NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|38683816|ref|NP_942592|]
View 

ankyrin repeat domain-containing protein 17 isoform b [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
385-666 3.68e-60

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 209.43  E-value: 3.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  385 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 464
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  465 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 544
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  545 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 621
Cdd:COG0666  164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 38683816  622 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 666
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
851-1139 5.22e-57

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.18  E-value: 5.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  851 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 930
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  931 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1010
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1011 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1090
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 38683816 1091 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1139
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-465 9.04e-57

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.41  E-value: 9.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  184 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 263
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  264 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 343
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  344 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 423
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 38683816  424 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 465
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 ...
1475-1545 1.95e-40

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: 144.13  E-value: 1.95e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683816 1475 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1545
Cdd:cd22502    1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
Ank_2 pfam12796
Ankyrin repeats (3 copies);
634-719 4.72e-15

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 4.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    634 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 713
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 38683816    714 CYLLDY 719
Cdd:pfam12796   78 KLLLEK 83
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1831-2086 1.91e-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: 60.17  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1831 PPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMT-------VPPLATSSAPVAVPSTAP 1903
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTpqssqsqVPPGPSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1904 VTYPMPQTPMGCP---QPTPK--METPAIRPPPHGTTAPHKNSASVQNSSvavlsvnHIK--RPHSVPSSVQLPSTLSTQ 1976
Cdd:pfam03154  327 TPPSQSQLQSQQPpreQPLPPapLSMPHIKPPPTTPIPQLPNPQSHKHPP-------HLSgpSPFQMNSNLPPPPALKPL 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1977 SACQNSVHPANKPiapnfsAPLPFGPFSTLFENSPTSAHAFWGGSVVSSQSTPESMLSGKSSYLPNSD-PLHQSDTSKAP 2055
Cdd:pfam03154  400 SSLSTHHPPSAHP------PPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPfPQHPFVPGGPP 473
                          250       260       270
                   ....*....|....*....|....*....|.
gi 38683816   2056 GFRPPLQRPAPSPSGIVNMDSPyGSVTPSST 2086
Cdd:pfam03154  474 PITPPSGPPTSTSSAMPGIQPP-SSASVSSS 503
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
831-859 1.17e-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: 1.17e-03
                            10        20
                    ....*....|....*....|....*....
gi 38683816     831 NHDTALTLACAGGHEELVQTLLERGASIE 859
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
385-666 3.68e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 209.43  E-value: 3.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  385 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 464
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  465 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 544
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  545 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 621
Cdd:COG0666  164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 38683816  622 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 666
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
851-1139 5.22e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.18  E-value: 5.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  851 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 930
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  931 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1010
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1011 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1090
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 38683816 1091 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1139
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-465 9.04e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.41  E-value: 9.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  184 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 263
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  264 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 343
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  344 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 423
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 38683816  424 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 465
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 ...
1475-1545 1.95e-40

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: 144.13  E-value: 1.95e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683816 1475 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1545
Cdd:cd22502    1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
846-1152 1.09e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 116.28  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   846 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVG--VVEILLDNGADIEAQsERTKDTPL-SLACSGGRQEVVELLLAR 921
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   922 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPL--MLAAMNGHTAAVKLLLDMGSDINAqI 997
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLavLLKSRNANVELLRLLIDAGADVYA-V 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   998 ETNRNTALTLAC--FQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssrdtal 1073
Cdd:PHA03095  184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA----------- 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816  1074 tiaadkghykfcelligrgahidvRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVR 1152
Cdd:PHA03095  253 ------------------------RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
240-560 1.67e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.73  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   240 EACSEGDVNAVRKLLIEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGIKGDiTPLMA-AANGGHVK 315
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   316 IVKLLLAHKADVNAQSSTGNTALtYACAGGY---VDVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLLLEN 389
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   390 GAGI-----------NTHSNEFKESAltlacykghlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 456
Cdd:PHA03095  177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   457 GAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQgaNINAQT-EETQE 535
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK--NPSAETvAATLN 324
                         330       340
                  ....*....|....*....|....*....
gi 38683816   536 TA----LTLACCGGFLEVADFLIKAGADI 560
Cdd:PHA03095  325 TAsvagGDIPSDATRLCVAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
305-395 2.57e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 2.57e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    305 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASieDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 38683816    385 LLLENGAGINT 395
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
568-659 4.23e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.26  E-value: 4.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    568 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHVCTVQ 647
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 38683816    648 FLISKGANVNRT 659
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
971-1062 5.63e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 5.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    971 LMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1050
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 38683816   1051 RVLLDKGADVNA 1062
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
250-463 1.35e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   250 VRKLLIEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVeDRGIKGDITPLMAAANG--GHVKIVKLLLA 322
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV-NAPDNNGITPLLYAISKksNSYSIVEYLLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   323 HKADVNAQSSTGNTALTYACAGGYVDV------------------VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PHA03100  130 NGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   385 LLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 456
Cdd:PHA03100  210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287

                  ....*..
gi 38683816   457 GAQVNMP 463
Cdd:PHA03100  288 GFYKNRK 294
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1476-1540 4.61e-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: 4.61e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816   1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1540
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
634-719 4.72e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 4.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    634 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 713
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 38683816    714 CYLLDY 719
Cdd:pfam12796   78 KLLLEK 83
KH smart00322
K homology RNA-binding domain;
1478-1542 3.04e-13

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 66.55  E-value: 3.04e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816    1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqKDKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIP--GPGSEERVVEITGPPENVEKAAELILEIL 68
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
565-743 1.63e-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: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  565 STPLMEAAQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 638
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  639 RAGHVCTVQFLISKGANVN--RTTAN------------NDHtVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 704
Cdd:cd22192   98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 38683816  705 AKGGHTSVVCYLLDYpnnLLSAPPPDvtQLTPPSHDLNR 743
Cdd:cd22192  177 VLQPNKTFACQMYDL---ILSYDKED--DLQPLDLVPNN 210
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
894-1123 2.10e-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: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  894 QSERTKDTPLSLACSGGRQEVVELLL--------ARGANKEhrnvsdyTPLSLAASGGYVNIIKILLNAGAE-INSRTGS 964
Cdd:cd22192   12 QQKRISESPLLLAAKENDVQAIKKLLkcpscdlfQRGALGE-------TALHVAALYDNLEAAVVLMEAAPElVNEPMTS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  965 KL--GISPLMLAAMNGHTAAVKLLLDMGSDINaqieTNRNTALtlaCFqgrtevvsllLDRKANV----EHraktgltPL 1038
Cdd:cd22192   85 DLyqGETALHIAVVNQNLNLVRELIARGADVV----SPRATGT---FF----------RPGPKNLiyygEH-------PL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1039 MEAASGGYAEVGRVLLDKGADVNAppvpssRD----TALTIAADKGHYKF-CE---LLIGRGAHID------VRNKKGNT 1104
Cdd:cd22192  141 SFAACVGNEEIVRLLIEHGADIRA------QDslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLT 214
                        250
                 ....*....|....*....
gi 38683816 1105 PLWLAANGGHLDVVQLLVQ 1123
Cdd:cd22192  215 PFKLAAKEGNIVMFQHLVQ 233
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1831-2086 1.91e-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: 60.17  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1831 PPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMT-------VPPLATSSAPVAVPSTAP 1903
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTpqssqsqVPPGPSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1904 VTYPMPQTPMGCP---QPTPK--METPAIRPPPHGTTAPHKNSASVQNSSvavlsvnHIK--RPHSVPSSVQLPSTLSTQ 1976
Cdd:pfam03154  327 TPPSQSQLQSQQPpreQPLPPapLSMPHIKPPPTTPIPQLPNPQSHKHPP-------HLSgpSPFQMNSNLPPPPALKPL 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1977 SACQNSVHPANKPiapnfsAPLPFGPFSTLFENSPTSAHAFWGGSVVSSQSTPESMLSGKSSYLPNSD-PLHQSDTSKAP 2055
Cdd:pfam03154  400 SSLSTHHPPSAHP------PPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPfPQHPFVPGGPP 473
                          250       260       270
                   ....*....|....*....|....*....|.
gi 38683816   2056 GFRPPLQRPAPSPSGIVNMDSPyGSVTPSST 2086
Cdd:pfam03154  474 PITPPSGPPTSTSSAMPGIQPP-SSASVSSS 503
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
238-421 2.47e-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: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  238 LAEACSEGDVNAVRKLLiEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDI----TPLMAAANG 311
Cdd:cd22192   21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLyqgeTALHIAVVN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  312 GHVKIVKLLLAHKADVNAQSST--------------GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL----ME 373
Cdd:cd22192  100 QNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvLQ 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 38683816  374 AGSAGHVEVARLLLENGAGINTHS-----NEFKESALTLACYKGHLEMVRFLL 421
Cdd:cd22192  180 PNKTFACQMYDLILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
818-1054 9.66e-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: 9.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    818 IYPAIDIDaqtESNHDTALTLACAGGHEELVQTLLERGAS--IEHRDKKGFTPLILAATAG-HVGVVEILLDNGADIEaq 894
Cdd:TIGR00870    6 IVPAEESP---LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    895 serTKDTPLsLACSGGRQEVVELLLA-------RGANKEHRNVS-------DYTPLSLAASGGYVNIIKILLNAGAEINS 960
Cdd:TIGR00870   81 ---VGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    961 R------------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIE---------------TNRNTALTLACFQgr 1013
Cdd:TIGR00870  157 RacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSlgntllhllvmenefKAEYEELSCQMYN-- 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 38683816   1014 tEVVSLL--LDRKANVEH-RAKTGLTPLMEAASGGYAEVGRVLL 1054
Cdd:TIGR00870  235 -FALSLLdkLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
634-738 2.00e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   634 LMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVV 713
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90       100
                  ....*....|....*....|....*...
gi 38683816   714 CYLLDYPNNLLSA---PPPDVTQLTPPS 738
Cdd:PTZ00322  165 QLLSRHSQCHFELganAKPDSFTGKPPS 192
PHA03247 PHA03247
large tegument protein UL36; Provisional
1774-2206 2.79e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1774 TNATYPMPTAKEHYPVSSPSSPSPPAQPGGVSRNSPLDcGSASPNKVASSSeqeaGSPPVVETTNTRPPNSSSSSGSSSA 1853
Cdd:PHA03247 2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRL----GRAAQASSPPQRPRRRAARPTVGSL 2695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1854 HSNQQQPPGSVSQEPRPPLQQSQVPPPEV----RMTVPPLATSSAPVAVPST-----APVTYPMPQTPMGCPQPTPKMET 1924
Cdd:PHA03247 2696 TSLADPPPPPPTPEPAPHALVSATPLPPGpaaaRQASPALPAAPAPPAVPAGpatpgGPARPARPPTTAGPPAPAPPAAP 2775
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1925 PAirPPPHGTTAPHKNSASVQNSSVAVLSvnhikRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIAPNfSAPLPFGPFS 2004
Cdd:PHA03247 2776 AA--GPPRRLTRPAVASLSESRESLPSPW-----DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT-APPPPPGPPP 2847
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  2005 TlfensPTSAhafwGGSVVssqstPESMLSGKSsylpnsdPLHQSDTSKAPGFRPP---LQRPAPSPSGIVNMDSPYGSV 2081
Cdd:PHA03247 2848 P-----SLPL----GGSVA-----PGGDVRRRP-------PSRSPAAKPAAPARPPvrrLARPAVSRSTESFALPPDQPE 2906
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  2082 TPssthlgnfasnisggqmygpgaplggapaaanfnRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSP-APSSVPLGS 2160
Cdd:PHA03247 2907 RP----------------------------------PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPlAPTTDPAGA 2952
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 38683816  2161 EKPSNVSQDRKVPVPIGTERSARIRQTGTSAPSVIGSNLSTSVGHS 2206
Cdd:PHA03247 2953 GEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTG 2998
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1101-1130 1.09e-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: 1.09e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 38683816    1101 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1130
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
499-528 1.14e-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: 1.14e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 38683816     499 EGYTPLMEAAREGHEEMVALLLGQGANINA 528
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
236-489 2.80e-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: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    236 RSLAEACSEGDVNAVRKLLIEGRSVNEHTEE--GESLLCLACSAG-YYELAQVLLamhaNVEDRGIKGDiTPLMAAANGg 312
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLL----NLSCRGAVGD-TLLHAISLE- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    313 HVKIVKLLLAHKADvnAQSSTGNTALTYACAGG--YVDvvkvllesgasiedhnengHTPLMEAGSAGHVEVARLLLENG 390
Cdd:TIGR00870   93 YVDAVEAILLHLLA--AFRKSGPLELANDQYTSefTPG-------------------ITALHLAAHRQNYEIVKLLLERG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    391 AGINT--HSNEFKESALT---------LACYK--GHLEMVRFLLEAGADQEhKTDEM-----HTALMEA----------- 441
Cdd:TIGR00870  152 ASVPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelsc 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 38683816    442 -CMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 489
Cdd:TIGR00870  231 qMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
341-494 4.86e-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: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    341 ACAGGYVDVVKVLLESGAS--IEDHNENGHTPLMEAGSAG-HVEVARLLLENGAGINThsnefKESALTLAC--YKGHLE 415
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV-----GDTLLHAISleYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    416 MVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ESP 470
Cdd:TIGR00870   99 AILLHLLAAFRKsgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgESP 178
                          170       180
                   ....*....|....*....|....
gi 38683816    471 LTLAACGGHVELAALLIERGASLE 494
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADIL 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
334-362 1.82e-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: 1.82e-04
                            10        20
                    ....*....|....*....|....*....
gi 38683816     334 GNTALTYACAGGYVDVVKVLLESGASIED 362
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
1475-1551 3.07e-04

