRMTVPPlatssAPVAVPSTAPVTYPMPQT---PMGCPQPTPKmetPAIRP 1816
Cdd:PRK11633    66 QPPEGAAEAVRagdaaaPSLDPATVAPPNTPVEPEP-----APVEPPKPKPVEKPKPKPkpqQKVEAPPAPK---PEPKP 137
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462596386 1817 PPHGTTAPH-----------KNSASVqNSSVAVLSVNHIkRPHSVPSS-VQ 1855
Cdd:PRK11633   138 VVEEKAAPTgkayvvqlgalKNADKV-NEIVAKLRLSGY-RVYTVPSTpVQ 186
Ank_4 pfam13637
Ankyrin repeats (many copies);
921-976 8.57e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 8.57e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386  921 GLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLI 976
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
273-325 8.67e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 8.67e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462596386  273 LLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTAL 325
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
925-1008 8.82e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 8.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  925 LMEAASGGYAEVGRVLLDKGADvnappvPSSRD----TALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGG 1000
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGAD------PNCRDydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159

                   ....*...
gi 2462596386 1001 HLDVVQLL 1008
Cdd:PTZ00322   160 FREVVQLL 167
PHA02875 PHA02875
ankyrin repeat protein; Provisional
455-606 8.95e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 8.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  455 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQ 534
Cdd:PHA02875     6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  535 FLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDY 606
Cdd:PHA02875    86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
207-258 9.47e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 9.47e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462596386  207 LLAHK-ADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL 258
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
988-1017 1.04e-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: 44.12  E-value: 1.04e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2462596386   988 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1017
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
386-415 1.08e-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: 44.12  E-value: 1.08e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 2462596386   386 EGYTPLMEAAREGHEEMVALLLGQGANINA 415
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
258-362 1.08e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  258 LMEAGSAGHVEVARLLLENGAgiNTHSNEFKESA-LTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEV 336
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGA--DPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462596386  337 ARLLL-----DSGAQVNMPADSF--------ESPLTLAA 362
Cdd:PTZ00322   164 VQLLSrhsqcHFELGANAKPDSFtgkppsleDSPISSHH 202
Ank_5 pfam13857
Ankyrin repeats (many copies);
190-228 1.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.15e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462596386  190 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYA 228
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
1370-1431 1.15e-05

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation.


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 44.97  E-value: 1.15e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386 1370 STVISRVIGRGGCNINAIREFTGAHIDIDKQKDktgDRIITIRGGTESTRQATQLINALIKD 1431
Cdd:cd22430      8 SSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQ---EAEVKIFGSDEAQQKAKELIDELVGR 66
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
310-408 1.20e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  310 AGADQEHKTDE------MHTALMEAC---MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASL 380
Cdd:PTZ00322    62 ATPDHNLTTEEvidpvvAHMLTVELCqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
                           90       100
                   ....*....|....*....|....*...
gi 2462596386  381 EEVNDEGYTPLMEAAREGHEEMVALLLG 408
Cdd:PTZ00322   142 TLLDKDGKTPLELAEENGFREVVQLLSR 169
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1365-1434 1.21e-05

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 44.89  E-value: 1.21e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIdKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDK 1434
Cdd:cd22417      4 TVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQF-PDKGDENDDEITITGYEKNAEAAKDAILKIVQELES 72
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1660-2080 1.44e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.55  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1660 PTNATYPMPTAkehypvsspsspsppaqpggvsrNSPLdcgsASPNKVASSSEQEAGSPPVVET----TNTRPPNSSSSS 1735
Cdd:PHA03307    22 PRPPATPGDAA-----------------------DDLL----SGSQGQLVSDSAELAAVTVVAGaaacDRFEPPTGPPPG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1736 GSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAV---PSTAPVTYPMPQTPmGCPQPTPKMETP 1812
Cdd:PHA03307    75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPAsppPSPAPDLSEMLRPV-GSPGPPPAASPP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1813 AIRPPPHGTTAPHKNSASvqnSSVAVLSVNHIKRPHSVPSSVQLPSTLSTqsACQNSVHPANKPIAPNFSAPLPFGPFST 1892
Cdd:PHA03307   154 AAGASPAAVASDAASSRQ---AALPLSSPEETARAPSSPPAEPPPSTPPA--AASPRPPRRSSPISASASSPAPAPGRSA 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1893 LFENSPTSahafwggsvvSSQSTPESMLSGKSSYLPNSDPLHQSDTSK----------APGFRPPLQRPAPSPSGivnmd 1962
Cdd:PHA03307   229 ADDAGASS----------SDSSSSESSGCGWGPENECPLPRPAPITLPtriweasgwnGPSSRPGPASSSSSPRE----- 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1963 sPYGSVTPSSTHLGNFASNISggqmygpgaplggapAAANFNRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSPA-PS 2041
Cdd:PHA03307   294 -RSPSPSPSSPGSGPAPSSPR---------------ASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSrPP 357
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2462596386 2042 SVPLGSEKPSNVSQDRKVPVPIGTERSARIRQTGTSAPS 2080
Cdd:PHA03307   358 PPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAG 396
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
758-862 1.83e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  758 LAATAGHVGVvEILLDNGADIEAQsERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKI 837
Cdd:PTZ00322    89 LAASGDAVGA-RILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462596386  838 LL---------NAGAEINSRTG--SKLGISPLMLAA 862
Cdd:PTZ00322   167 LSrhsqchfelGANAKPDSFTGkpPSLEDSPISSHH 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
974-1041 1.91e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.91e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  974 LLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYL 1041
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
862-951 2.08e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  862 AMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 941
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
                           90
                   ....*....|....*
gi 2462596386  942 -----DKGADVNAPP 951
Cdd:PTZ00322   169 rhsqcHFELGANAKP 183
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
190-217 2.38e-05

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: 43.05  E-value: 2.38e-05
                           10        20
                   ....*....|....*....|....*....
gi 2462596386  190 TPLMAAA-NGGHVKIVKLLLAHKADVNAQ 217
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
123-376 2.66e-05

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: 49.69  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  123 RSLAEACSEGDVNAVRKLLIEGRSVNEHTEE--GESLLCLACSAG-YYELAQVLLamhaNVEDRGIKGDiTPLMAAANGg 199
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLL----NLSCRGAVGD-TLLHAISLE- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  200 HVKIVKLLLAHKADvnAQSSTGNTALTYACAGG--YVDvvkvllesgasiedhnengHTPLMEAGSAGHVEVARLLLENG 277
Cdd:TIGR00870   93 YVDAVEAILLHLLA--AFRKSGPLELANDQYTSefTPG-------------------ITALHLAAHRQNYEIVKLLLERG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  278 AGINT--HSNEFKESALT---------LACYK--GHLEMVRFLLEAGADQEhKTDEM-----HTALMEA----------- 328
Cdd:TIGR00870  152 ASVPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelsc 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462596386  329 -CMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 376
Cdd:TIGR00870  231 qMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
304-373 2.85e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 2.85e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  304 VRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALL 373
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
KH-I_NOVA_rpt1 cd22435
first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
1365-1425 2.94e-05

first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411863 [Multi-domain]  Cd Length: 73  Bit Score: 44.07  E-value: 2.94e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462596386 1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1425
Cdd:cd22435      5 KLLVPNYAAGSIIGKGGQTIAQLQKETGARIKLSKNNDfypGTTERVCLIQGEVEAVNAVLDFI 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
1522-1975 3.06e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1522 PPPQFAHALLAAQTFQQIRPPRL------PMTHFGGTFP--PAQSTWGPFPVRPLSPARAT---NSPKPHMVPRHSNQNS 1590
Cdd:PHA03247  2551 PPPPLPPAAPPAAPDRSVPPPRPaprpsePAVTSRARRPdaPPQSARPRAPVDDRGDPRGPappSPLPPDTHAPDPPPPS 2630
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1591 SGSQVNSAGSLTSSPTTttsssastvPGTSTNGSPSSPSVRRQLFVTVVKTSNATTTTVTTTASNNNTAP----TNATYP 1666
Cdd:PHA03247  2631 PSPAANEPDPHPPPTVP---------PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgslTSLADP 2701
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1667 MPTAKEHYPVSSPSSPSPPAQPGgvsrnsPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSSAHsnqqq 1746
Cdd:PHA03247  2702 PPPPPTPEPAPHALVSATPLPPG------PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA----- 2770
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1747 PPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPV-TYPMPQTPMGcPQPTPKMETPAIRPPPHGTTAPh 1825
Cdd:PHA03247  2771 PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAaALPPAASPAG-PLPPPTSAQPTAPPPPPGPPPP- 2848
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1826 knSASVQNSSVAVLSVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIA--PNFSAPLPFGPFSTLFENSPTSAHA 1903
Cdd:PHA03247  2849 --SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAlpPDQPERPPQPQAPPPPQPQPQPPPP 2926
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1904 FWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDT---------------SKAPGFRPPLQRPAPSPSGIVNMDSPYGSV 1968
Cdd:PHA03247  2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgalvpgrvavprFRVPQPAPSREAPASSTPPLTGHSLSRVSS 3006

                   ....*..
gi 2462596386 1969 TPSSTHL 1975
Cdd:PHA03247  3007 WASSLAL 3013
Ank_5 pfam13857
Ankyrin repeats (many copies);
446-491 3.57e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 3.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462596386  446 DIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYA 491
Cdd:pfam13857   11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
854-882 4.36e-05

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: 42.24  E-value: 4.36e-05
                           10        20
                   ....*....|....*....|....*....
gi 2462596386  854 GISPLMLAAMNGHTAAVKLLLDMGSDINA 882
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
228-381 4.61e-05

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: 48.54  E-value: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  228 ACAGGYVDVVKVLLESGAS--IEDHNENGHTPLMEAGSAG-HVEVARLLLENGAGINThsnefKESALTLAC--YKGHLE 302
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV-----GDTLLHAISleYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  303 MVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ESP 357
Cdd:TIGR00870   99 AILLHLLAAFRKsgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgESP 178
                          170       180
                   ....*....|....*....|....
gi 2462596386  358 LTLAACGGHVELAALLIERGASLE 381
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADIL 202
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1363-1431 4.65e-05

fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fifth one.


Pssm-ID: 411837 [Multi-domain]  Cd Length: 70  Bit Score: 43.34  E-value: 4.65e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIR-EFTGAHIDIDKQKDKtgdriITIRGGTESTRQATQLINALIKD 1431
Cdd:cd22409      3 VAEVSAPSWLHRFIIGKKGANIKKITqDLPKVHIEFTEGEDK-----IELEGPPEEVEVVREQLEAIVKE 67
Ank_4 pfam13637
Ankyrin repeats (many copies);
888-941 4.83e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 4.83e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  888 RNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 941
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
213-407 4.97e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 48.34  E-value: 4.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  213 DVNAQSSTGNTALTYAC---AGGYVDVVKVLLESG-----------ASIEDHNENGHTPLMEAGSAGHVEVARLLLENGA 278
Cdd:cd21882     18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAApdsgnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  279 GINTHSN------------EFKESALTLACYKGHLEMVRFLLEAGAD--QEHKTDEMHTALMEACmdghVEVARLLLDSG 344
Cdd:cd21882     98 DVSARATgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQpaALEAQDSLGNTVLHAL----VLQADNTPENS 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462596386  345 AQVnmpADSFESPLTLAACGGHVElaalliergaSLEEV-NDEGYTPLMEAAREGHEEMVALLL 407
Cdd:cd21882    174 AFV---CQMYNLLLSYGAHLDPTQ----------QLEEIpNHQGLTPLKLAAVEGKIVMFQHIL 224
PHA02859 PHA02859
ankyrin repeat protein; Provisional
201-315 5.03e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.74  E-value: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  201 VKIVKLLLAHKADVNAQSSTGNTAL--TYACAGGYV--DVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLL 273
Cdd:PHA02859    66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV-RINVIKLL 144
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462596386  274 LENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQE 315
Cdd:PHA02859   145 IDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDIN 186
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1377-1425 5.12e-05

tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the tenth one.


Pssm-ID: 411841 [Multi-domain]  Cd Length: 66  Bit Score: 43.02  E-value: 5.12e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462596386 1377 IGRGGCNINAIREFTGAHIDIDKQKDKTGDrIITIRGGTESTRQATQLI 1425
Cdd:cd22413     18 IGRGGANIRKIRDNTGARIIFPTARDEDQE-LITIIGTKEAVEKAKEEL 65
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
1365-1429 5.30e-05

type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic translation initiation factor 4E-binding protein Mextli and similar proteins; Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster.


Pssm-ID: 411882 [Multi-domain]  Cd Length: 71  Bit Score: 43.07  E-value: 5.30e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386 1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22454      7 EVVIPNADVGKVIGKGGETIKRIEALTDTVITFERVNGGSPNREVQITGSPDNVAAAKRLIEDTI 71
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
751-781 5.59e-05

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: 41.89  E-value: 5.59e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462596386  751 KGFTPLILAAT-AGHVGVVEILLDNGADIEAQ 781
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
452-538 5.92e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 5.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  452 STPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVC 531
Cdd:PTZ00322    83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                   ....*..
gi 2462596386  532 TVQFLIS 538
Cdd:PTZ00322   163 VVQLLSR 169
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
453-481 6.22e-05

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: 41.89  E-value: 6.22e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462596386  453 TPLMEAA-QEGHLELVKYLLAAGANVHATT 481
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
517-547 6.35e-05

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: 41.89  E-value: 6.35e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462596386  517 GRTPLMKAA-RAGHVCTVQFLISKGANVNRTT 547
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
854-882 6.97e-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: 41.80  E-value: 6.97e-05
                            10        20
                    ....*....|....*....|....*....
gi 2462596386   854 GISPLMLAAMNGHTAAVKLLLDMGSDINA 882
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
KH-I_FUBP2_rpt1 cd22479
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1363-1429 8.20e-05

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 2 (FUBP2) and similar proteins; FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP2 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411907 [Multi-domain]  Cd Length: 71  Bit Score: 42.62  E-value: 8.20e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22479      2 TEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGSPEAVQKAKMMLDDIV 68
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
386-415 1.00e-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: 41.09  E-value: 1.00e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462596386  386 EGYTPLMEAAREGHEEMVALLLGQGANINA 415
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_MER1_like cd22458
type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic ...
1364-1425 1.10e-04

type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic recombination 1 protein (MER1) and similar proteins; MER1 is required for chromosome pairing and genetic recombination. It may function to bring the axial elements of the synaptonemal complex corresponding to homologous chromosomes together by initiating recombination. MER1 might be responsible for regulating the MER2 gene and/or gene product.