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 46.15  E-value: 3.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816 1475 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqkDktgDRIITIrGGT--ESTRQATQLINALIKDPdkEIDE 1551
Cdd:COG1185  549 RIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIE---D---DGTVKI-AATdgEAAEKAIERIEGITAEP--EVGE 618
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
1475-1551 4.09e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.81  E-value: 4.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816  1475 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDPdkEIDE 1551
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 ...
831-859 1.17e-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: 1.17e-03
                            10        20
                    ....*....|....*....|....*....
gi 38683816     831 NHDTALTLACAGGHEELVQTLLERGASIE 859
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
831-863 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 38683816    831 NHDTALTLACA-GGHEELVQTLLERGASIEHRDK 863
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
SCS2 COG5066
VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and ...
1825-1931 9.05e-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: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1825 EQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPV 1904
Cdd:COG5066  121 SEEEISKNVHECSEDRGAAVLLVEMPTLLNILYLEVRFFVNQKEVPAEPETQPPVQVKKEEVPPVTQKTVPHENEKQTSV 200
                         90       100
                 ....*....|....*....|....*..
gi 38683816 1905 TYPMPQTPMGCPQPTPKmETPAIRPPP 1931
Cdd:COG5066  201 STPKPQNQIKEAATVPA-ENEPSSMPI 226
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
385-666 3.68e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 209.43  E-value: 3.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  385 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 464
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  465 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 544
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  545 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 621
Cdd:COG0666  164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 38683816  622 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 666
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
414-723 9.92e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 207.88  E-value: 9.92e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  414 LEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASL 493
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  494 EEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQetaltlaccggflevadflikagadielgcsTPLMEAAQ 573
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-------------------------------TPLHLAAY 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  574 EGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKG 653
Cdd:COG0666  130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  654 ANVNRTTaNNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPNNL 723
Cdd:COG0666  210 ADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
851-1139 5.22e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.18  E-value: 5.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  851 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 930
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  931 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1010
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1011 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1090
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 38683816 1091 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1139
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-465 9.04e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.41  E-value: 9.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  184 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 263
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  264 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 343
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  344 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 423
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 38683816  424 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 465
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
347-634 1.11e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.41  E-value: 1.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  347 VDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFkESALTLACYKGHLEMVRFLLEAGAD 426
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALG-ALLLLAAALAGDLLVALLLLAAGAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  427 QEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLME 506
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  507 AAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYL 583
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNdgkTALDLAAENGNLEIVKLL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 38683816  584 LAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPL 634
Cdd:COG0666  239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
314-601 8.93e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 196.71  E-value: 8.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  314 VKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGI 393
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  394 NThSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 473
Cdd:COG0666   81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  474 AACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFL 553
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 38683816  554 IKAGADIELGC---STPLMEAAQEGHLELVKYLLAAGANVHATTATGDTAL 601
Cdd:COG0666  239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
814-1062 9.70e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 193.63  E-value: 9.70e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  814 AMLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEA 893
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  894 QSERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLML 973
Cdd:COG0666  116 RDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR--DNDGETPLHL 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  974 AAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVL 1053
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271

                 ....*....
gi 38683816 1054 LDKGADVNA 1062
Cdd:COG0666  272 LLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
815-1106 4.31e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 191.71  E-value: 4.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  815 MLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQ 894
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  895 SERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLA 974
Cdd:COG0666   84 DDG-GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  975 AMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1054
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 38683816 1055 DKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPL 1106
Cdd:COG0666  240 EAGADLNAK--DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-438 9.97e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 176.30  E-value: 9.97e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  153 LLLSGTADGADLRTVDPETQARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQ 232
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  233 SDNRSLAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGG 312
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  313 HVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAG 392
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 38683816  393 INtHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTAL 438
Cdd:COG0666  245 LN-AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
947-1156 7.24e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.13  E-value: 7.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  947 IIKILLNAGAEINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKAN 1026
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADA-LGALLLLAAALAGDLLVALLLLAAGAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1027 VEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPL 1106
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA--RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 38683816 1107 WLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVK 1156
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
546-959 2.45e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 2.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  546 FLEVADFLIKAGADIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEH 625
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  626 ESEGGRTPLMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGstmlieaa 705
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG-------- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  706 kgghtsvvcylldypnnllsapppdvtqltppshdlnraprvpvqalpmvvppqepdkppanvattlpirnkavsgrasa 785
Cdd:COG0666      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  786 msntpthsiaasisqpqtptpspiispsamlpiypaididaqtesnhDTALTLACAGGHEELVQTLLERGASIEHRDKKG 865
Cdd:COG0666  154 -----------------------------------------------NTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  866 FTPLILAATAGHVGVVEILLDNGADIEAQSERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYV 945
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
                        410
                 ....*....|....
gi 38683816  946 NIIKILLNAGAEIN 959
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 ...
1475-1545 1.95e-40

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: 144.13  E-value: 1.95e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683816 1475 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1545
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 ...
1475-1556 1.83e-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: 136.03  E-value: 1.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1475 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDKEIDELIP 1554
Cdd:cd22503    1 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIP 80

                 ..
gi 38683816 1555 KN 1556
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 ...
1475-1545 5.09e-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: 134.26  E-value: 5.09e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683816 1475 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1545
Cdd:cd22404    1 KSKKVTVPNSAISRVIGRGGCNINAIREVSGAHIEIDKQKGEQGDRRITIKGSADATRQAAQLINALIKDP 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
846-1152 1.09e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 116.28  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   846 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVG--VVEILLDNGADIEAQsERTKDTPL-SLACSGGRQEVVELLLAR 921
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   922 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPL--MLAAMNGHTAAVKLLLDMGSDINAqI 997
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLavLLKSRNANVELLRLLIDAGADVYA-V 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   998 ETNRNTALTLAC--FQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssrdtal 1073
Cdd:PHA03095  184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA----------- 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816  1074 tiaadkghykfcelligrgahidvRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVR 1152
Cdd:PHA03095  253 ------------------------RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
901-1187 2.99e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.38  E-value: 2.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   901 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYV-----NIIKILLNAGAEINSrtGSKLGISPLMLAA 975
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA--PDNNGITPLLYAI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   976 MN--GHTAAVKLLLDMGSDINAqietnrntaltlacfqgrtevvsllldrkanvehRAKTGLTPLMEAASGGYA--EVGR 1051
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNI----------------------------------KNSDGENLLHLYLESNKIdlKILK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1052 VLLDKGADVNAppvpssrdtaltiaADKghykfCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAA 1131
Cdd:PHA03100  161 LLIDKGVDINA--------------KNR-----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683816  1132 DNRKITPLMAAFRKGHVKVVRYLvkeVNQFPSDS---ECMRY-----IATITDKEMLKKCHLCM 1187
Cdd:PHA03100  222 NKYGDTPLHIAILNNNKEIFKLL---LNNGPSIKtiiETLLYfkdkdLNTITKIKMLKKSIMYM 282
PHA03095 PHA03095
ankyrin-like protein; Provisional
240-560 1.67e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.73  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   240 EACSEGDVNAVRKLLIEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGIKGDiTPLMA-AANGGHVK 315
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   316 IVKLLLAHKADVNAQSSTGNTALtYACAGGY---VDVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLLLEN 389
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   390 GAGI-----------NTHSNEFKESAltlacykghlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 456
Cdd:PHA03095  177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   457 GAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQgaNINAQT-EETQE 535
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK--NPSAETvAATLN 324
                         330       340
                  ....*....|....*....|....*....
gi 38683816   536 TA----LTLACCGGFLEVADFLIKAGADI 560
Cdd:PHA03095  325 TAsvagGDIPSDATRLCVAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
305-395 2.57e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 2.57e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    305 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASieDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 38683816    385 LLLENGAGINT 395
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
568-659 4.23e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.26  E-value: 4.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    568 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHVCTVQ 647
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 38683816    648 FLISKGANVNRT 659
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
447-625 6.46e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 107.06  E-value: 6.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   447 VEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-----ELAALLIERGASLEEVNDEGYTPLMEAARE--GHEEMVALL 519
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   520 LGQGANINAQTEeTQETALTLA--CCGGFLEVADFLIKAGADI----------ELGC---------STPLMEAAQEGHLE 578
Cdd:PHA03100  128 LDNGANVNIKNS-DGENLLHLYleSNKIDLKILKLLIDKGVDInaknrvnyllSYGVpinikdvygFTPLHYAVYNNNPE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 38683816   579 LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEH 625
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
438-529 5.36e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 5.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    438 LMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASleEVNDEGYTPLMEAAREGHEEMVA 517
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 38683816    518 LLLGQGANINAQ 529
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
971-1062 5.63e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 5.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    971 LMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1050
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 38683816   1051 RVLLDKGADVNA 1062
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
396-704 7.22e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 101.64  E-value: 7.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   396 HSNEFKESAL---TLACYKGHLEMVRFLLEAGADQEHK----TDEMHTALMEACMDGhVEVARLLLDSGAQVNMPADSFE 468
Cdd:PHA03095    6 SVDIIMEAALydyLLNASNVTVEEVRRLLAAGADVNFRgeygKTPLHLYLHYSSEKV-KDIVRLLLEAGADVNAPERCGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   469 SPLTLAACGGHVE-LAALLIERGASLEEVNDEGYTPLMEAAR--EGHEEMVALLLGQGANINAqTEETQETALtlaccgg 545
Cdd:PHA03095   85 TPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNA-LDLYGMTPL------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   546 flevADFLIKAGADIELgcstplmeaaqeghlelVKYLLAAGANVHATTATGDTALTYACENGHTDVADV--LLQAGADL 623
Cdd:PHA03095  157 ----AVLLKSRNANVEL-----------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDP 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   624 EHESEGGRTPLMKAArAGHVCT---VQFLISKGANVNRTTaNNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTM 700
Cdd:PHA03095  216 AATDMLGNTPLHSMA-TGSSCKrslVLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                  ....
gi 38683816   701 LIEA 704
Cdd:PHA03095  294 LSLM 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
238-623 1.12e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 102.83  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   238 LAEACSEGDV--NAVRKLLIEGRSVNEHTEEGESLLclacsagyyelAQVLLAMHANVEDRGIKGdITPLMAAANGGHVK 315
Cdd:PHA02876  125 LKEAISGNDIhyDKINESIEYMKLIKERIQQDELLI-----------AEMLLEGGADVNAKDIYC-ITPIHYAAERGNAK 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   316 IVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIedhNENGHTpLMEAGSAGHVEVARLLLENGAGINT 395
Cdd:PHA02876  193 MVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI---NKNDLS-LLKAIRNEDLETSLLLYDAGFSVNS 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   396 hSNEFKESALTLACYKGHL-EMVRFLLEAGADQEHKTDEMHTALMEACMDGH-VEVARLLLDSGAQVNMPADSFESPLTL 473
Cdd:PHA02876  269 -IDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQ 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   474 AAC-GGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQeTALTLACCGG--FLEVA 550
Cdd:PHA02876  348 ASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTnpYMSVK 426
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816   551 DfLIKAGADIELG---CSTPLMEAAQEG-HLELVKYLLAAGANVHATTATGDTALTYACenGHTDVADVLLQAGADL 623
Cdd:PHA02876  427 T-LIDRGANVNSKnkdLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
338-430 4.30e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 4.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    338 LTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENgagINTHSNEFKESALTLACYKGHLEMV 417
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 38683816    418 RFLLEAGADQEHK 430
Cdd:pfam12796   78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
371-461 7.34e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 7.34e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    371 LMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEaGADQEHKTDEMhTALMEACMDGHVEVA 450
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIV 77
                           90
                   ....*....|.
gi 38683816    451 RLLLDSGAQVN 461
Cdd:pfam12796   78 KLLLEKGADIN 88
PHA03100 PHA03100
ankyrin repeat protein; Provisional
289-528 1.00e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   289 MHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYV-----DVVKVLLESGASIEDH 363
Cdd:PHA03100   23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   364 NENGHTPLMEAGSA--GHVEVARLLLENGAGINTHSNEFKES-ALTLACYKGHLEMVRFLLEAGADQEHKTDemhtalme 440
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLlHLYLESNKIDLKILKLLIDKGVDINAKNR-------- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   441 acmdghVEvarLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLL 520
Cdd:PHA03100  175 ------VN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245

                  ....*...
gi 38683816   521 GQGANINA 528
Cdd:PHA03100  246 NNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
847-1143 1.38e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 98.98  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   847 LVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIE------------AQSERTKDT------------- 901
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvlecAVDSKNIDTikaiidnrsnink 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   902 -PLSL--ACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVN-IIKILLNAGAEINSRTGSklGISPLMLAAMN 977
Cdd:PHA02876  240 nDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK--GETPLYLMAKN 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   978 GH-TAAVKLLLDMGSDINAQiETNRNTALTLACFQGR-TEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLD 1055
Cdd:PHA02876  318 GYdTENIRTLIMLGADVNAA-DRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1056 KGADVNAppVPSSRDTALTIA-ADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAA-NGGHLDVVQLLVQAGADVDAADN 1133
Cdd:PHA02876  397 YGADIEA--LSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINI 474
                         330
                  ....*....|
gi 38683816  1134 RKITPLMAAF 1143
Cdd:PHA02876  475 QNQYPLLIAL 484
Ank_2 pfam12796
Ankyrin repeats (3 copies);
936-1030 2.29e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 2.29e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    936 LSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHTAAVKLLLDMgsdINAQIETNRNTALTLACFQGRTE 1015
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*
gi 38683816   1016 VVSLLLDRKANVEHR 1030
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
845-1029 2.62e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 2.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   845 EELVQTLLERGASIEHRDKKGFTPLILAATAGHV-----GVVEILLDNGADIEAQSERTkDTPLSLACSGGRQ--EVVEL 917
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG-ITPLLYAISKKSNsySIVEY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   918 LLARGANKEHRNVSDYTPLSLAASGGYV--NIIKILLNAGAEINSRT--------GSKL------GISPLMLAAMNGHTA 981
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNrvnyllsyGVPInikdvyGFTPLHYAVYNNNPE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 38683816   982 AVKLLLDMGSDINAqIETNRNTALTLACFQGRTEVVSLLLDRKANVEH 1029
Cdd:PHA03100  207 FVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
504-593 5.88e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 5.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    504 LMEAAREGHEEMVALLLGQGANINAQTEETQeTALTLACCGGFLEVADFLI-KAGADIELGCSTPLMEAAQEGHLELVKY 582
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLLeHADVNLKDNGRTALHYAARSGHLEIVKL 79
                           90
                   ....*....|.
gi 38683816    583 LLAAGANVHAT 593
Cdd:pfam12796   80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
601-693 6.74e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 6.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    601 LTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKgANVNRTtaNNDHTVLSLACAGGHLAVV 680
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK--DNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 38683816    681 ELLLAHGADPTHR 693
Cdd:pfam12796   78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
903-996 1.59e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.59e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    903 LSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNaGAEINSRTGsklGISPLMLAAMNGHTAA 982
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN---GRTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 38683816    983 VKLLLDMGSDINAQ 996
Cdd:pfam12796   77 VKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
846-999 1.63e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.96  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   846 ELVQTLLERGASIEHRDKKGFTPLILAATA--GHVGVVEILLDNGADIEAQSERTKdTPLSLACSGGRQ--EVVELLLAR 921
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKIdlKILKLLIDK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   922 GA--NKEHR--------------NVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHTAAVKL 985
Cdd:PHA03100  166 GVdiNAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN--KYGDTPLHIAILNNNKEIFKL 243
                         170
                  ....*....|....
gi 38683816   986 LLDMGSDINAQIET 999
Cdd:PHA03100  244 LLNNGPSIKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
312-634 1.79e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.87  E-value: 1.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   312 GHVKIVKLLLAHKAD-VNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENG 390
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   391 agINThsnefkeSALTLACYKGhlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 470
Cdd:PHA02874   92 --VDT-------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   471 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQteetqetaltlaCCGGFleva 550
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK------------CKNGF---- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   551 dflikagadielgcsTPLMEAAQegHLELVKYLLAAGANVHATTATGDTALTYA----CEnghTDVADVLLQAGADLEHE 626
Cdd:PHA02874  225 ---------------TPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADISIK 284