Pssm-ID: 411886 [Multi-domain]  Cd Length: 65  Bit Score: 42.05  E-value: 1.10e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386 1364 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTgDRIITIRGGTESTRQATQLI 1425
Cdd:cd22458      3 WEIKLPQALCGRLIGAKGKNIKALSEKSGASIRLIPISNSS-QQTIHLSGTDKQIALAISSI 63
KH-I_RCF3_like_rpt5 cd22463
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1366-1429 1.19e-04

fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein RCF3 and similar protein; RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of RCF3.


Pssm-ID: 411891 [Multi-domain]  Cd Length: 71  Bit Score: 42.42  E-value: 1.19e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386 1366 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD--KTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22463      6 FQIPEAVVGLIIGKSGNTIKQISERSGAFVAIVQDRYplEETQKILRISGTEEQLKRAQSLVEGLI 71
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
751-780 1.24e-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: 1.24e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2462596386   751 KGFTPLILAATAGHVGVVEILLDNGADIEA 780
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
1778-1976 1.26e-04

Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase.


Pssm-ID: 430088 [Multi-domain]  Cd Length: 684  Bit Score: 47.13  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1778 TSSAPVAVPSTaPVTYPMPQTPMGCPQPTPKMETPAIRPPPHGTTAPHKNSASVQNSsvavLSVNHIKRPHSVPSSvqlP 1857
Cdd:pfam08580  491 PSKIPRASPNH-SGFLSTPSNTATSETPTPALRPPSRPQPPPPGNRPRWNASTNTND----LDVGHNFKPLTLTTP---S 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1858 STLSTQSACQNSVHPANKPIAPNFSAPLPFGPFSTLFENSPTSAHAfwggSVVSSQSTPESMLsgkssylpNSDPLHQSD 1937
Cdd:pfam08580  563 PTPSRSSRSSSTLPPVSPLSRDKSRSPAPTCRSVSRASRRRASRKP----TRIGSPNSRTSLL--------DEPPYPKLT 630
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462596386 1938 TSKAPGfRPPLQRP---APSPSGIVNMDSPYGSVTPSSTHLG 1976
Cdd:pfam08580  631 LSKGLP-RTPRNRQsyaGTSPSRSVSVSSGLGPQTRPGTSLG 671
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
453-479 1.29e-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: 1.29e-04
                            10        20
                    ....*....|....*....|....*..
gi 2462596386   453 TPLMEAAQEGHLELVKYLLAAGANVHA 479
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
253-281 1.30e-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: 41.12  E-value: 1.30e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462596386  253 NGHTPLMEA-GSAGHVEVARLLLENGAGIN 281
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVN 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
767-897 1.35e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  767 VVEILLDNGADIEAQsERTKDTPLSLACSGGRQ-----EVVELLLARGANKEHRNVSDYTPLSLAASGGYVN---IIKIL 838
Cdd:PHA02798    53 IVKLFINLGANVNGL-DNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINnleILLFM 131
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  839 LNAGAEINSRtgSKLGISPLMLAAMNGHTA---AVKLLLDMGSDINaqIETNRNTALTLACF 897
Cdd:PHA02798   132 IENGADTTLL--DKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDIN--THNNKEKYDTLHCY 189
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
517-544 1.46e-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: 40.65  E-value: 1.46e-04
                            10        20
                    ....*....|....*....|....*...
gi 2462596386   517 GRTPLMKAARAGHVCTVQFLISKGANVN 544
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
KH-I_IGF2BP_rpt4 cd22403
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1366-1421 1.50e-04

fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/CRD-BP/VICKZ1, IGF2BP2/IMP-2/VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the fourth one.


Pssm-ID: 411831 [Multi-domain]  Cd Length: 66  Bit Score: 41.84  E-value: 1.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386 1366 VSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTGDRIITIRGGTESTRQA 1421
Cdd:cd22403      4 IRVPSSMVGRIIGKGGQNVRELQRLTGAIIKLprDQTPDEGDEVPVEIIGNFYATQSA 61
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
235-409 1.58e-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: 47.06  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  235 DVVKVLLEsgASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGIN----------THSNE---FKESALTLACYKGHL 301
Cdd:cd22194    124 GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEgfyFGETPLALAACTNQP 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  302 EMVRFLLEAGADQEHKTDEMHTALMEACmdghVEVARlllDSGAQVNMPADSFESPLTlaACGGHvelaalliergaSLE 381
Cdd:cd22194    202 EIVQLLMEKESTDITSQDSRGNTVLHAL----VTVAE---DSKTQNDFVKRMYDMILL--KSENK------------NLE 260
                          170       180
                   ....*....|....*....|....*....
gi 2462596386  382 EV-NDEGYTPLMEAAREGHEEMVALLLGQ 409
Cdd:cd22194    261 TIrNNEGLTPLQLAAKMGKAEILKYILSR 289
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
484-511 1.72e-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: 40.65  E-value: 1.72e-04
                            10        20
                    ....*....|....*....|....*...
gi 2462596386   484 GDTALTYACENGHTDVADVLLQAGADLE 511
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
221-249 1.74e-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: 40.65  E-value: 1.74e-04
                            10        20
                    ....*....|....*....|....*....
gi 2462596386   221 GNTALTYACAGGYVDVVKVLLESGASIED 249
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
373-428 1.93e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 1.93e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386  373 LIERG-ASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETqETALTLA 428
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
711-840 2.20e-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: 46.29  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  711 IDAQ-TESNHD--TALTLACAGGHEELVQTLLERGASIEHRDKKGF--------------TPLILAATAGHVGVVEILLD 773
Cdd:cd22194    130 INAEyTEEAYEgqTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLME 209
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386  774 NGADIEAQSERTKDTPL---------SLACSGGRQEVVELLLARGANKE---HRNVSDYTPLSLAASGGYVNIIKILLN 840
Cdd:cd22194    210 KESTDITSQDSRGNTVLhalvtvaedSKTQNDFVKRMYDMILLKSENKNletIRNNEGLTPLQLAAKMGKAEILKYILS 288
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
935-1088 2.30e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  935 EVGRVLLDKGADVNAPPVPSSrdtALTIAAdKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGAD 1014
Cdd:PLN03192   508 NVGDLLGDNGGEHDDPNMASN---LLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1015 VDAADNRKITPLMAAFRKGHVKVVRYLvkevNQFPSDS------ECMRYIATITDKEMLKKChLCMESIVQAKDRQAAEA 1088
Cdd:PLN03192   584 VHIRDANGNTALWNAISAKHHKIFRIL----YHFASISdphaagDLLCTAAKRNDLTAMKEL-LKQGLNVDSEDHQGATA 658
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
121-341 2.31e-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: 46.61  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  121 DNRSLAEACSEGDVNAVRKLLIEgrsVNEHTEEGESLLcLACSAGYY----ELAQVLLAMH--------ANVEDRG-IKG 187
Cdd:TIGR00870   52 GRSALFVAAIENENLELTELLLN---LSCRGAVGDTLL-HAISLEYVdaveAILLHLLAAFrksgplelANDQYTSeFTP 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  188 DITPLMAAANGGHVKIVKLLLAHKADVNA-------QSSTGNTAL--------TYACAGGYvDVVKVLLESGASIEDHNE 252
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFyhgesplnAAACLGSP-SIVALLSEDPADILTADS 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  253 NGHTplmeagsaghveVARLLLENgaginthsNEFKESALTLACykghlEMVRFLLEAGaDQEHKTDEMH--------TA 324
Cdd:TIGR00870  207 LGNT------------LLHLLVME--------NEFKAEYEELSC-----QMYNFALSLL-DKLRDSKELEvilnhqglTP 260
                          250
                   ....*....|....*..
gi 2462596386  325 LMEACMDGHVEVARLLL 341
Cdd:TIGR00870  261 LKLAAKEGRIVLFRLKL 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
190-216 2.45e-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: 40.26  E-value: 2.45e-04
                            10        20
                    ....*....|....*....|....*..
gi 2462596386   190 TPLMAAANGGHVKIVKLLLAHKADVNA 216
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
854-883 2.53e-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: 2.53e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462596386  854 GISPLMLAA-MNGHTAAVKLLLDMGSDINAQ 883
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
158-251 2.57e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  158 LCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVV 237
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                           90
                   ....*....|....
gi 2462596386  238 KVLleSGASIEDHN 251
Cdd:PTZ00322   165 QLL--SRHSQCHFE 176
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
1362-1438 2.91e-04

Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 46.15  E-value: 2.91e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386 1362 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqkDktgDRIITIrGGT--ESTRQATQLINALIKDPdkEIDE 1438
Cdd:COG1185    549 RIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIE---D---DGTVKI-AATdgEAAEKAIERIEGITAEP--EVGE 618
Ank_5 pfam13857
Ankyrin repeats (many copies);
771-826 3.35e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 3.35e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386  771 LLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLA 826
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
1362-1438 3.88e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.81  E-value: 3.88e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386 1362 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDPdkEIDE 1438
Cdd:PRK11824   554 RIETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIED------DGTVKIAATDgEAAEAAKERIEGITAEP--EVGE 623
PHA02946 PHA02946
ankyin-like protein; Provisional
729-925 3.89e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 3.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  729 GGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKdTPLSLaCSGGRQEVVE---LL 805
Cdd:PHA02946    49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHK-TPLYY-LSGTDDEVIErinLL 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  806 LARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEinSRTGSKLGISPL--MLAAMNGHTAAVKLLLDMGSDiNAQ 883
Cdd:PHA02946   127 VQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFE--ARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGIS-PSK 203
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462596386  884 IETNRNTALTLACFQ--GRTEVVSLLLDrKANVEHRAKTGLTPL 925
Cdd:PHA02946   204 PDHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPL 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
838-895 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        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  838 LLNAGAeINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLA 895
Cdd:pfam13857    1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK-DEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
982-1026 4.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 4.33e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462596386  982 IDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1026
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02884 PHA02884
ankyrin repeat protein; Provisional
233-330 4.42e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.59  E-value: 4.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  233 YVDVVKVLLESGASIE---DHNENGHT-PLMEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLL 308
Cdd:PHA02884    45 YTDIIDAILKLGADPEapfPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
                           90       100
                   ....*....|....*....|..
gi 2462596386  309 EAGADQEHKTDEMHTALMEACM 330
Cdd:PHA02884   125 SYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
517-544 4.51e-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: 4.51e-04
                           10        20
                   ....*....|....*....|....*...
gi 2462596386  517 GRTPLMKAARAGHVCTVQFLISKGANVN 544
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
423-471 4.82e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 4.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  423 TALTLACCGGFLEVADFLIKAGADI---ELGCSTPLMEAAQEGHLELVKYLL 471
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADInavDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
988-1017 5.94e-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: 39.16  E-value: 5.94e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462596386  988 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1017
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
402-612 6.52e-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: 44.75  E-value: 6.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  402 MVALLlgqgaNINAQTEETQETALTLACCGGFLEVadfLIKAGADIE-LGCSTPLMEAAQEGHLELVKYLLAAGANVHAt 480
Cdd:cd22194     99 MKALL-----NINENTKEIVRILLAFAEENGILDR---FINAEYTEEaYEGQTALNIAIERRQGDIVKLLIAKGADVNA- 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  481 TATGdtaltyacenghtdvadVLLQAgadlEHESEG---GRTPLMKAAraghvCT-----VQFLISKGANVNRTTANNDH 552
Cdd:cd22194    170 HAKG-----------------VFFNP----KYKHEGfyfGETPLALAA-----CTnqpeiVQLLMEKESTDITSQDSRGN 223
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386  553 TVL-SLACAG----GHLAVV-----ELLLAHGAD--PTHRLKDGSTMLIEAAKGGHTSVVCYLL-----DYPNNLLS 612
Cdd:cd22194    224 TVLhALVTVAedskTQNDFVkrmydMILLKSENKnlETIRNNEGLTPLQLAAKMGKAEILKYILsreikEKPNRSLS 300
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
322-349 7.28e-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: 38.72  E-value: 7.28e-04
                            10        20
                    ....*....|....*....|....*...
gi 2462596386   322 HTALMEACMDGHVEVARLLLDSGAQVNM 349
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
253-281 7.80e-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: 38.72  E-value: 7.80e-04
                            10        20
                    ....*....|....*....|....*....
gi 2462596386   253 NGHTPLMEAGSAGHVEVARLLLENGAGIN 281
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
KH-I_IGF2BP2_rpt4 cd22500
fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
1366-1430 9.06e-04

fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2) and similar proteins; IGF2BP2, also called IGF2 mRNA-binding protein 2 (IMP-2), or hepatocellular carcinoma autoantigen p62, or IGF-II mRNA-binding protein 2, or VICKZ family member 2 (VICKZ2), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It also binds to beta-actin/ACTB and MYC transcripts. IGF2BP2 can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. It contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the fourth one.