                  ....*...
gi 38683816   627 SEGGRTPL 634
Cdd:PHA02874  285 DNKGENPI 292
Ank_2 pfam12796
Ankyrin repeats (3 copies);
836-929 1.93e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.93e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    836 LTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNgADIEAQSErtKDTPLSLACSGGRQEVV 915
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 38683816    916 ELLLARGANKEHRN 929
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
346-652 2.06e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   346 YVDVVKVLLESGASIEDHNENGHTPL---MEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLE 422
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   423 AGADQEHKTDEMHTALmEACMDG---HVEVARLLLDSGAQVNmpaDSFESPLTLAAC-----GGHVELAALLIERGASLE 494
Cdd:PHA03095  106 AGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVN---ALDLYGMTPLAVllksrNANVELLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   495 EVNDEGYTPLmeaaregheemvalllgqgaNINAQTEETQETaltlaccggfleVADFLIKAGAD---IELGCSTPLMEA 571
Cdd:PHA03095  182 AVDDRFRSLL--------------------HHHLQSFKPRAR------------IVRELIRAGCDpaaTDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   572 AQEGHLE--LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFL 649
Cdd:PHA03095  230 ATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309

                  ...
gi 38683816   650 ISK 652
Cdd:PHA03095  310 LAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
471-562 5.10e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 5.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    471 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLgQGANINAQTEetQETALTLACCGGFLEVA 550
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN--GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 38683816    551 DFLIKAGADIEL 562
Cdd:pfam12796   78 KLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1073-1156 9.80e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 9.80e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1073 LTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQaGADVDAADNRKiTPLMAAFRKGHVKVVR 1152
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVK 78

                   ....
gi 38683816   1153 YLVK 1156
Cdd:pfam12796   79 LLLE 82
PHA02876 PHA02876
ankyrin repeat protein; Provisional
349-719 1.04e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 93.20  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   349 VVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEfKESALTLACYKGHLEMVRFLLeagaDQE 428
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAII----DNR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   429 HKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-ELAALLIERGASLEEVNDEGYTPLMEA 507
Cdd:PHA02876  235 SNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLM 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   508 AREGHE-EMVALLLGQGANINAqteetqetaltlaccggflevADFLIkagadielgcSTPLMEAAQ-EGHLELVKYLLA 585
Cdd:PHA02876  315 AKNGYDtENIRTLIMLGADVNA---------------------ADRLY----------ITPLHQASTlDRNKDIVITLLE 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   586 AGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGH-VCTVQFLISKGANVNrtTANND 664
Cdd:PHA02876  364 LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVN--SKNKD 441
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816   665 -HTVLSLACAGG-HLAVVELLLAHGADPTH-RLKDGSTMLIEAakgGHTSVVCYLLDY 719
Cdd:PHA02876  442 lSTPLHYACKKNcKLDVIEMLLDNGADVNAiNIQNQYPLLIAL---EYHGIVNILLHY 496
PHA03100 PHA03100
ankyrin repeat protein; Provisional
250-463 1.35e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   250 VRKLLIEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVeDRGIKGDITPLMAAANG--GHVKIVKLLLA 322
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV-NAPDNNGITPLLYAISKksNSYSIVEYLLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   323 HKADVNAQSSTGNTALTYACAGGYVDV------------------VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PHA03100  130 NGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   385 LLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 456
Cdd:PHA03100  210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287

                  ....*..
gi 38683816   457 GAQVNMP 463
Cdd:PHA03100  288 GFYKNRK 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
553-906 1.51e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   553 LIKAGADI----ELGCsTPL---MEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHT-DVADVLLQAGADLE 624
Cdd:PHA03095   33 LLAAGADVnfrgEYGK-TPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   625 HESEGGRTPLmkaaragHVC---------TVQFLISKGANVNrttANNDHTVLSLAC----AGGHLAVVELLLAHGADPT 691
Cdd:PHA03095  112 AKDKVGRTPL-------HVYlsgfninpkVIRLLLRKGADVN---ALDLYGMTPLAVllksRNANVELLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   692 HRLKDGSTMLieaakggHtsvvcYLLDYPnnllsapppdvtqltppshdlnraprvpvqalpmvvppqepdKPPANVATT 771
Cdd:PHA03095  182 AVDDRFRSLL-------H-----HHLQSF------------------------------------------KPRARIVRE 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   772 LPIRNKAVSGRaSAMSNTPTHSIAASISqpqtptpspiispsamlpiypaididaqtesnhdtaltlaCAGGheeLVQTL 851
Cdd:PHA03095  208 LIRAGCDPAAT-DMLGNTPLHSMATGSS----------------------------------------CKRS---LVLPL 243
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 38683816   852 LERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSErTKDTPLSLA 906
Cdd:PHA03095  244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1038-1132 2.09e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 2.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1038 LMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIgrgAHIDVRNK-KGNTPLWLAANGGHLD 1116
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANL--QDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKdNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 38683816   1117 VVQLLVQAGADVDAAD 1132
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-371 3.12e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 3.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  152 KLLLsgtADGADLRTVDPETQArleALLEAAGIGklstadgkafaDPEVLRRLtssvscaLDEAAAALTRMRAESTAnag 231
Cdd:COG0666  104 KLLL---EAGADVNARDKDGET---PLHLAAYNG-----------NLEIVKLL-------LEAGADVNAQDNDGNTP--- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  232 qsdnrsLAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANG 311
Cdd:COG0666  157 ------LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAEN 229
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  312 GHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL 371
Cdd:COG0666  230 GNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
822-1065 5.16e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.70  E-value: 5.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   822 IDIDAqTESNHDTAL-TLACAGGHEELVQTLLERGASIEHRDKKGFTPL--ILAATAGHVGVVEILLDNGADIEAQSERT 898
Cdd:PHA03095   74 ADVNA-PERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   899 KdTPLS--------------LACSGG-----------------------RQEVVELLLARGANKEHRNVSDYTPLSLAAS 941
Cdd:PHA03095  153 M-TPLAvllksrnanvellrLLIDAGadvyavddrfrsllhhhlqsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMAT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   942 GGYVNIIKI--LLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrNTALTLACFQGRTEVVSL 1019
Cdd:PHA03095  232 GSSCKRSLVlpLLIAGISINAR--NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG-NTPLSLMVRNNNGRAVRA 308
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 38683816  1020 LLDRKANVEHRAKTgLTPLMEAASGGYAEVGR-----VLLDKGADVNAPPV 1065
Cdd:PHA03095  309 ALAKNPSAETVAAT-LNTASVAGGDIPSDATRlcvakVVLRGAFSLLPEPI 358
PHA02874 PHA02874
ankyrin repeat protein; Provisional
875-1204 1.75e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 87.71  E-value: 1.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   875 AGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNA 954
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   955 GAEinsrtgsklgISPLMLAAMNGHTaaVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTG 1034
Cdd:PHA02874   91 GVD----------TSILPIPCIEKDM--IKTILDCGIDVNIK-DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1035 LTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLA----- 1109
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVK--DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiihnr 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1110 ----------------ANGG-----------HLDVVQLLVQAGADVDAADNRKITPLMAAFRK-GHVKVVR------YLV 1155
Cdd:PHA02874  236 saiellinnasindqdIDGStplhhainppcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKdiianaVLI 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 38683816  1156 KEVNQFPsDSECMRYIATITDKEMLKKCHLCMESIVQAKdRQAAEANKN 1204
Cdd:PHA02874  316 KEADKLK-DSDFLEHIEIKDNKEFSDFIKECNEEIEDMK-KTKCGCDKN 362
PHA03095 PHA03095
ankyrin-like protein; Provisional
514-727 2.01e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.77  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   514 EMVALLLGQGANINaQTEETQETALT--LAC-CGGFLEVADFLIKAGADIEL----GCsTPL---MEAAQEghLELVKYL 583
Cdd:PHA03095   28 EEVRRLLAAGADVN-FRGEYGKTPLHlyLHYsSEKVKDIVRLLLEAGADVNApercGF-TPLhlyLYNATT--LDVIKLL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   584 LAAGANVHATTATGDTAL-TYAC-ENGHTDVADVLLQAGADLEHESEGGRTPL---MKAARAgHVCTVQFLISKGANVnR 658
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhVYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDAGADV-Y 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   659 TTANNDHTVLSLacaggHL-------AVVELLLAHGADPTHRLKDGSTMLIEAAKGG--HTSVVCYLL------DYPNNL 723
Cdd:PHA03095  182 AVDDRFRSLLHH-----HLqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLiagisiNARNRY 256

                  ....
gi 38683816   724 LSAP 727
Cdd:PHA03095  257 GQTP 260
PHA02875 PHA02875
ankyrin repeat protein; Provisional
834-1026 2.01e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.35  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   834 TALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQE 913
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   914 VVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGskLGISPLMLAAMNGHTAAVKLLLDMGSDI 993
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC--CGCTPLIIAMAKGDIAICKMLLDSGANI 194
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 38683816   994 NAqieTNRNTALTLACF---QGRTEVVSLLLDRKAN 1026
Cdd:PHA02875  195 DY---FGKNGCVAALCYaieNNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
238-330 2.16e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 2.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGikgdITPLMAAANGGHVKI 316
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNG----RTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 38683816    317 VKLLLAHKADVNAQ 330
Cdd:pfam12796   77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1005-1099 2.81e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 2.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1005 LTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKgADVNappVPSSRDTALTIAADKGHYKF 1084
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN---LKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 38683816   1085 CELLIGRGAHIDVRN 1099
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1476-1540 4.61e-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: 4.61e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816   1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1540
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
PHA02876 PHA02876
ankyrin repeat protein; Provisional
612-993 1.35e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 86.27  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   612 VADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANnDHTVLSLACAGGHLAVVELLLahgaDPT 691
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAII----DNR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   692 HRLKDGSTMLIEAAKGG--HTSVVCYLLDYPNNLLsapppDVTQLTPpshdLNRAPRVPvqALPMVVPP---QEPDKPPA 766
Cdd:PHA02876  235 SNINKNDLSLLKAIRNEdlETSLLLYDAGFSVNSI-----DDCKNTP----LHHASQAP--SLSRLVPKlleRGADVNAK 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   767 NVATTLPIRNKAVSGrasamsnTPTHSIAASISQpqtptpspiispsamlpiypAIDIDAqTESNHDTALTLACA-GGHE 845
Cdd:PHA02876  304 NIKGETPLYLMAKNG-------YDTENIRTLIML--------------------GADVNA-ADRLYITPLHQASTlDRNK 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   846 ELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTkDTPLSLACSGGRQEV-VELLLARGAN 924
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKI-GTALHFALCGTNPYMsVKTLIDRGAN 434
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816   925 KEHRNVSDYTPLSLAASGG-YVNIIKILLNAGAEINSrtgskLGIS---PLMLAAmnGHTAAVKLLLDMGSDI 993
Cdd:PHA02876  435 VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA-----INIQnqyPLLIAL--EYHGIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
1015-1156 6.89e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 6.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1015 EVVSLLLDRKANVEHR---AKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALtiaadkgHYKFC------ 1085
Cdd:PHA03095   28 EEVRRLLAAGADVNFRgeyGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAP--ERCGFTPL-------HLYLYnattld 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816  1086 --ELLIGRGAHIDVRNKKGNTPL--WLAANGGHLDVVQLLVQAGADVDAADNRKITPLmAAFRKGH---VKVVRYLVK 1156
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 ...
1477-1539 7.58e-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: 7.58e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816 1477 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLIN 1539
Cdd:cd00105    1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGERVVTITGTPEAVEKAKELIE 63
PHA02876 PHA02876
ankyrin repeat protein; Provisional
570-1060 7.93e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.96  E-value: 7.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   570 EAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFL 649
Cdd:PHA02876  151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   650 ISKGANVNRttanNDhtvLSLacagghlavvelllahgadpthrLKDGSTMLIEaakgghTSVVCYLLDYPNNLLsappp 729
Cdd:PHA02876  231 IDNRSNINK----ND---LSL-----------------------LKAIRNEDLE------TSLLLYDAGFSVNSI----- 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   730 DVTQltppshdlnraprvpvqalpmvvppqepdkppanvattlpirnkavsgrasamsNTPTHSIAasisqpQTPTPSpi 809
Cdd:PHA02876  270 DDCK------------------------------------------------------NTPLHHAS------QAPSLS-- 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   810 ispsamlpiypaididaqtesnhdtaltlacaggheELVQTLLERGASIEHRDKKGFTPLILAATAGH-VGVVEILLDNG 888
Cdd:PHA02876  288 ------------------------------------RLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLG 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   889 ADIEAqSERTKDTPLSLACSGGR-QEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgSKLG 967
Cdd:PHA02876  332 ADVNA-ADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS-QKIG 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   968 IS-PLMLAAMNGHTaAVKLLLDMGSDINAQiETNRNTALTLACFQG-RTEVVSLLLDRKANVEHRAKTGLTPLMEAAsgG 1045
Cdd:PHA02876  410 TAlHFALCGTNPYM-SVKTLIDRGANVNSK-NKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--E 485
                         490
                  ....*....|....*
gi 38683816  1046 YAEVGRVLLDKGADV 1060
Cdd:PHA02876  486 YHGIVNILLHYGAEL 500
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
305-473 1.10e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 83.38  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   305 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   385 LLLENGAGINTHSNefkESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVN-MP 463
Cdd:PLN03192  609 ILYHFASISDPHAA---GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkAN 685
                         170
                  ....*....|
gi 38683816   464 ADSFESPLTL 473
Cdd:PLN03192  686 TDDDFSPTEL 695
PHA02875 PHA02875
ankyrin repeat protein; Provisional
337-559 4.16e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 4.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   337 ALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFkESALTLACYKGHLEM 416
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   417 VRFLLEAG--ADQEHKTDEMhTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLE 494
Cdd:PHA02875   84 VEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816   495 EVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTLACCGGFLEVADFLIKAGAD 559
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
634-719 4.72e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 4.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    634 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 713
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 38683816    714 CYLLDY 719
Cdd:pfam12796   78 KLLLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
246-442 7.71e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.26  E-value: 7.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   246 DVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKA 325
Cdd:PHA02875   47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   326 DVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKESAL 405
Cdd:PHA02875  127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 38683816   406 TLACYKGHLEMVRFLLEAGADQEHKT---DEMHTALMEAC 442
Cdd:PHA02875  207 CYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDMIC 246
PHA02875 PHA02875
ankyrin repeat protein; Provisional
437-689 1.04e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.88  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   437 ALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAsLEEVNDEGY-TPLMEAAREGHEEM 515
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   516 VALLLGQGANINaqteetqetaltlaccggflevaDFLIKAGadielgcSTPLMEAAQEGHLELVKYLLAAGANVHATTA 595
Cdd:PHA02875   84 VEELLDLGKFAD-----------------------DVFYKDG-------MTPLHLATILKKLDIMKLLIARGADPDIPNT 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   596 TGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGG 675
Cdd:PHA02875  134 DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENN 213
                         250
                  ....*....|....
gi 38683816   676 HLAVVELLLAHGAD 689
Cdd:PHA02875  214 KIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
478-742 1.64e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   478 GHVELAALLIE-RGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTlACCGGFLEVADFLIKA 556
Cdd:PHA02874   12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLT-AIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   557 GADIELgCSTPLMEAaqeghlELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMK 636
Cdd:PHA02874   91 GVDTSI-LPIPCIEK------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   637 AARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLiEAAKGGHTSVVCYL 716
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL-HNAIIHNRSAIELL 241
                         250       260
                  ....*....|....*....|....*.
gi 38683816   717 LdypnNLLSAPPPDVTQLTPPSHDLN 742
Cdd:PHA02874  242 I----NNASINDQDIDGSTPLHHAIN 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
846-1145 1.90e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.38  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   846 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVGVVEILLDNGADIEAQSERTkdtpLSLACSGGRQEVVELLLARGAN 924
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPDHRDLTPLhIICKEPNKLGMKEMIRSINKCSVFYTLVA----IKDAFNNRNVEIFKIILTNRYK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   925 KEHrnVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRTGSKLGiSPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrN 1002
Cdd:PHA02878  127 NIQ--TIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTN-N 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1003 TALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMeaASGGYA---EVGRVLLDKGADVNAppvpssRDTALTIAAdk 1079
Cdd:PHA02878  203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH--ISVGYCkdyDILKLLLEHGVDVNA------KSYILGLTA-- 272
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683816  1080 ghykfcelligrgAHIDVRNKkgntplwlaangghlDVVQLLVQAGADVDAADNRKITPLMAAFRK 1145
Cdd:PHA02878  273 -------------LHSSIKSE---------------RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
901-1093 3.83e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.95  E-value: 3.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   901 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSrTGSKLGISPLMLAAMNGHT 980
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADD-VFYKDGMTPLHLATILKKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   981 AAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADV 1060
Cdd:PHA02875  116 DIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 38683816  1061 N----APPVpssrdTALTIAADKGHYKFCELLIGRGA 1093
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 ...
1476-1541 5.34e-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: 5.34e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINAL 1541
Cdd:cd22439    3 TQEITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEDGSTERSVTITGTPEAVSLAQYLINAR 68
PHA02875 PHA02875
ankyrin repeat protein; Provisional
906-1127 5.56e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 5.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   906 ACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGsklGI-SPLMLAAMNGHTAAVK 984
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIeSELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   985 LLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPP 1064
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683816  1065 VPSSrdTALTIAADKGHYKFCELLIGRGAHIDVRNKKGN-TPLWLAANGGHLDVVQLLVQAGAD 1127
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 ...
1478-1542 1.90e-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: 1.90e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816 1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22462    2 EILIPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDSATGERIVLISGTPDQARHAQNLIEAFI 66
PHA02875 PHA02875
ankyrin repeat protein; Provisional
271-491 2.63e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.64  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   271 LCLACSAGYYELAQVLLAMHANvEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVV 350
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGIN-PNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   351 KVLLESGASIED-HNENGHTPLMEAGSAGHVEVARLLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH 429
Cdd:PHA02875   85 EELLDLGKFADDvFYKDGMTPLHLATILKKLDIMKLLIARGADPDI-PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683816   430 KTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAdsfESPLTLAACGG----HVELAALLIERGA 491
Cdd:PHA02875  164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFG---KNGCVAALCYAiennKIDIVRLFIKRGA 226
KH smart00322
K homology RNA-binding domain;
1478-1542 3.04e-13

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 66.55  E-value: 3.04e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816    1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqKDKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIP--GPGSEERVVEITGPPENVEKAAELILEIL 68
PHA02875 PHA02875
ankyrin repeat protein; Provisional
939-1156 3.59e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 3.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   939 AASGGYVNIIKILLNAGaeINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRnTALTLACFQGRTEVVS 1018
Cdd:PHA02875    9 AILFGELDIARRLLDIG--INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1019 LLLDRKANVEHRA-KTGLTPLMEAASGGYAEVGRVLLDKGADvnaPPVPSS-RDTALTIAADKGHYKFCELLIGRGAHID 1096
Cdd:PHA02875   86 ELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGAD---PDIPNTdKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683816  1097 VRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRK-ITPLMAAFRKGHVKVVRYLVK 1156
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA02875 PHA02875
ankyrin repeat protein; Provisional
312-540 4.76e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.87  E-value: 4.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   312 GHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGAsIEDHNENG-HTPLMEAGSAGHVEVARLLLENG 390
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   391 AGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 470
Cdd:PHA02875   92 KFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683816   471 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHE-EMVALLLGQGANINAQTEETQETALTL 540
Cdd:PHA02875  172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNIMFMIEGEECTIL 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
818-894 5.42e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 5.42e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816    818 IYPAIDIDAQTEsNHDTALTLACAGGHEELVQTLLERgASIEHRDkKGFTPLILAATAGHVGVVEILLDNGADIEAQ 894
Cdd:pfam12796   17 LENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
449-684 2.33e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   449 VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGAN--I 526
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   527 NAQTEETQETALTLACCGGFLEVADFLIKagadielgcsTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACE 606
Cdd:PHA02874   97 LPIPCIEKDMIKTILDCGIDVNIKDAELK----------TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816   607 NGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHlAVVELLL 684
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM-NKCKNGFTPLHNAIIHNR-SAIELLI 242
PHA02876 PHA02876
ankyrin repeat protein; Provisional
914-1155 2.37e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 2.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   914 VVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDI 993
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD--DLSVLECAVDSKNIDTIKAIIDNRSNI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   994 NAQ----IETNRNTALtlacfqgrtEVVSLLLDRKANVEHRAKTGLTPLMEAASG-GYAEVGRVLLDKGADVNAPPVPSs 1068
Cdd:PHA02876  238 NKNdlslLKAIRNEDL---------ETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKG- 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1069 rDTALTIAADKGH-YKFCELLIGRGAHIDVRNKKGNTPLWLAAN-GGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKG 1146
Cdd:PHA02876  308 -ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                  ....*....
gi 38683816  1147 HVKVVRYLV 1155
Cdd:PHA02876  387 NVVIINTLL 395
PHA02878 PHA02878
ankyrin repeat protein; Provisional
880-1054 2.48e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   880 VVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 959
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   960 SRtgSKLGISPLMLAAMNGHTAAV-KLLLDMGSDINAQIETNRNTALTLACFQGRteVVSLLLDRKANVEHRAKTGLTPL 1038
Cdd:PHA02878  229 AR--DKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPL 304
                         170
                  ....*....|....*..
gi 38683816  1039 MEAASGGYA-EVGRVLL 1054
Cdd:PHA02878  305 SSAVKQYLCiNIGRILI 321
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
482-749 2.87e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.59  E-value: 2.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   482 LAALLIERGASLEE---VNDEGYTPLMEAAREGHEEMVALLLGQ--GANINAQTEETQET-ALTLACCG--GFLEVadfL 553
Cdd:PLN03192  468 LSQLLRLKTSTLIEamqTRQEDNVVILKNFLQHHKELHDLNVGDllGDNGGEHDDPNMASnLLTVASTGnaALLEE---L 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   554 IKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAgADLEHESEGG 630
Cdd:PLN03192  545 LKAKLDPDIGDSkgrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAG 623
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   631 RTpLMKAARAGHVCTVQFLISKGANVNrttaNNDH---TVLSLACAGGHLAVVELLLAHGADPTHRLKD---GSTMLIEA 704
Cdd:PLN03192  624 DL-LCTAAKRNDLTAMKELLKQGLNVD----SEDHqgaTALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELREL 698
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 38683816   705 AK----GGHTSVVCYLLDYPNNLLSAPPPDVTQLTPPSHDLNRAPRVPV 749
Cdd:PLN03192  699 LQkrelGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSI 747
PHA02878 PHA02878
ankyrin repeat protein; Provisional
236-426 2.95e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   236 RSLAEACSEGDVNAVRKLLIegrsvNEHTEEGESLLCLACSAGY-----YELAQVLLAMHANVEDRGIKGDITPLMAAAN 310
Cdd:PHA02878  103 VAIKDAFNNRNVEIFKIILT-----NRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   311 GGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL-MEAGSAGHVEVARLLLEN 389
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 38683816   390 GAGINTHSNEFKESALTLACYKGhlEMVRFLLEAGAD 426
Cdd:PHA02878  258 GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGAD 292
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
447-627 5.15e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.44  E-value: 5.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   447 VEVARLLLDSGAQVNMPADSFeSPLTLAACGGHVELAALLieRGASLEEVND-EGYTPLMEAAREGHEEMVALLLGQGAN 525
Cdd:PLN03192  507 LNVGDLLGDNGGEHDDPNMAS-NLLTVASTGNAALLEELL--KAKLDPDIGDsKGRTPLHIAASKGYEDCVLVLLKHACN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   526 INAQtEETQETALTLACCGGFLEVADFLIK--------AGADIelgcstpLMEAAQEGHLELVKYLLAAGANVHATTATG 597
Cdd:PLN03192  584 VHIR-DANGNTALWNAISAKHHKIFRILYHfasisdphAAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655
                         170       180       190
                  ....*....|....*....|....*....|
gi 38683816   598 DTALTYACENGHTDVADVLLQAGADLEHES 627
Cdd:PLN03192  656 ATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
303-354 5.36e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.68  E-value: 5.36e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683816    303 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLL 354
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
1476-1545 8.04e-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: 8.04e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1545
Cdd:cd22434    3 TTQVTIPKDLAGSIIGKGGQRIRQIRHESGASIKIDEPLPGSEDRIITITGTQDQIQNAQYLLQNSVKQY 72
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1106-1160 9.06e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 9.06e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38683816   1106 LWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVKEVNQ 1160
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV 55
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1000-1156 1.03e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1000 NRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGA--DVNAPPVPSSrdtaLTIAA 1077
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIESE----LHDAV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1078 DKGHYKFCELLIGRGAHI-DVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVK 1156
Cdd:PHA02875   77 EEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
Ank_4 pfam13637
Ankyrin repeats (many copies);
564-617 1.06e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 1.06e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683816    564 CSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLL 617
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
565-743 1.63e-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: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  565 STPLMEAAQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 638
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  639 RAGHVCTVQFLISKGANVN--RTTAN------------NDHtVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 704
Cdd:cd22192   98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 38683816  705 AKGGHTSVVCYLLDYpnnLLSAPPPDvtQLTPPSHDLNR 743
Cdd:cd22192  177 VLQPNKTFACQMYDL---ILSYDKED--DLQPLDLVPNN 210
PHA02878 PHA02878
ankyrin repeat protein; Provisional
347-639 2.62e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   347 VDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLengAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGAD 426
Cdd:PHA02878   50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   427 QEHKTDEMHtaLMEACMDGHVE--VARLLLDSGAQVNM-PADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTP 503
Cdd:PHA02878  127 NIQTIDLVY--IDKKSKDDIIEaeITKLLLSYGADINMkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   504 LMEAAREGHEEMVALLLGQGANINAQTEetqetaltlacCGgflevadflikagadielgcSTPL-MEAAQEGHLELVKY 582
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENGASTDARDK-----------CG--------------------NTPLhISVGYCKDYDILKL 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816   583 LLAAGANVHA-TTATGDTALTYACENghTDVADVLLQAGADLEHESEGGRTPLMKAAR 639
Cdd:PHA02878  254 LLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02878 PHA02878
ankyrin repeat protein; Provisional
304-560 5.71e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 5.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   304 PLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESgaSIEDHNENGHTPLMEAGSAGHVEVA 383
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   384 RLLLengagINTHSNEfKESALTLACYKGH-----LEMVRFLLEAGADQEHKT-DEMHTALMEACMDGHVEVARLLLDSG 457
Cdd:PHA02878  118 KIIL-----TNRYKNI-QTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   458 AQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPL-MEAAREGHEEMVALLLGQGANINAQTEETQET 536
Cdd:PHA02878  192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLT 271
                         250       260
                  ....*....|....*....|....
gi 38683816   537 ALTLACCGGflEVADFLIKAGADI 560
Cdd:PHA02878  272 ALHSSIKSE--RKLKLLLEYGADI 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
369-584 9.35e-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: 9.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  369 TPLMEAGSAGHVE-VARLLLENGAGINTHSnEFKESALTLACYKGHLEMVRFLLEAGAD--QEHKTDEMH---TALMEAC 442
Cdd:cd22192   19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRG-ALGETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  443 MDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPL---- 504
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilv 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  505 MEAAREGHEEMVALLLGQGANINAQTEETQETALTLaccggflevadflikagadielgcsTPLMEAAQEGHLELVKYLL 584
Cdd:cd22192  178 LQPNKTFACQMYDLILSYDKEDDLQPLDLVPNNQGL-------------------------TPFKLAAKEGNIVMFQHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
1102-1155 1.69e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.69e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683816   1102 GNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLV 1155
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
969-1132 1.93e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.43  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   969 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRnTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAE 1048
Cdd:PLN03192  527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1049 VGRVLLDKGADVNappvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADV 1128
Cdd:PLN03192  606 IFRILYHFASISD----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681