Pssm-ID: 411928  Cd Length: 78  Bit Score: 40.12  E-value: 9.06e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386 1366 VSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTGDRIITIRGGTESTRQATQLINALIK 1430
Cdd:cd22500      6 IKVPSSAAGRVIGKGGKTVNELQNLTSAEVIVprDQTPDENEEVIVKIIGHFFASQTAQRKIREIVQ 72
Ank_5 pfam13857
Ankyrin repeats (many copies);
906-963 1.05e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  906 LLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIA 963
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK--DEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
718-746 1.11e-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: 38.34  E-value: 1.11e-03
                            10        20
                    ....*....|....*....|....*....
gi 2462596386   718 NHDTALTLACAGGHEELVQTLLERGASIE 746
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
720-867 1.11e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.23  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  720 DTALTLACAGGHEELVQTLLERGAS-----IEHRDKKGFTPLILAATAGHVGVVEILLDNGADIeaQSERTKDT------ 788
Cdd:cd22192     52 ETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLVRELIARGADV--VSPRATGTffrpgp 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  789 ---------PLSLACSGGRQEVVELLLARGANKEHRNVSDYTP---LSLAASGGYV-NIIKILLNAGAEINSRTGSKL-- 853
Cdd:cd22192    130 knliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVlhiLVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVpn 209
                          170
                   ....*....|....*.
gi 2462596386  854 --GISPLMLAAMNGHT 867
Cdd:cd22192    210 nqGLTPFKLAAKEGNI 225
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1761-1955 1.14e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.31  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1761 QSQVPPPEVRMTVPPLATSSAPVAVPSTAPVTYPMPQTPmgcpqptpkmeTPAIRPPPHGTTaPHKNSASVQNSSVAvls 1840
Cdd:PRK10263   331 QSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTG-----------EPVIAPAPEGYP-QQSQYAQPAVQYNE--- 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1841 vnHIKRPHSVPSSVQLPSTLSTQSACQNSVHPAnKPIAPNFSAPLPFGPfstlfensptSAHAFWGGSVVSSQSTPESML 1920
Cdd:PRK10263   396 --PLQQPVQPQQPYYAPAAEQPAQQPYYAPAPE-QPAQQPYYAPAPEQP----------VAGNAWQAEEQQSTFAPQSTY 462
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2462596386 1921 SGKSSYLpnsDPLHQSDTSKAPGFRPPLQRPAPSP 1955
Cdd:PRK10263   463 QTEQTYQ---QPAAQEPLYQQPQPVEQQPVVEPEP 494
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1747-1879 1.17e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.93  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1747 PPGSVSQEPRPPLQQSQVPPPevrmtVPPLATSSAPVAVPSTAPVTYPMPQTPmgcPQPTPKMETPAIRPPPhgttAPHK 1826
Cdd:PRK14951   373 AAPAEKKTPARPEAAAPAAAP-----VAQAAAAPAPAAAPAAAASAPAAPPAA---APPAPVAAPAAAAPAA----APAA 440
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1827 NSASVQNSSVAvlSVNHIKRPHSVPSSVQlPSTLSTQSACQNSVHPANKPIAP 1879
Cdd:PRK14951   441 APAAVALAPAP--PAQAAPETVAIPVRVA-PEPAVASAAPAPAAAPAAARLTP 490
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
819-846 1.26e-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: 37.95  E-value: 1.26e-03
                            10        20
                    ....*....|....*....|....*...
gi 2462596386   819 DYTPLSLAASGGYVNIIKILLNAGAEIN 846
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
723-911 1.29e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.92  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  723 LTLACAGGHEELVQTLLERGASIEHRDKkgftpLILAATAGHVGVVE----ILLDNGADI--------EAQSERTKD-TP 789
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDAVEaillHLLAAFRKSgplelandQYTSEFTPGiTA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  790 LSLACSGGRQEVVELLLARGAN------------KEHRNVSDYT--PLSLAASGGYVNIIKILLNAGAEInsRTGSKLGI 855
Cdd:TIGR00870  132 LHLAAHRQNYEIVKLLLERGASvparacgdffvkSQGVDSFYHGesPLNAAACLGSPSIVALLSEDPADI--LTADSLGN 209
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462596386  856 SPLMLAAMNGHTAAV---------KLLLDMG--SDINAQIE--TNRN--TALTLACFQGRTEVVSLLLDRK 911
Cdd:TIGR00870  210 TLLHLLVMENEFKAEyeelscqmyNFALSLLdkLRDSKELEviLNHQglTPLKLAAKEGRIVLFRLKLAIK 280
KH-I_Rnc1_rpt1 cd22455
first type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
1376-1425 1.35e-03

first type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding protein Rnc1 and similar proteins; Rnc1, also called RNA-binding protein that suppresses calcineurin deletion 1, is an RNA-binding protein that acts as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. It binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression of Rnc1 suppresses the Cl(-) sensitivity of calcineurin deletion. The nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. Rnc1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411883  Cd Length: 70  Bit Score: 39.20  E-value: 1.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1376 VIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLI 1425
Cdd:cd22455     15 IIGKGGENIARLRATTGVKAGVSKVVPGVHDRVLTVSGPLEGVAKAFGLI 64
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
252-471 1.38e-03

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: 43.98  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  252 ENGHTPLMEAgsaghvevarlLLEngagINTHSNEFKESALTLACYKGHLEmvRFLleaGADQEHKTDEMHTALMEACMD 331
Cdd:cd22194     92 DTGKTCLMKA-----------LLN----INENTKEIVRILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIER 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  332 GHVEVARLLLDSGAQVNMPA-----------DSF---ESPLTLAACGGHVELAALLIERGAsleevndegyTPLMEAARE 397
Cdd:cd22194    152 RQGDIVKLLIAKGADVNAHAkgvffnpkykhEGFyfgETPLALAACTNQPEIVQLLMEKES----------TDITSQDSR 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  398 GHEEMVALLlgqganINAQTEETQETALTlaccggflEVADFLIKAGADIELGCS------TPLMEAAQEGHLELVKYLL 471
Cdd:cd22194    222 GNTVLHALV------TVAEDSKTQNDFVK--------RMYDMILLKSENKNLETIrnneglTPLQLAAKMGKAEILKYIL 287
KH-I_IGF2BP2_rpt2 cd22494
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
1365-1421 1.41e-03

second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2) and similar proteins; IGF2BP2, also called IGF2 mRNA-binding protein 2 (IMP-2), or hepatocellular carcinoma autoantigen p62, or IGF-II mRNA-binding protein 2, or VICKZ family member 2 (VICKZ2), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It also binds to beta-actin/ACTB and MYC transcripts. IGF2BP2 can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. It contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the second one.


Pssm-ID: 411922  Cd Length: 77  Bit Score: 39.63  E-value: 1.41e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKT---GDRIITIRGGTESTRQA 1421
Cdd:cd22494      3 KILAHNSLVGRLIGKEGRNLKKIEQDTGTKITISSLQDLTiynPERTITVKGSIEACSSA 62
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
718-750 1.44e-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: 1.44e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462596386  718 NHDTALTLACA-GGHEELVQTLLERGASIEHRDK 750
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
804-861 1.50e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  804 LLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLA 861
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE--GLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
733-846 1.70e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  733 ELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL---DNGADIEAQSERTKdTPLSLACSGGRQ---EVVELLL 806
Cdd:PHA02798    90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGF-TMLQVYLQSNHHidiEIIKLLL 168
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462596386  807 ARGAN-KEHRNVSDYTPLSLAASGGY----VNIIKILLNAGAEIN 846
Cdd:PHA02798   169 EKGVDiNTHNNKEKYDTLHCYFKYNIdridADILKLFVDNGFIIN 213
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
721-772 1.71e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 1.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  721 TALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL 772
Cdd:PTZ00322   117 TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
756-1010 1.89e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  756 LILAATAGHVGVVEILLDNGADIEAQS-ERTKDTPLSLACSGGR-QEVVELLLarganKEHRNVSDYTPLSLAASGGYVN 833
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEPKKLNINCpDRLGRSALFVAAIENEnLELTELLL-----NLSCRGAVGDTLLHAISLEYVD 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  834 ----IIKILLNAGAE------INSRTGSKL--GISPLMLAAMNGHTAAVKLLLDMGSDINAQietnrntaltlAC---FQ 898
Cdd:TIGR00870   96 aveaILLHLLAAFRKsgplelANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPAR-----------ACgdfFV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  899 GRTEVVSLLLDRkanvehraktglTPLMEAASGGYAEVGRVLLDKGADVNAppvpssRDT-------ALTIAAD-KGHYK 970
Cdd:TIGR00870  165 KSQGVDSFYHGE------------SPLNAAACLGSPSIVALLSEDPADILT------ADSlgntllhLLVMENEfKAEYE 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  971 F----C-ELLIGRGAHID-------VRNKKGNTPLWLAANGGHLDVVQLLVQ 1010
Cdd:TIGR00870  227 ElscqMyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLA 278
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
484-512 1.89e-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: 1.89e-03
                           10        20
                   ....*....|....*....|....*....
gi 2462596386  484 GDTALTYACENGHTDVADVLLQAGADLEH 512
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
503-558 1.95e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.95e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386  503 LLQAG-ADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDhTVLSLA 558
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1660-1986 2.07e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.37  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1660 PTNATYPMPTAKehypvSSPSSPSPPAQPGGVSRNSPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSS 1739
Cdd:pfam05109  455 PTNLTAPASTGP-----TVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTT 529
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1740 AHSNQQQP------PGSVSQEPRP----PLQQSQVPPPEVrmTVPPLATSSAPVAVPSTAP-VTYPM-----PQTPMGCP 1803
Cdd:pfam05109  530 PTPNATSPtlgktsPTSAVTTPTPnatsPTPAVTTPTPNA--TIPTLGKTSPTSAVTTPTPnATSPTvgetsPQANTTNH 607
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1804 QPTPKMETPAI-RPPPHGTTAPHKNSASVQNSSVAVLSVnhikRPHSVPSSVQlPSTLSTQSACQNSVHPANKPIAPNFS 1882
Cdd:pfam05109  608 TLGGTSSTPVVtSPPKNATSAVTTGQHNITSSSTSSMSL----RPSSISETLS-PSTSDNSTSHMPLLTSAHPTGGENIT 682
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1883 APLPfgpfstlfenSPTSAHafwggSVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFRPPLQRPAP-SPSGivnm 1961
Cdd:pfam05109  683 QVTP----------ASTSTH-----HVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPqAPSG---- 743
                          330       340
                   ....*....|....*....|....*
gi 2462596386 1962 dspYGSVTPSSTHLGNFASNISGGQ 1986
Cdd:pfam05109  744 ---QKTAVPTVTSTGGKANSTTGGK 765
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
237-308 2.17e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 2.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462596386  237 VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKeSALTLACYKGHLEMVRFLL 308
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLS 168
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
778-1006 2.21e-03

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: 43.21  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  778 IEAQSERTKDTPLSL--ACSGGRQEVVELLlargANKEHRN-------VSDYTPLSLAASG-GYVNIIKILLNagaeINS 847
Cdd:cd22194     36 AELAKEEQRDKKKRLkkVSEAAVEELGELL----KELKDLSrrrrktdVPDFLMHKLTASDtGKTCLMKALLN----INE 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  848 RTGSklgISPLMLAAMNGHTAAVKLlldmgsdINAQIeTNRN----TALTLACFQGRTEVVSLLLDRKANVEHRAKT--- 920
Cdd:cd22194    108 NTKE---IVRILLAFAEENGILDRF-------INAEY-TEEAyegqTALNIAIERRQGDIVKLLIAKGADVNAHAKGvff 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  921 -----------GLTPLMEAASGGYAEVGRVLLDKGADVNappvpSSRDT-------ALTIAAD--KGHYKFCE------L 974
Cdd:cd22194    177 npkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDI-----TSQDSrgntvlhALVTVAEdsKTQNDFVKrmydmiL 251
                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462596386  975 LIGRGAHID-VRNKKGNTPLWLAANGGHLDVVQ 1006
Cdd:cd22194    252 LKSENKNLEtIRNNEGLTPLQLAAKMGKAEILK 284
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
323-539 2.24e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.25  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  323 TALMEACM---DGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAaLLIERgasleevndegytplmeaaREGH 399
Cdd:cd22193     31 TCLMKALLnlnPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEGQTALH-IAIER-------------------RQGD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  400 eeMVALLLGQGANINAQTeetqetaltlacCGGFLEVADflikAGADIELGcSTPLMEAAQEGHLELVKYLLA---AGAN 476
Cdd:cd22193     91 --IVALLVENGADVHAHA------------KGRFFQPKY----QGEGFYFG-ELPLSLAACTNQPDIVQYLLEnehQPAD 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386  477 VHATTATGDT---ALTYACENGHTDVA------DVLLQAGADLEHESE-------GGRTPLMKAARAGHVCTVQFLISK 539
Cdd:cd22193    152 IEAQDSRGNTvlhALVTVADNTKENTKfvtrmyDMILIRGAKLCPTVEleeirnnDGLTPLQLAAKMGKIEILKYILQR 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
721-839 2.43e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  721 TALTLACAGGHEELVQTLLERGASIEHRDKKGF-------------TPLILAATAGHVGVVEILLDNGADIEAQSER--- 784
Cdd:cd21882     75 TALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGAQPAALEAQdsl 154
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386  785 -----------TKDTP--LSLACSggrqeVVELLLARGANKEH-------RNVSDYTPLSLAASGGYVNIIKILL 839
Cdd:cd21882    155 gntvlhalvlqADNTPenSAFVCQ-----MYNLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGKIVMFQHIL 224
KH-I_IGF2BP_rpt3 cd22402
third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1368-1425 2.47e-03

third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the third one.


Pssm-ID: 411830 [Multi-domain]  Cd Length: 66  Bit Score: 38.39  E-value: 2.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462596386 1368 VPSTVISRVIGRGGCNINAIREFTGAHIDI-DKQKDKTGDRIITIRGGTESTRQATQLI 1425
Cdd:cd22402      7 IPNKAVGAIIGTKGSHIRYIKRFSGASIKIaPADSPDAPERKVTITGPPEAQWKAQLCI 65
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
190-216 2.59e-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: 37.24  E-value: 2.59e-03
                           10        20
                   ....*....|....*....|....*..
gi 2462596386  190 TPLMAAANGGHVKIVKLLLAHKADVNA 216
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
285-414 2.96e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.34  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  285 NEFKESALtLACY---KGHLEMVRFLLEAGADQEHKTDEMHTALMEACM----DGHVEVARLLLDSGAQVNMPADSFESP 357
Cdd:PHA02859    48 NDLYETPI-FSCLekdKVNVEILKFLIENGADVNFKTRDNNLSALHHYLsfnkNVEPEILKILIDSGSSITEEDEDGKNL 126
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386  358 L--TLAACGGHVELAALLIERGASLEEVNDEG----YTPLMeaaREGHEEMVALLLGQGANIN 414
Cdd:PHA02859   127 LhmYMCNFNVRINVIKLLIDSGVSFLNKDFDNnnilYSYIL---FHSDKKIFDFLTSLGIDIN 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
290-313 3.03e-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: 3.03e-03
                            10        20
                    ....*....|....*....|....
gi 2462596386   290 SALTLACYKGHLEMVRFLLEAGAD 313
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGAD 27
KH-I_FUBP3_rpt1 cd22480
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1363-1429 3.11e-03

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411908 [Multi-domain]  Cd Length: 71  Bit Score: 38.34  E-value: 3.11e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22480      2 TEEYKVPDKMVGFIIGRGGEQISRIQLESGCKIQIAPDSGGMPERPCVLTGTPESIEQAKRLLGQIV 68
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
221-252 3.86e-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: 3.86e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462596386  221 GNTALTYACA-GGYVDVVKVLLESGASIEDHNE 252
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1366-1425 3.93e-03

fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourth one.