                  ....
gi 38683816  1129 DAAD 1132
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 ...
1477-1538 2.24e-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: 2.24e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816 1477 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1538
Cdd:cd09031    3 IELEVPENLVGAILGKGGKTLVEIQELTGARIQISKKGEfvpGTRNRKVTITGTPAAVQAAQYLI 67
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
229-407 3.61e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   229 NAGQSDNRSLAE----ACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTP 304
Cdd:PLN03192  516 NGGEHDDPNMASnlltVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN-TA 594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   305 LMAAANGGHVKIVKLLLAHKADVNAQssTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PLN03192  595 LWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
                         170       180
                  ....*....|....*....|....
gi 38683816   385 LLLENGAGInTHSNEFKE-SALTL 407
Cdd:PLN03192  673 LLIMNGADV-DKANTDDDfSPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
832-885 4.28e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 4.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683816    832 HDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL 885
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
303-429 5.80e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 5.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   303 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESgASIEDHNENGHTpLMEAGSAGHVEV 382
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDLTA 637
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 38683816   383 ARLLLENGAGINTHSNEFKeSALTLACYKGHLEMVRFLLEAGADQEH 429
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA03100 PHA03100
ankyrin repeat protein; Provisional
245-366 6.22e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   245 GDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR-------GIKGDI------TPLMA 307
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsyGVPINIkdvygfTPLHY 198
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816   308 AANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNEN 366
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
925-1139 6.68e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 6.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   925 KEHR----NVSDYTPLSLAASGGYVNIIKILLNAGAEINsRTGSKlGISPLMLAAMNGHTAAVKLLLdmgSDINAQIETN 1000
Cdd:PHA02878   26 TENYstsaSLIPFIPLHQAVEARNLDVVKSLLTRGHNVN-QPDHR-DLTPLHIICKEPNKLGMKEMI---RSINKCSVFY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1001 RNTALTLACFQGRTEVV-SLLLDRKANVEhraKTGLTPLMEAASGGY--AEVGRVLLDKGADVNAPPvPSSRDTALTIAA 1077
Cdd:PHA02878  101 TLVAIKDAFNNRNVEIFkIILTNRYKNIQ---TIDLVYIDKKSKDDIieAEITKLLLSYGADINMKD-RHKGNTALHYAT 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816  1078 DKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1139
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 ...
1486-1540 7.85e-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: 7.85e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816 1486 ISRVIGRGGCNINAIREFTGAHIDIDKQKDKT---GDRIITIRGGTESTRQATQLINA 1540
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 ...
1477-1542 9.92e-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: 9.92e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816 1477 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKT--GDRIITIRGGTESTRQATQLINALI 1542
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) ...
1476-1540 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 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1540
Cdd:cd22523    3 SQEFLIPNDLIGCVIGRQGSKISEIRQMSGAHIKIGNQTEGTSERHVTITGSPVSITLAQYLITT 67
Ank_4 pfam13637
Ankyrin repeats (many copies);
1069-1122 1.31e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.31e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683816   1069 RDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLV 1122
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
668-721 1.49e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 1.49e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683816    668 LSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPN 721
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
238-398 1.73e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLL----------------AMHANVEDRGIKGD 301
Cdd:PHA02874   39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekDMIKTILDCGIDVN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   302 I------TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAG 375
Cdd:PHA02874  119 IkdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
                         170       180
                  ....*....|....*....|...
gi 38683816   376 SAGHVEVARLLLENGAGINTHSN 398
Cdd:PHA02874  199 EYGDYACIKLLIDHGNHIMNKCK 221
Ank_4 pfam13637
Ankyrin repeats (many copies);
334-387 2.03e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 2.03e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683816    334 GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLL 387
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
841-919 2.08e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 2.08e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816   841 AGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAqSERTKDTPLSLACSGGRQEVVELLL 919
Cdd:PTZ00322   91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
367-421 2.09e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 2.09e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38683816    367 GHTPLMEAGSAGHVEVARLLLENGAGINtHSNEFKESALTLACYKGHLEMVRFLL 421
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
894-1123 2.10e-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: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  894 QSERTKDTPLSLACSGGRQEVVELLL--------ARGANKEhrnvsdyTPLSLAASGGYVNIIKILLNAGAE-INSRTGS 964
Cdd:cd22192   12 QQKRISESPLLLAAKENDVQAIKKLLkcpscdlfQRGALGE-------TALHVAALYDNLEAAVVLMEAAPElVNEPMTS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  965 KL--GISPLMLAAMNGHTAAVKLLLDMGSDINaqieTNRNTALtlaCFqgrtevvsllLDRKANV----EHraktgltPL 1038
Cdd:cd22192   85 DLyqGETALHIAVVNQNLNLVRELIARGADVV----SPRATGT---FF----------RPGPKNLiyygEH-------PL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1039 MEAASGGYAEVGRVLLDKGADVNAppvpssRD----TALTIAADKGHYKF-CE---LLIGRGAHID------VRNKKGNT 1104
Cdd:cd22192  141 SFAACVGNEEIVRLLIEHGADIRA------QDslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLT 214
                        250
                 ....*....|....*....
gi 38683816 1105 PLWLAANGGHLDVVQLLVQ 1123
Cdd:cd22192  215 PFKLAAKEGNIVMFQHLVQ 233
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
1477-1538 2.13e-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: 2.13e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816 1477 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQK-DKTGDRIITIRGGTESTRQATQLI 1538
Cdd:cd22457    1 QNISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAKAPhDETGERMFTITGTPEANDRALRLL 63
Ank_4 pfam13637
Ankyrin repeats (many copies);
597-650 2.24e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.24e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683816    597 GDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLI 650
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
666-717 2.24e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.24e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683816    666 TVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLL 717
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
238-510 2.44e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSA----GYYELAQVLLAMHANVEDRGIKgditplmAAANGGH 313
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIK-------DAFNNRN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   314 VKIVKLLLAHKADVNAQSStgntaLTYACAGGYVD-----VVKVLLESGASIEDHNEN-GHTPLMEAGSAGHVEVARLLL 387
Cdd:PHA02878  114 VEIFKIILTNRYKNIQTID-----LVYIDKKSKDDiieaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   388 ENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEA---CMDghVEVARLLLDSGAQVNmpA 464
Cdd:PHA02878  189 SYGANVNI-PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVN--A 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 38683816   465 DSFESPLTLAACGGHVE-LAALLIERGASLEEVNDEGYTPLMEAARE 510
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 ...
1476-1538 3.84e-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: 3.84e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGD--RIITIRGGTESTRQATQLI 1538
Cdd:cd22429    3 TEELHVPQRAVGRIIGRGGETIRSICRTSGAKVKCDRESDDTLDlvRLITITGTKKEVDAAKSLI 67
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
1475-1545 4.51e-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: 54.79  E-value: 4.51e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816 1475 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDP 1545
Cdd:cd02393    4 RITTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIED------DGTVTIFATDkESAEAAKAMIEDIVAEP 69
PHA02798 PHA02798
ankyrin-like protein; Provisional
314-531 4.59e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 61.39  E-value: 4.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   314 VKIVKLLLAHKADVNAQSSTGNTALT--------YACAggyVDVVKVLLESGASIEDHNENGHTP---LMEAGSAGHVEV 382
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCtilsnikdYKHM---LDIVKILIENGADINKKNSDGETPlycLLSNGYINNLEI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   383 ARLLLENGAGINTHSNeFKESALTLACYKGH---LEMVRFLLEAGAD-----QEHKTDEMHTALME--ACMDghVEVARL 452
Cdd:PHA02798  128 LLFMIENGADTTLLDK-DGFTMLQVYLQSNHhidIEIIKLLLEKGVDinthnNKEKYDTLHCYFKYniDRID--ADILKL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   453 LLDSGAQVNMPADSFESPL-----TLAACGGHVELAAL-LIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANI 526
Cdd:PHA02798  205 FVDNGFIINKENKSHKKKFmeylnSLLYDNKRFKKNILdFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDI 284

                  ....*
gi 38683816   527 NAQTE 531
Cdd:PHA02798  285 NIITE 289
KH-I_NOVA_rpt2 cd22436
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
1478-1538 5.93e-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: 5.93e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816 1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD--KTGDRIITIRGGTESTRQATQLI 1538
Cdd:cd22436    4 KILVPNSTAGMIIGKGGATIKAIMEQSGARVQISQKPEsiNLQERVVTVTGEPEANRKAVSLI 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
469-520 9.70e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 9.70e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683816    469 SPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLL 520
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
434-487 1.01e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683816    434 MHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLI 487
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
834-953 1.10e-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: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  834 TALTLACAGGHEELVQTLLERGASIE---------HRDKK-----GFTPLILAATAGHVGVVEILLDNGADIEAQsERTK 899
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLG 169
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816  900 DTPL---------SLACsggrqEVVELLLARGANK-----EH-RNVSDYTPLSLAASGGYVNIIKILLN 953
Cdd:cd22192  170 NTVLhilvlqpnkTFAC-----QMYDLILSYDKEDdlqplDLvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
990-1155 1.23e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   990 GSDINAQIETNRNTALTLacfqGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSsr 1069
Cdd:PLN03192  518 GEHDDPNMASNLLTVAST----GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG-- 591
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1070 DTALTIAADKGHYKFCELLIgRGAHIDVRNKKGNTpLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVK 1149
Cdd:PLN03192  592 NTALWNAISAKHHKIFRILY-HFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669