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 37.54  E-value: 3.93e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1366 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLI 1425
Cdd:cd22408      4 VEVPKSQHRFVIGPRGSTIQEILEETGCSVEV--PPNDSDSETITLRGPADKLGAALTLV 61
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
1796-1964 4.29e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 42.28  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1796 PQTPMGCPQPTPKMETPAIRPPPHgtTAPHKNSAS--------VQNSSVAVLSVNHIKRPHSVPSSVQLPSTLSTQS--- 1864
Cdd:PRK12727    60 SDTPATAAAPAPAPQAPTKPAAPV--HAPLKLSANanmsqrqrVASAAEDMIAAMALRQPVSVPRQAPAAAPVRAASips 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1865 -ACQNSVHPANKPIAPNFSAPLPFGPfSTLFENSPTSA----HAFWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDts 1939
Cdd:PRK12727   138 pAAQALAHAAAVRTAPRQEHALSAVP-EQLFADFLTTApvprAPVQAPVVAAPAPVPAIAAALAAHAAYAQDDDEQLD-- 214
                          170       180       190
                   ....*....|....*....|....*....|
gi 2462596386 1940 kAPGFR-----PPLQRPAPSPSGIVNMDSP 1964
Cdd:PRK12727   215 -DDGFDlddalPQILPPAALPPIVVAPAAP 243
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
732-874 4.33e-03

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: 42.05  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  732 EELVQTLLERG-----------ASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERT-------------KD 787
Cdd:cd22194    110 KEIVRILLAFAeengildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfGE 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  788 TPLSLACSGGRQEVVELLL-----------ARGANKEHR--NVSDytplslaASGGYVNIIK-----ILLNAGAEINSRT 849
Cdd:cd22194    190 TPLALAACTNQPEIVQLLMekestditsqdSRGNTVLHAlvTVAE-------DSKTQNDFVKrmydmILLKSENKNLETI 262
                          170       180
                   ....*....|....*....|....*
gi 2462596386  850 GSKLGISPLMLAAMNGHTAAVKLLL 874
Cdd:cd22194    263 RNNEGLTPLQLAAKMGKAEILKYIL 287
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
1361-1395 4.33e-03

second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) and similar proteins; BICC1, also called Bic-C, is a mammalian homologue of Drosophila Bicaudal-C (dBic-C). BICC1 functions as an RNA-binding protein that represses the translation of selected mRNAs to control development. It regulates gene expression and modulates cell proliferation and apoptosis. BICC1 is a negative regulator of Wnt signaling. Increased levels of BICC1 may be associated with depression. Besides, BICC1 is a genetic determinant of osteoblastogenesis and bone mineral density. BICC1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411849  Cd Length: 70  Bit Score: 37.71  E-value: 4.33e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462596386 1361 RRSKKVSVPSTVISRVIGRGGCNINAIREFTGAHI 1395
Cdd:cd22421      2 RVTLKMDVSHTDHSHVIGKGGNNIKKVMEDTGCHI 36
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
921-949 4.35e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 4.35e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462596386  921 GLTPLMEAA-SGGYAEVGRVLLDKGADVNA 949
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
821-956 4.63e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  821 TPLSLAASGGYVNIIKILLNAGAEINSR-----------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNR- 888
Cdd:cd21882     75 TALHIAIENRNLNLVRLLVENGADVSARatgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSl 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  889 -NTALTLACFQGR---------TEVVSLLLDRKANVEHRAK-------TGLTPLMEAASGGYAEVGRVLLDKgaDVNAPP 951
Cdd:cd21882    155 gNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQR--EFSGPY 232

                   ....*
gi 2462596386  952 VPSSR 956
Cdd:cd21882    233 QPLSR 237
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
800-944 4.67e-03

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: 42.05  E-value: 4.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  800 EVVELLLA---------RGANKEHRNvSDY---TPLSLAASGGYVNIIKILLNAGAEINSRT------------GSKLGI 855
Cdd:cd22194    111 EIVRILLAfaeengildRFINAEYTE-EAYegqTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykheGFYFGE 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  856 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNT---ALTLAC--FQGRTEVVSLLLD------RKANVEH-RAKTGLT 923
Cdd:cd22194    190 TPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTvlhALVTVAedSKTQNDFVKRMYDmillksENKNLETiRNNEGLT 269
                          170       180
                   ....*....|....*....|....*.
gi 2462596386  924 PLMEAASGGYAEV-----GRVLLDKG 944
Cdd:cd22194    270 PLQLAAKMGKAEIlkyilSREIKEKP 295
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
453-479 5.01e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 5.01e-03
                           10        20
                   ....*....|....*....|....*..
gi 2462596386  453 TPLMEAAQEGHLELVKYLLAAGANVHA 479
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_PCBP1_2_rpt2 cd22518
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
1365-1425 5.13e-03

second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411946 [Multi-domain]  Cd Length: 78  Bit Score: 37.79  E-value: 5.13e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTgDRIITIRGGTESTRQATQLI 1425
Cdd:cd22518     10 RLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVagDMLPNST-ERAITIAGIPQSIIECVKQI 71
KH-I_AtC3H36_like cd22464
type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana zinc finger CCCH ...
1365-1429 5.39e-03

type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana zinc finger CCCH domain-containing proteins AtC3H36, AtC3H52 and similar proteins; The family corresponds to a group of plant CCCH family zinc finger proteins, such as AtC3H36 and AtC3H52, which contain one K homology (KH) RNA-binding domain. They may play important roles in RNA processing as RNA-binding proteins in animals. They may also have an effective role in stress tolerance.


Pssm-ID: 411892 [Multi-domain]  Cd Length: 66  Bit Score: 37.45  E-value: 5.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462596386 1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22464      2 KISVDASLAGAIIGKGGVNSKQICRETGVKLSIRDHERDPNLKNVELEGSFEQIKEASGMVRELI 66
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
751-780 5.47e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 5.47e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462596386  751 KGFTPLILAATAGHVGVVEILLDNGADIEA 780
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
125-210 5.66e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 5.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  125 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVE--DRGIKgdiTPLMAAANGGHVK 202
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTllDKDGK---TPLELAEENGFRE 162

                   ....*...
gi 2462596386  203 IVKLLLAH 210
Cdd:PTZ00322   163 VVQLLSRH 170
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
1694-1829 5.81e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.68  E-value: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1694 NSPLDCGSASPnkvaSSSEQEAGSPPVVETTNTRPPNSSSssgsssahsNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTV 1773
Cdd:PRK14971   361 QLTQKGDDASG----GRGPKQHIKPVFTQPAAAPQPSAAA---------AASPSPSQSSAAAQPSAPQSATQPAGTPPTV 427
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386 1774 PPLATSSAPVAVPSTAPVTYPMPQTPMgcPQPTPKMETPAIRPPphgTTAPHKNSA 1829
Cdd:PRK14971   428 SVDPPAAVPVNPPSTAPQAVRPAQFKE--EKKIPVSKVSSLGPS---TLRPIQEKA 478
KH-I_PEPPER_like_rpt3 cd22461
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1363-1429 5.97e-03

third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER and flowering locus K homology domain protein (FLK). PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. The model corresponds to the KH3 domain of PEPPER and FLK.