                  ....*.
gi 38683816  1150 VVRYLV 1155
Cdd:PLN03192  670 MVRLLI 675
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1479-1540 1.50e-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: 1.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816 1479 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqKDKTGDrIITIRGGTESTRQATQLINA 1540
Cdd:cd22452    6 IKVSPRYFGRIIGPGGSNINQIREKSGCFINVPK-KNKESD-VITLRGTKEGVEKAEEMIKK 65
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1831-2086 1.91e-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: 60.17  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1831 PPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMT-------VPPLATSSAPVAVPSTAP 1903
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTpqssqsqVPPGPSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1904 VTYPMPQTPMGCP---QPTPK--METPAIRPPPHGTTAPHKNSASVQNSSvavlsvnHIK--RPHSVPSSVQLPSTLSTQ 1976
Cdd:pfam03154  327 TPPSQSQLQSQQPpreQPLPPapLSMPHIKPPPTTPIPQLPNPQSHKHPP-------HLSgpSPFQMNSNLPPPPALKPL 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1977 SACQNSVHPANKPiapnfsAPLPFGPFSTLFENSPTSAHAFWGGSVVSSQSTPESMLSGKSSYLPNSD-PLHQSDTSKAP 2055
Cdd:pfam03154  400 SSLSTHHPPSAHP------PPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPfPQHPFVPGGPP 473
                          250       260       270
                   ....*....|....*....|....*....|.
gi 38683816   2056 GFRPPLQRPAPSPSGIVNMDSPyGSVTPSST 2086
Cdd:pfam03154  474 PITPPSGPPTSTSSAMPGIQPP-SSASVSSS 503
PHA02878 PHA02878
ankyrin repeat protein; Provisional
346-731 2.56e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   346 YVDVVKVLLESGASIeDHNENGHT--------PLMEAGSAGHVEVARLLLENGAGINTHSNEFKeSALTLACYK----GH 413
Cdd:PHA02878    9 YTDNYETILKYIEYI-DHTENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDL-TPLHIICKEpnklGM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   414 LEMVRFLLEAGADQEHKtdemhtALMEACMDGHVEVARLLLdsgaqvnmpADSFESpltlaacgghvelaalliERGASL 493
Cdd:PHA02878   87 KEMIRSINKCSVFYTLV------AIKDAFNNRNVEIFKIIL---------TNRYKN------------------IQTIDL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   494 EEVNDEGYTPLMEAaregheEMVALLLGQGANINAQTEETQetaltlaccggflevadflikagadielgcSTPLMEAAQ 573
Cdd:PHA02878  134 VYIDKKSKDDIIEA------EITKLLLSYGADINMKDRHKG------------------------------NTALHYATE 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   574 EGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPL-MKAARAGHVCTVQFLISK 652
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816   653 GANVNRTTANNDHTVLSLACAGGHlaVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPNNLLSAPPPDV 731
Cdd:PHA02878  258 GVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334
Ank_4 pfam13637
Ankyrin repeats (many copies);
500-554 3.37e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 3.37e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38683816    500 GYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLI 554
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
663-924 4.55e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   663 NDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYpNNLLSAPPPDVTQltpPSHD-L 741
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKH-GAIPDVKYPDIES---ELHDaV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   742 NRAPRVPVQALPMVvppqepdkppanvattlpirNKAVSGRASAMSNTPTHsiAASISQPqtptpspiISPSAMLPIYPA 821
Cdd:PHA02875   77 EEGDVKAVEELLDL--------------------GKFADDVFYKDGMTPLH--LATILKK--------LDIMKLLIARGA 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   822 iDIDAqTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDT 901
Cdd:PHA02875  127 -DPDI-PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
                         250       260
                  ....*....|....*....|...
gi 38683816   902 PLSLACSGGRQEVVELLLARGAN 924
Cdd:PHA02875  205 ALCYAIENNKIDIVRLFIKRGAD 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
630-684 4.84e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 4.84e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38683816    630 GRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDhTVLSLACAGGHLAVVELLL 684
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) ...
1476-1540 4.92e-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: 4.92e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1540
Cdd:cd22521    6 SHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINA 70
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1474-1544 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: 52.41  E-value: 5.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816 1474 RRSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRI--------ITIRGGTESTRQATQLINALIKD 1544
Cdd:cd22446    6 KVTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGNYDEddddetveISIEGDAEGVELAKKEIEAIVKE 84
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
938-1040 5.57e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 5.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   938 LAASGGYVNIiKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDINAqIETNRNTALTLACFQGRTEVV 1017
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCRDYD--GRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVV 164
                          90       100       110
                  ....*....|....*....|....*....|
gi 38683816  1018 SLLL-------DRKANVEHRAKTGLTPLME 1040
Cdd:PTZ00322  165 QLLSrhsqchfELGANAKPDSFTGKPPSLE 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
403-454 7.23e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 7.23e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683816    403 SALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLL 454
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
314-618 7.57e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 57.44  E-value: 7.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   314 VKIVKLLLAHKADVNAQS--STGNTAL---TYACAGGYVDVVKVLLESGASIEDHNENGHTPLM---EAGSAGHVEVARL 385
Cdd:PHA02989   50 IKIVKLLIDNGADVNYKGyiETPLCAVlrnREITSNKIKKIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRF 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   386 LLENGAGINTHSNE--FKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVArllldsgaqvnmp 463
Cdd:PHA02989  130 LLSKGINVNDVKNSrgYNLLHMYLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMNIYLRNDIDVI------------- 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   464 adsfespltlaacggHVELAALLIERGASLEEvNDEGYTPLMEAAREGHEEMValllgqganinaqteeTQEtaltlacc 543
Cdd:PHA02989  197 ---------------SIKVIKYLIKKGVNIET-NNNGSESVLESFLDNNKILS----------------KKE-------- 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816   544 ggfLEVADFL---IKAGADIELGCsTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQ 618
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 ...
1479-1543 8.38e-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: 51.65  E-value: 8.38e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816 1479 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRI--------ITIRGGTESTRQATQLINALIK 1543
Cdd:cd22447    8 VPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPADedddtmveVTITGDEFNVQHAKQRIEEIIS 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
611-1000 1.16e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.60  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   611 DVADVLLQAGADLEHESEGGRTPLMKAARAGHVCT-----VQFLISKGANVNRTTANNDHTVLSLACAG-GHLAVVELLL 684
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   685 AHGADPTHRLKDGSTMLIEAAKGGHTsvvcylldypnnllsapppdvtqltppshDLNraprvpvqalpmvvppqepdkp 764
Cdd:PHA03100  129 DNGANVNIKNSDGENLLHLYLESNKI-----------------------------DLK---------------------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   765 panvattlpirnkavsgrasamsntpthsiaasisqpqtptpspIISpsamLPIYPAIDIDAQTEsnhdtaltlacaggh 844
Cdd:PHA03100  158 --------------------------------------------ILK----LLIDKGVDINAKNR--------------- 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   845 eelVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERtKDTPLSLACSGGRQEVVELLLARGAN 924
Cdd:PHA03100  175 ---VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY-GDTPLHIAILNNNKEIFKLLLNNGPS 250
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816   925 kehrnvsdytplslaasggyVNIIK--ILLNAGAEINSRTGSKLGISPLMLAamnghtaavkLLLDMGSDINAQIETN 1000
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 ...
1481-1542 1.37e-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: 50.33  E-value: 1.37e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816 1481 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1542
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 ...
1481-1538 1.38e-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: 1.38e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816 1481 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTG-DRIITIRGGTESTRQATQLI 1538
Cdd:cd22400    6 VPSEFVGAIIGKGGATIRQITQQTGARIDIHRKENAGAaEKAITIYGTPEGCSSACKQI 64
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1101-1133 1.54e-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: 1.54e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 38683816   1101 KGNTPLWLAA-NGGHLDVVQLLVQAGADVDAADN 1133
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1478-1543 1.61e-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: 1.61e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683816 1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqkDKTGDRIITIRGGTESTRQATQLINALIK 1543
Cdd:cd22449    7 KFDVPAKYVPHIIGKKGANINKLREEYGVKIDFE---DKTGEGNVEIKGSKKNVEEAKKRILSQID 69
PHA02878 PHA02878
ankyrin repeat protein; Provisional
823-1011 1.64e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   823 DIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSeRTKDTP 902
Cdd:PHA02878  159 DINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD-KCGNTP 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   903 LSLACSggrqevvelllargankehrNVSDYtplslaasggyvNIIKILLNAGAEINSRTgSKLGISPLMLAAMNghTAA 982
Cdd:PHA02878  238 LHISVG--------------------YCKDY------------DILKLLLEHGVDVNAKS-YILGLTALHSSIKS--ERK 282
                         170       180
                  ....*....|....*....|....*....
gi 38683816   983 VKLLLDMGSDINAqIETNRNTALTLACFQ 1011
Cdd:PHA02878  283 LKLLLEYGADINS-LNSYKLTPLSSAVKQ 310
PHA02989 PHA02989
ankyrin repeat protein; Provisional
913-1151 1.66e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 56.29  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   913 EVVELLLARGANKEHRNVSDyTPL------SLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAV--- 983
Cdd:PHA02989   51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFN--GVSPIVCFIYNSNINNCdml 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   984 KLLLDMGSDINAQIETNRNTAL--TLACFQGRTEVVSLLLDRKANV-EHRAKTGLTP----LMEAASGGYAEVGRVLLDK 1056
Cdd:PHA02989  128 RFLLSKGINVNDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKK 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1057 GADVNAPPVPSSRDTALTIAADKGHYKFC-ELL--IGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADN 1133
Cdd:PHA02989  208 GVNIETNNNGSESVLESFLDNNKILSKKEfKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSK 287
                         250
                  ....*....|....*...
gi 38683816  1134 RKITPLMAAFRKGHVKVV 1151
Cdd:PHA02989  288 DGDTVLTYAIKHGNIDML 305
Ank_5 pfam13857
Ankyrin repeats (many copies);
851-906 1.84e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.84e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816    851 LLERG-ASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKdTPLSLA 906
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
308-387 1.90e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   308 AANGGHVKIvKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLL 387
Cdd:PTZ00322   90 AASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
969-1021 2.19e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 2.19e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 38683816    969 SPLMLAAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLL 1021
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; ...
1476-1539 2.31e-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: 2.31e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLIN 1539
Cdd:cd22411    1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDL--PEENSDSDVITITGKKEDVEKARERIL 62
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
238-421 2.47e-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: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  238 LAEACSEGDVNAVRKLLiEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDI----TPLMAAANG 311
Cdd:cd22192   21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLyqgeTALHIAVVN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  312 GHVKIVKLLLAHKADVNAQSST--------------GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL----ME 373
Cdd:cd22192  100 QNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvLQ 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 38683816  374 AGSAGHVEVARLLLENGAGINTHS-----NEFKESALTLACYKGHLEMVRFLL 421
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 ...
1476-1538 3.17e-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: 3.17e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1538
Cdd:cd22514    2 SVTIGVPDEHIGAILGRGGRTINEIQQHSGARIKISDRGDfvsGTRNRKVTITGPQDAVQMAQYLL 67
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
969-1156 3.85e-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: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  969 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKT-----GLTPLMEAAS 1043
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1044 GGYAEVGRVLLDKGADVNAPPV------PSSR------DTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLwlaan 1111
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPRAtgtffrPGPKnliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL----- 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816 1112 ggHLDVVQ------------LLVQAGADVDAA-----DNRKITPLMAAFRKGHVKVVRYLVK 1156
Cdd:cd22192  174 --HILVLQpnktfacqmydlILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQ 233
KH-I_PCBP3_rpt3 cd22522
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
1476-1540 4.96e-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: 4.96e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1540
Cdd:cd22522   10 THELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGSPANISLAQYLINA 74
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
828-1007 5.51e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 5.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   828 TESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQsERTKDTPLSLAC 907
Cdd:PLN03192  521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR-DANGNTALWNAI 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   908 SGGRQEVVELLLARGANKEHRNVSDYtpLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLL 987
Cdd:PLN03192  600 SAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSE--DHQGATALQVAMAEDHVDMVRLLI 675
                         170       180
                  ....*....|....*....|
gi 38683816   988 DMGSDINAQIETNRNTALTL 1007
Cdd:PLN03192  676 MNGADVDKANTDDDFSPTEL 695
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1544-1971 5.60e-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: 55.16  E-value: 5.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1544 DPdKEIDElipKNRLKSSSANSKIGSSAPTTTAANTSLMGIKMTTVALSSTSQTATALTVPAISSASTH-KTIKNPVNNV 1622
Cdd:pfam03154  133 DP-KDIDQ---DNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAgPTPSAPSVPP 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1623 RPGFPVSLPLAYPPPQFAHALLAAQTfQQIRPPRLPMTHfggtfPPAQSTwgpfpvrPLSPARATNSPKPHMVPRHSNQN 1702
Cdd:pfam03154  209 QGSPATSQPPNQTQSTAAPHTLIQQT-PTLHPQRLPSPH-----PPLQPM-------TQPPPPSQVSPQPLPQPSLHGQM 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1703 SSGSQVNSAGSLTSSPTTTTSSSASTVPGTSTNGSPS-SPSVRRQLFVTVVKTSNATTTTVTTTASNNNTAPtnATYPMP 1781
Cdd:pfam03154  276 PPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGpSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPP--APLSMP 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1782 TAKehypvsSPSSPSPPAQPGGVSRNSPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPP 1861
Cdd:pfam03154  354 HIK------PPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPP 427
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1862 GS----VSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPvtypmPQTPMGCPQPTPKMETPAIRPPphgTTAP 1937
Cdd:pfam03154  428 PAqppvLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPP-----PITPPSGPPTSTSSAMPGIQPP---SSAS 499
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 38683816   1938 HKNSASVQNSSVAVLSVNHIK--------RPHSVPSSVQLPS 1971
Cdd:pfam03154  500 VSSSGPVPAAVSCPLPPVQIKeealdeaeEPESPPPPPRSPS 541
KH-I_FUBP_rpt4 cd22399
fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1480-1539 6.60e-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: 48.37  E-value: 6.60e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683816 1480 SVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD-KTGDRIITIRGGTESTRQATQLIN 1539
Cdd:cd22399    5 LVPANKCGLVIGKGGETIRQINQQSGAHVELDRNPPpNPNEKLFIIRGNPQQIEHAKQLIR 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
1021-1156 7.04e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 7.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1021 LDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCE---LLIGRGAHIDV 1097
Cdd:PHA03095    1 DEEDESVDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816  1098 RNKKGNTPLWL-AANGGHLDVVQLLVQAGADVDAADNRKITPL---MAAFRKgHVKVVRYLVK 1156
Cdd:PHA03095   79 PERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvyLSGFNI-NPKVIRLLLR 140
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
818-1054 9.66e-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: 9.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    818 IYPAIDIDaqtESNHDTALTLACAGGHEELVQTLLERGAS--IEHRDKKGFTPLILAATAG-HVGVVEILLDNGADIEaq 894
Cdd:TIGR00870    6 IVPAEESP---LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    895 serTKDTPLsLACSGGRQEVVELLLA-------RGANKEHRNVS-------DYTPLSLAASGGYVNIIKILLNAGAEINS 960
Cdd:TIGR00870   81 ---VGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    961 R------------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIE---------------TNRNTALTLACFQgr 1013
Cdd:TIGR00870  157 RacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSlgntllhllvmenefKAEYEELSCQMYN-- 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 38683816   1014 tEVVSLL--LDRKANVEH-RAKTGLTPLMEAASGGYAEVGRVLL 1054
Cdd:TIGR00870  235 -FALSLLdkLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
KH-I_FUBP2_rpt4 cd22488
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1480-1538 1.01e-06

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: 48.17  E-value: 1.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816 1480 SVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGD---RIITIRGGTESTRQATQLI 1538
Cdd:cd22488    5 SIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQPPPNGDpnfKLFIIRGSPQQIDHAKQLI 66
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1481-1524 1.30e-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: 1.30e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 38683816 1481 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITI 1524
Cdd:cd22459    8 CPVSKAGSVIGKGGEIIKQLRQETGARIKVEDGVPGTEERVITI 51
Ank_4 pfam13637
Ankyrin repeats (many copies);
933-987 1.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38683816    933 YTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLL 987
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGN--GETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
578-893 1.57e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   578 ELVKYLLAAGANVHATTATGDTALTYACENGHT-----DVADVLLQAGADLEHESEGGRTPLMKAA--RAGHVCTVQFLI 650
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   651 SKGANVNRTTANNdHTVLSLACAGGH--LAVVELLLAHGADpthrlkdgstmlIEAakgghTSVVCYLLDYPnnllsapp 728
Cdd:PHA03100  129 DNGANVNIKNSDG-ENLLHLYLESNKidLKILKLLIDKGVD------------INA-----KNRVNYLLSYG-------- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   729 pdvtqltppshdlnraprvpvqalpmvVPPQEPDKppanvattlpirnkavsgrasaMSNTPTHSiaasisqpqtptpsp 808
Cdd:PHA03100  183 ---------------------------VPINIKDV----------------------YGFTPLHY--------------- 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   809 iispsamlpiypaididaqtesnhdtaltlACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNG 888
Cdd:PHA03100  199 ------------------------------AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248

                  ....*
gi 38683816   889 ADIEA 893
Cdd:PHA03100  249 PSIKT 253
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
634-738 2.00e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   634 LMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVV 713
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90       100
                  ....*....|....*....|....*...
gi 38683816   714 CYLLDYPNNLLSA---PPPDVTQLTPPS 738
Cdd:PTZ00322  165 QLLSRHSQCHFELganAKPDSFTGKPPS 192
PHA02989 PHA02989
ankyrin repeat protein; Provisional
982-1183 2.10e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.82  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   982 AVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRA--KTGLTPLM---EAASGGYAEVGRVLLDK 1056
Cdd:PHA02989   18 ALEFLLRTGFDVNEEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGyiETPLCAVLrnrEITSNKIKKIVKLLLKF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1057 GADVNAPPVPSSRDTALTIAadKGHYKFCE---LLIGRGAHI-DVRNKKGNTPL--WLAANGGHLDVVQLLVQAGADV-D 1129
Cdd:PHA02989   98 GADINLKTFNGVSPIVCFIY--NSNINNCDmlrFLLSKGINVnDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfE 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816  1130 AADNRKITPLMAAFRKG----HVKVVRYLVK-----EVNQFPSDSECMRYIAtiTDKEMLKKC 1183
Cdd:PHA02989  176 KTSLYGLTPMNIYLRNDidviSIKVIKYLIKkgvniETNNNGSESVLESFLD--NNKILSKKE 236
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1479-1542 2.33e-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: 46.87  E-value: 2.33e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683816 1479 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22398    4 VPVPRFAVGVVIGKGGEMIKKIQNETGARVQFKPDDGNSPDRICVITGPPDQVQHAARMIQELI 67
PHA03247 PHA03247
large tegument protein UL36; Provisional
1774-2206 2.79e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1774 TNATYPMPTAKEHYPVSSPSSPSPPAQPGGVSRNSPLDcGSASPNKVASSSeqeaGSPPVVETTNTRPPNSSSSSGSSSA 1853
Cdd:PHA03247 2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRL----GRAAQASSPPQRPRRRAARPTVGSL 2695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1854 HSNQQQPPGSVSQEPRPPLQQSQVPPPEV----RMTVPPLATSSAPVAVPST-----APVTYPMPQTPMGCPQPTPKMET 1924
Cdd:PHA03247 2696 TSLADPPPPPPTPEPAPHALVSATPLPPGpaaaRQASPALPAAPAPPAVPAGpatpgGPARPARPPTTAGPPAPAPPAAP 2775
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1925 PAirPPPHGTTAPHKNSASVQNSSVAVLSvnhikRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIAPNfSAPLPFGPFS 2004
Cdd:PHA03247 2776 AA--GPPRRLTRPAVASLSESRESLPSPW-----DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT-APPPPPGPPP 2847
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  2005 TlfensPTSAhafwGGSVVssqstPESMLSGKSsylpnsdPLHQSDTSKAPGFRPP---LQRPAPSPSGIVNMDSPYGSV 2081
Cdd:PHA03247 2848 P-----SLPL----GGSVA-----PGGDVRRRP-------PSRSPAAKPAAPARPPvrrLARPAVSRSTESFALPPDQPE 2906
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  2082 TPssthlgnfasnisggqmygpgaplggapaaanfnRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSP-APSSVPLGS 2160
Cdd:PHA03247 2907 RP----------------------------------PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPlAPTTDPAGA 2952
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 38683816  2161 EKPSNVSQDRKVPVPIGTERSARIRQTGTSAPSVIGSNLSTSVGHS 2206
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 ...
1481-1538 3.29e-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: 3.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816 1481 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLI 1538
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 ...
1481-1542 4.39e-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: 4.39e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816 1481 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQK-DKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd02396    8 VPASQCGSLIGKGGSKIKEIRESTGASVQVASEMlPNSTERAVTISGSPEAITKCVEQICCVM 70
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
436-652 4.41e-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: 4.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  436 TALMEACMDGHVE-VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIErgASLEEVND-------EGYTPLMEA 507
Cdd:cd22192   19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  508 AREGHEEMVALLLGQGANInaqteetqetaLTLACCGGFlevadFLIKAGADIELGcSTPLMEAAQEGHLELVKYLLAAG 587
Cdd:cd22192   97 VVNQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNLIYYG-EHPLSFAACVGNEEIVRLLIEHG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  588 ANVHATTATGDTAL---------TYACEnghtdVADVLL-----QAGADLEHESEG-GRTPLMKAARAGHVCTVQFLISK 652
Cdd:cd22192  160 ADIRAQDSLGNTVLhilvlqpnkTFACQ-----MYDLILsydkeDDLQPLDLVPNNqGLTPFKLAAKEGNIVMFQHLVQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
880-1062 4.42e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   880 VVEILLDNGadiEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 959
Cdd:PLN03192  509 VGDLLGDNG---GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   960 SRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrntALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLM 1039
Cdd:PLN03192  586 IRDAN--GNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
                         170       180
                  ....*....|....*....|...
gi 38683816  1040 EAASGGYAEVGRVLLDKGADVNA 1062
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 ...
1481-1538 4.97e-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: 4.97e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683816 1481 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDK---TGDRIITIRGGTESTRQATQLI 1538
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 ...
1486-1538 5.25e-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: 5.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 38683816 1486 ISRVIGRGGCNINAIREFTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLI 1538
Cdd:cd22438   10 VGSIIGKKGETIKKFREESGARINI--SDGSCPERIVTVTGTTDAVFKAFELI 60
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
499-531 5.62e-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: 5.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 38683816    499 EGYTPLMEAA-REGHEEMVALLLGQGANINAQTE 531
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
KH-I_FUBP3_rpt4 cd22489
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1480-1539 5.78e-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: 5.78e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816 1480 SVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGD---RIITIRGGTESTRQATQLIN 1539
Cdd:cd22489    5 TIPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNTDpnvRIFTIRGVPQQIEHARQLID 67
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1481-1542 6.32e-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: 6.32e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816 1481 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDK-----TGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22460    6 VASSQAGSLIGKGGAIIKQIREESGASVRILPEEELppcasPDDRVVQISGEAQAVKKALELVSSRL 72
Ank_4 pfam13637
Ankyrin repeats (many copies);
901-952 6.64e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 6.64e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683816    901 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILL 952
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, ...
1477-1543 6.83e-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: 6.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816 1477 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDriITIRGGTESTRQATQLINALIK 1543
Cdd:cd02394    4 TTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDE--IRIEGSPEGVKKAKAEILELVD 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
867-919 7.69e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 7.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 38683816    867 TPLILAATAGHVGVVEILLDNGADIEAQSERtKDTPLSLACSGGRQEVVELLL 919
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
967-1123 8.18e-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: 8.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  967 GISPLMLAAMN---GHTAAVKLLLDMGSD-------INAQIETNR---NTALTLACFQGRTEVVSLLLDRKANVEHRA-- 1031
Cdd:cd21882   26 GKTCLHKAALNlndGVNEAIMLLLEAAPDsgnpkelVNAPCTDEFyqgQTALHIAIENRNLNLVRLLVENGADVSARAtg 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1032 ----KTGLT-------PLMEAASGGYAEVGRVLLDKGADvnaPPVPSSRDT-------ALTIAADK--GHYKFC----EL 1087
Cdd:cd21882  106 rffrKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQ---PAALEAQDSlgntvlhALVLQADNtpENSAFVcqmyNL 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 38683816 1088 LIGRGAHID-------VRNKKGNTPLWLAANGGHLDVVQLLVQ 1123
Cdd:cd21882  183 LLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1857-2066 8.64e-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: 51.31  E-value: 8.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1857 QQQPPgsVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPVTYPMPQTPMGCPQP-TPKMETPAIRPP----P 1931
Cdd:pfam03154  168 QTQPP--VLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPhTLIQQTPTLHPQrlpsP 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1932 HGTTAPhknsasvqnssvavlsvnhikRPHSVPssvqlPSTLSTQSACQNSVHPANKPIA-------PNFSAPLPFGPFS 2004
Cdd:pfam03154  246 HPPLQP---------------------MTQPPP-----PSQVSPQPLPQPSLHGQMPPMPhslqtgpSHMQHPVPPQPFP 299
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683816   2005 TLFENS----PTSAHAFWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSkAPGFRPPLQRPAP 2066
Cdd:pfam03154  300 LTPQSSqsqvPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLS-MPHIKPPPTTPIP 364
Ank_5 pfam13857
Ankyrin repeats (many copies);
386-438 8.85e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 8.85e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 38683816    386 LLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTAL 438
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
1034-1089 9.00e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 9.00e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 38683816   1034 GLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLI 1089
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
320-371 9.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 9.11e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 38683816    320 LLAHK-ADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL 371
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1038-1121 9.15e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 9.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1038 LMEAASGGYAEVGRVLLDKGADvnappvPSSRD----TALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGG 1113
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGAD------PNCRDydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159

                  ....*...
gi 38683816  1114 HLDVVQLL 1121
Cdd:PTZ00322  160 FREVVQLL 167
PHA02875 PHA02875
ankyrin repeat protein; Provisional
568-719 9.44e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 9.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   568 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQ 647
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816   648 FLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDY 719
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
PRK11633 PRK11633
cell division protein DedD; Provisional
1859-1968 1.02e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 49.23  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1859 QPPGSVSQEPR------PPLQQSQVPPPEVRMTVPPlatssAPVAVPSTAPVTYPMPQT---PMGCPQPTPKmetPAIRP 1929
Cdd:PRK11633   66 QPPEGAAEAVRagdaaaPSLDPATVAPPNTPVEPEP-----APVEPPKPKPVEKPKPKPkpqQKVEAPPAPK---PEPKP 137
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 38683816  1930 PPHGTTAPH-----------KNSASVqNSSVAVLSVNHIkRPHSVPSS-VQ 1968
Cdd:PRK11633  138 VVEEKAAPTgkayvvqlgalKNADKV-NEIVAKLRLSGY-RVYTVPSTpVQ 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1101-1130 1.09e-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: 1.09e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 38683816    1101 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1130
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
303-341 1.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.10e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 38683816    303 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYA 341
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
371-475 1.12e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   371 LMEAGSAGHVEVARLLLENGAgiNTHSNEFKESA-LTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEV 449
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGA--DPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 38683816   450 ARLLL-----DSGAQVNMPADSF--------ESPLTLAA 475
Cdd:PTZ00322  164 VQLLSrhsqcHFELGANAKPDSFtgkppsleDSPISSHH 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
499-528 1.14e-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: 1.14e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 38683816     499 EGYTPLMEAAREGHEEMVALLLGQGANINA 528
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
1483-1544 1.21e-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: 1.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816 1483 STVISRVIGRGGCNINAIREFTGAHIDIDKQKDktgDRIITIRGGTESTRQATQLINALIKD 1544
Cdd:cd22430    8 SSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQ---EAEVKIFGSDEAQQKAKELIDELVGR 66
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
423-521 1.25e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   423 AGADQEHKTDE------MHTALMEAC---MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASL 493
Cdd:PTZ00322   62 ATPDHNLTTEEvidpvvAHMLTVELCqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
                          90       100
                  ....*....|....*....|....*...
gi 38683816   494 EEVNDEGYTPLMEAAREGHEEMVALLLG 521
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; ...
1478-1547 1.27e-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: 1.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIdKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDK 1547
Cdd:cd22417    4 TVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQF-PDKGDENDDEITITGYEKNAEAAKDAILKIVQELES 72
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1773-2193 1.81e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.17  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1773 PTNATYPMPTAkehypvsspsspsppaqpggvsrNSPLdcgsASPNKVASSSEQEAGSPPVVET----TNTRPPNSSSSS 1848
Cdd:PHA03307   22 PRPPATPGDAA-----------------------DDLL----SGSQGQLVSDSAELAAVTVVAGaaacDRFEPPTGPPPG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1849 GSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAV---PSTAPVTYPMPQTPmGCPQPTPKMETP 1925
Cdd:PHA03307   75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPAsppPSPAPDLSEMLRPV-GSPGPPPAASPP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1926 AIRPPPHGTTAPHKNSASvqnSSVAVLSVNHIKRPHSVPSSVQLPSTLSTqsACQNSVHPANKPIAPNFSAPLPFGPFST 2005
Cdd:PHA03307  154 AAGASPAAVASDAASSRQ---AALPLSSPEETARAPSSPPAEPPPSTPPA--AASPRPPRRSSPISASASSPAPAPGRSA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  2006 LFENSPTSahafwggsvvSSQSTPESMLSGKSSYLPNSDPLHQSDTSK----------APGFRPPLQRPAPSPSGivnmd 2075
Cdd:PHA03307  229 ADDAGASS----------SDSSSSESSGCGWGPENECPLPRPAPITLPtriweasgwnGPSSRPGPASSSSSPRE----- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  2076 sPYGSVTPSSTHLGNFASNISggqmygpgaplggapAAANFNRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSPA-PS 2154
Cdd:PHA03307  294 -RSPSPSPSSPGSGPAPSSPR---------------ASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSrPP 357
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 38683816  2155 SVPLGSEKPSNVSQDRKVPVPIGTERSARIRQTGTSAPS 2193
Cdd:PHA03307  358 PPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAG 396
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
871-975 1.90e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   871 LAATAGHVGVvEILLDNGADIEAQsERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKI 950
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 38683816   951 LL---------NAGAEINSRTG--SKLGISPLMLAA 975
Cdd:PTZ00322  167 LSrhsqchfelGANAKPDSFTGkpPSLEDSPISSHH 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1087-1154 2.00e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 2.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816  1087 LLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYL 1154
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
975-1064 2.20e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   975 AMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1054
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
                          90
                  ....*....|....*
gi 38683816  1055 -----DKGADVNAPP 1064
Cdd:PTZ00322  169 rhsqcHFELGANAKP 183
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
303-330 2.29e-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: 2.29e-05
                           10        20
                   ....*....|....*....|....*....
gi 38683816    303 TPLMAAA-NGGHVKIVKLLLAHKADVNAQ 330
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
236-489 2.80e-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: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    236 RSLAEACSEGDVNAVRKLLIEGRSVNEHTEE--GESLLCLACSAG-YYELAQVLLamhaNVEDRGIKGDiTPLMAAANGg 312
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLL----NLSCRGAVGD-TLLHAISLE- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    313 HVKIVKLLLAHKADvnAQSSTGNTALTYACAGG--YVDvvkvllesgasiedhnengHTPLMEAGSAGHVEVARLLLENG 390
Cdd:TIGR00870   93 YVDAVEAILLHLLA--AFRKSGPLELANDQYTSefTPG-------------------ITALHLAAHRQNYEIVKLLLERG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    391 AGINT--HSNEFKESALT---------LACYK--GHLEMVRFLLEAGADQEhKTDEM-----HTALMEA----------- 441
Cdd:TIGR00870  152 ASVPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelsc 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 38683816    442 -CMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 489
Cdd:TIGR00870  231 qMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
417-486 3.01e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 3.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   417 VRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALL 486
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 ...
1478-1538 3.15e-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: 3.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683816 1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1538
Cdd:cd22435    5 KLLVPNYAAGSIIGKGGQTIAQLQKETGARIKLSKNNDfypGTTERVCLIQGEVEAVNAVLDFI 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
1635-2088 3.42e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 3.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1635 PPPQFAHALLAAQTFQQIRPPRL------PMTHFGGTFP--PAQSTWGPFPVRPLSPARAT---NSPKPHMVPRHSNQNS 1703
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRPaprpsePAVTSRARRPdaPPQSARPRAPVDDRGDPRGPappSPLPPDTHAPDPPPPS 2630
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1704 SGSQVNSAGSLTSSPTTttsssastvPGTSTNGSPSSPSVRRQLFVTVVKTSNATTTTVTTTASNNNTAP----TNATYP 1779
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVP---------PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgslTSLADP 2701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1780 MPTAKEHYPVSSPSSPSPPAQPGgvsrnsPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSSAHsnqqq 1859
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPG------PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA----- 2770
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1860 PPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPV-TYPMPQTPMGcPQPTPKMETPAIRPPPHGTTAPh 1938
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAaALPPAASPAG-PLPPPTSAQPTAPPPPPGPPPP- 2848
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1939 knSASVQNSSVAVLSVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIA--PNFSAPLPFGPFSTLFENSPTSAHA 2016
Cdd:PHA03247 2849 --SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAlpPDQPERPPQPQAPPPPQPQPQPPPP 2926
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  2017 FWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDT---------------SKAPGFRPPLQRPAPSPSGIVNMDSPYGSV 2081
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgalvpgrvavprFRVPQPAPSREAPASSTPPLTGHSLSRVSS 3006