Pssm-ID: 411889  Cd Length: 69  Bit Score: 37.53  E-value: 5.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22461      3 SQQMQIPLSYADAIIGTAGANISYIRRTSGATITIQETRGAPGEMTVEIHGTQSQVQTAQQLIQNFM 69
KH-I_PCBP4_rpt2 cd22520
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
1365-1429 5.99e-03

second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) and similar proteins; PCBP4, also called alpha-CP4, or heterogeneous nuclear ribonucleoprotein E4, or hnRNP E4, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It regulates both basal and stress-induced p21 expression through binding p21 3'-UTR and modulating p21 mRNA stability. It also plays a role in the cell cycle and is implicated in lung tumor suppression. PCBP4 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411948 [Multi-domain]  Cd Length: 72  Bit Score: 37.69  E-value: 5.99e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386 1365 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTgDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22520      5 RLVIPASQCGSLIGKAGSKIKEIRESTGAQVQVagDLLPNST-ERAVTVSGVPDAIIQCVRQICAVI 70
PHA02798 PHA02798
ankyrin-like protein; Provisional
267-425 6.02e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 6.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  267 VEVARLLLENGAGINTHSNEFKESALTLAC----YKGHLEMVRFLLEAGADQEHKTDEMHTALMeaCMdghvevarllLD 342
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdYKHMLDIVKILIENGADINKKNSDGETPLY--CL----------LS 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  343 SGAQVNMpadsfespltlaacgghvELAALLIERGASLEEVNDEGYTPLMEAAREGHE---EMVALLLGQGANINAQTEE 419
Cdd:PHA02798   119 NGYINNL------------------EILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNK 180

                   ....*.
gi 2462596386  420 TQETAL 425
Cdd:PHA02798   181 EKYDTL 186
KH-I_FUBP3_rpt3 cd22486
third type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1363-1429 6.04e-03

third type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411914  Cd Length: 70  Bit Score: 37.24  E-value: 6.04e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386 1363 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1429
Cdd:cd22486      4 SIEVSVPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGISPERVAQVMGPPDRCQHAAHIINELI 70
PHA02884 PHA02884
ankyrin repeat protein; Provisional
496-602 6.23e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.12  E-value: 6.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  496 HTDVADVLLQAGADLEHE---SEGGRT-PLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLL 571
Cdd:PHA02884    45 YTDIIDAILKLGADPEAPfplSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462596386  572 AHGADPTHRLKDGSTMlIEAAkgghtSVVCY 602
Cdd:PHA02884   125 SYGADINIQTNDMVTP-IELA-----LMICN 149
Ank_5 pfam13857
Ankyrin repeats (many copies);
940-996 6.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 6.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596386  940 LLDKG-ADVNAPPvpSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLA 996
Cdd:pfam13857    1 LLEHGpIDLNRLD--GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
322-348 6.51e-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: 36.11  E-value: 6.51e-03
                           10        20
                   ....*....|....*....|....*...
gi 2462596386  322 HTALMEAC-MDGHVEVARLLLDSGAQVN 348
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
938-1047 6.62e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 6.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386  938 RVLLDKGADVNAppVPSSRDTAL-TIAADKGHYK----FCELLIGRGAHIDVRNKKGNTPLW-LAANG--GHLDVVQLLV 1009
Cdd:PHA02798    55 KLFINLGANVNG--LDNEYSTPLcTILSNIKDYKhmldIVKILIENGADINKKNSDGETPLYcLLSNGyiNNLEILLFMI 132
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2462596386 1010 QAGADVDAADNRKITPLMAAFRKGH---VKVVRYLVK---EVNQ 1047
Cdd:PHA02798   133 ENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEkgvDINT 176
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
323-349 6.86e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 6.86e-03
                           10        20
                   ....*....|....*....|....*..
gi 2462596386  323 TALMEACMDGHVEVARLLLDSGAQVNM 349
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA03377 PHA03377
EBNA-3C; Provisional
1768-2096 7.18e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 41.58  E-value: 7.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1768 EVRMTVPPLATSSAPVAVPSTAPVTYPMPQTPMGCPQPTPKMETPAIRPPPHGTTAPHKNSASVQNSSVAVL-------- 1839
Cdd:PHA03377   444 EQAQSTPERPGPSDQPSVPVEPAHLTPVEHTTVILHQPPQSPPTVAIKPAPPPSRRRRGACVVYDDDIIEVIdvetteee 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1840 -SVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKpiAPNFSAPLPFGPFSTlfeNSPTSAHAFWGGSVVSSQSTPES 1918
Cdd:PHA03377   524 eSVTQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSDR--GPPKASPPVMAPPST---GPRVMATPSTGPRDMAPPSTGPR 598
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1919 MLSGKSSYLPNSDPLHQSDTSKAPGFRPP-----------LQRP-APSPSGIVNM----DSPyGSVTPSSTHLGNFASNI 1982
Cdd:PHA03377   599 QQAKCKDGPPASGPHEKQPPSSAPRDMAPsvvrmflrerlLEQStGPKPKSFWEMragrDGS-GIQQEPSSRRQPATQST 677
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1983 SGGQMYGPGAPLGGAPAAAN---FNRQHFSPLSLLTPCSSASN------DSSAQSVSSGVRAPSPAPSSVPLGSEKPsnv 2053
Cdd:PHA03377   678 PPRPSWLPSVFVLPSVDAGRaqpSEESHLSSMSPTQPISHEEQpryedpDDPLDLSLHPDQAPPPSHQAPYSGHEEP--- 754
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 2462596386 2054 sQDRKVPVPIGTE-RSARIRQTGTSAPSVIGSNLSTSVGHSGIW 2096
Cdd:PHA03377   755 -QAQQAPYPGYWEpRPPQAPYLGYQEPQAQGVQVSSYPGYAGPW 797
Ank_5 pfam13857
Ankyrin repeats (many copies);
307-361 7.99e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 7.99e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596386  307 LLEAG-ADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLA 361
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SCS2 COG5066
VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and ...
1712-1818 8.15e-03

VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and secretion];


Pssm-ID: 227398 [Multi-domain]  Cd Length: 242  Bit Score: 40.33  E-value: 8.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596386 1712 EQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPV 1791
Cdd:COG5066    121 SEEEISKNVHECSEDRGAAVLLVEMPTLLNILYLEVRFFVNQKEVPAEPETQPPVQVKKEEVPPVTQKTVPHENEKQTSV 200
                           90       100
                   ....*....|....*....|....*..
gi 2462596386 1792 TYPMPQTPMGCPQPTPKmETPAIRPPP 1818
Cdd:COG5066    201 STPKPQNQIKEAATVPA-ENEPSSMPI 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
240-295 8.73e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 8.73e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596386  240 LLESG-ASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINThSNEFKESALTLA 295
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
KH-I_BICC1_rpt3 cd22422
third type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
1376-1425 9.20e-03

third type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) and similar proteins; BICC1, also called Bic-C, is a mammalian homologue of Drosophila Bicaudal-C (dBic-C). BICC1 functions as an RNA-binding protein that represses the translation of selected mRNAs to control development. It regulates gene expression and modulates cell proliferation and apoptosis. BICC1 is a negative regulator of Wnt signaling. Increased levels of BICC1 may be associated with depression. Besides, BICC1 is a genetic determinant of osteoblastogenesis and bone mineral density. BICC1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411850  Cd Length: 67  Bit Score: 36.93  E-value: 9.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462596386 1376 VIGRGGCNINAIREFTGAHI---DIDKQKDKTGdrIITIRGGTESTRQATQLI 1425
Cdd:cd22422     16 MLGRNGSNIKHIMQRTGAQIhfpDPNNPPQRKS--TVFISGSIDSVYLARQQL 66
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
484-510 9.94e-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: 35.73  E-value: 9.94e-03
                           10        20
                   ....*....|....*....|....*...
gi 2462596386  484 GDTALTYACE-NGHTDVADVLLQAGADL 510
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADV 29
 
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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