                  ....*..
gi 38683816  2082 TPSSTHL 2088
Cdd:PHA03247 3007 WASSLAL 3013
Ank_5 pfam13857
Ankyrin repeats (many copies);
559-604 3.46e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 3.46e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 38683816    559 DIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYA 604
Cdd:pfam13857   11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
967-995 4.58e-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: 4.58e-05
                           10        20
                   ....*....|....*....|....*....
gi 38683816    967 GISPLMLAAMNGHTAAVKLLLDMGSDINA 995
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
341-494 4.86e-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: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    341 ACAGGYVDVVKVLLESGAS--IEDHNENGHTPLMEAGSAG-HVEVARLLLENGAGINThsnefKESALTLAC--YKGHLE 415
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV-----GDTLLHAISleYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    416 MVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ESP 470
Cdd:TIGR00870   99 AILLHLLAAFRKsgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgESP 178
                          170       180
                   ....*....|....*....|....
gi 38683816    471 LTLAACGGHVELAALLIERGASLE 494
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, ...
1476-1544 4.94e-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: 4.94e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIR-EFTGAHIDIDKQKDKtgdriITIRGGTESTRQATQLINALIKD 1544
Cdd:cd22409    3 VAEVSAPSWLHRFIIGKKGANIKKITqDLPKVHIEFTEGEDK-----IELEGPPEEVEVVREQLEAIVKE 67
Ank_4 pfam13637
Ankyrin repeats (many copies);
1001-1054 5.07e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 5.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683816   1001 RNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1054
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
326-520 5.24e-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: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  326 DVNAQSSTGNTALTYAC---AGGYVDVVKVLLESG-----------ASIEDHNENGHTPLMEAGSAGHVEVARLLLENGA 391
Cdd:cd21882   18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAApdsgnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  392 GINTHSN------------EFKESALTLACYKGHLEMVRFLLEAGAD--QEHKTDEMHTALMEACmdghVEVARLLLDSG 457
Cdd:cd21882   98 DVSARATgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQpaALEAQDSLGNTVLHAL----VLQADNTPENS 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683816  458 AQVnmpADSFESPLTLAACGGHVElaalliergaSLEEV-NDEGYTPLMEAAREGHEEMVALLL 520
Cdd:cd21882  174 AFV---CQMYNLLLSYGAHLDPTQ----------QLEEIpNHQGLTPLKLAAVEGKIVMFQHIL 224
PHA02859 PHA02859
ankyrin repeat protein; Provisional
314-428 5.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.74  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   314 VKIVKLLLAHKADVNAQSSTGNTAL--TYACAGGYV--DVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLL 386
Cdd:PHA02859   66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV-RINVIKLL 144
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 38683816   387 LENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQE 428
Cdd:PHA02859  145 IDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDIN 186
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
864-894 5.42e-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: 42.28  E-value: 5.42e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 38683816    864 KGFTPLILAAT-AGHVGVVEILLDNGADIEAQ 894
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1490-1538 5.43e-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: 5.43e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 38683816 1490 IGRGGCNINAIREFTGAHIDIDKQKDKTGDrIITIRGGTESTRQATQLI 1538
Cdd:cd22413   18 IGRGGANIRKIRDNTGARIIFPTARDEDQE-LITIIGTKEAVEKAKEEL 65
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
1478-1542 5.57e-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: 5.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816 1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22454    7 EVVIPNADVGKVIGKGGETIKRIEALTDTVITFERVNGGSPNREVQITGSPDNVAAAKRLIEDTI 71
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
566-594 6.16e-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: 6.16e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683816    566 TPLMEAA-QEGHLELVKYLLAAGANVHATT 594
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
630-660 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 38683816    630 GRTPLMKAA-RAGHVCTVQFLISKGANVNRTT 660
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
565-651 6.25e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   565 STPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVC 644
Cdd:PTZ00322   83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                  ....*..
gi 38683816   645 TVQFLIS 651
Cdd:PTZ00322  163 VVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
967-995 7.32e-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: 7.32e-05
                            10        20
                    ....*....|....*....|....*....
gi 38683816     967 GISPLMLAAMNGHTAAVKLLLDMGSDINA 995
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 ...
1476-1542 9.23e-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: 9.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22479    2 TEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGSPEAVQKAKMMLDDIV 68
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
499-528 1.05e-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: 1.05e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683816    499 EGYTPLMEAAREGHEEMVALLLGQGANINA 528
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_MER1_like cd22458
type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic ...
1477-1538 1.11e-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: 1.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816 1477 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTgDRIITIRGGTESTRQATQLI 1538
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 ...
1479-1542 1.25e-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: 1.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683816 1479 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD--KTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22463    6 FQIPEAVVGLIIGKSGNTIKQISERSGAFVAIVQDRYplEETQKILRISGTEEQLKRAQSLVEGLI 71
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
366-394 1.26e-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: 1.26e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683816    366 NGHTPLMEA-GSAGHVEVARLLLENGAGIN 394
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVN 30
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
1891-2089 1.30e-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: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1891 TSSAPVAVPSTaPVTYPMPQTPMGCPQPTPKMETPAIRPPPHGTTAPHKNSASVQNSsvavLSVNHIKRPHSVPSSvqlP 1970
Cdd:pfam08580  491 PSKIPRASPNH-SGFLSTPSNTATSETPTPALRPPSRPQPPPPGNRPRWNASTNTND----LDVGHNFKPLTLTTP---S 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1971 STLSTQSACQNSVHPANKPIAPNFSAPLPFGPFSTLFENSPTSAHAfwggSVVSSQSTPESMLsgkssylpNSDPLHQSD 2050
Cdd:pfam08580  563 PTPSRSSRSSSTLPPVSPLSRDKSRSPAPTCRSVSRASRRRASRKP----TRIGSPNSRTSLL--------DEPPYPKLT 630
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 38683816   2051 TSKAPGfRPPLQRP---APSPSGIVNMDSPYGSVTPSSTHLG 2089
Cdd:pfam08580  631 LSKGLP-RTPRNRQsyaGTSPSRSVSVSSGLGPQTRPGTSLG 671
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
864-893 1.31e-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: 1.31e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 38683816     864 KGFTPLILAATAGHVGVVEILLDNGADIEA 893
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
566-592 1.36e-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: 1.36e-04
                            10        20
                    ....*....|....*....|....*..
gi 38683816     566 TPLMEAAQEGHLELVKYLLAAGANVHA 592
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
880-1010 1.42e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   880 VVEILLDNGADIEAQsERTKDTPLSLACSGGRQ-----EVVELLLARGANKEHRNVSDYTPLSLAASGGYVN---IIKIL 951
Cdd:PHA02798   53 IVKLFINLGANVNGL-DNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINnleILLFM 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816   952 LNAGAEINSRtgSKLGISPLMLAAMNGHTA---AVKLLLDMGSDINaqIETNRNTALTLACF 1010
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 ...
630-657 1.53e-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: 1.53e-04
                            10        20
                    ....*....|....*....|....*...
gi 38683816     630 GRTPLMKAARAGHVCTVQFLISKGANVN 657
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 ...
1479-1534 1.64e-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: 1.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816 1479 VSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTGDRIITIRGGTESTRQA 1534
Cdd:cd22403    4 IRVPSSMVGRIIGKGGQNVRELQRLTGAIIKLprDQTPDEGDEVPVEIIGNFYATQSA 61
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
348-522 1.67e-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: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  348 DVVKVLLEsgASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGIN----------THSNE---FKESALTLACYKGHL 414
Cdd:cd22194  124 GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEgfyFGETPLALAACTNQP 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  415 EMVRFLLEAGADQEHKTDEMHTALMEACmdghVEVARlllDSGAQVNMPADSFESPLTlaACGGHvelaalliergaSLE 494
Cdd:cd22194  202 EIVQLLMEKESTDITSQDSRGNTVLHAL----VTVAE---DSKTQNDFVKRMYDMILL--KSENK------------NLE 260
                        170       180
                 ....*....|....*....|....*....
gi 38683816  495 EV-NDEGYTPLMEAAREGHEEMVALLLGQ 522
Cdd:cd22194  261 TIrNNEGLTPLQLAAKMGKAEILKYILSR 289
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
597-624 1.81e-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: 1.81e-04
                            10        20
                    ....*....|....*....|....*...
gi 38683816     597 GDTALTYACENGHTDVADVLLQAGADLE 624
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
486-541 1.82e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 1.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816    486 LIERG-ASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETqETALTLA 541
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
334-362 1.82e-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: 1.82e-04
                            10        20
                    ....*....|....*....|....*....
gi 38683816     334 GNTALTYACAGGYVDVVKVLLESGASIED 362
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
824-953 2.32e-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: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  824 IDAQ-TESNHD--TALTLACAGGHEELVQTLLERGASIEHRDKKGF--------------TPLILAATAGHVGVVEILLD 886
Cdd:cd22194  130 INAEyTEEAYEgqTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLME 209
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816  887 NGADIEAQSERTKDTPL---------SLACSGGRQEVVELLLARGANKE---HRNVSDYTPLSLAASGGYVNIIKILLN 953
Cdd:cd22194  210 KESTDITSQDSRGNTVLhalvtvaedSKTQNDFVKRMYDMILLKSENKNletIRNNEGLTPLQLAAKMGKAEILKYILS 288
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
967-996 2.41e-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: 2.41e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 38683816    967 GISPLMLAA-MNGHTAAVKLLLDMGSDINAQ 996
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1048-1201 2.42e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1048 EVGRVLLDKGADVNAPPVPSSrdtALTIAAdKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGAD 1127
Cdd:PLN03192  508 NVGDLLGDNGGEHDDPNMASN---LLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1128 VDAADNRKITPLMAAFRKGHVKVVRYLvkevNQFPSDS------ECMRYIATITDKEMLKKChLCMESIVQAKDRQAAEA 1201
Cdd:PLN03192  584 VHIRDANGNTALWNAISAKHHKIFRIL----YHFASISdphaagDLLCTAAKRNDLTAMKEL-LKQGLNVDSEDHQGATA 658
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
234-454 2.43e-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: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    234 DNRSLAEACSEGDVNAVRKLLIEgrsVNEHTEEGESLLcLACSAGYY----ELAQVLLAMH--------ANVEDRG-IKG 300
Cdd:TIGR00870   52 GRSALFVAAIENENLELTELLLN---LSCRGAVGDTLL-HAISLEYVdaveAILLHLLAAFrksgplelANDQYTSeFTP 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    301 DITPLMAAANGGHVKIVKLLLAHKADVNA-------QSSTGNTAL--------TYACAGGYvDVVKVLLESGASIEDHNE 365
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFyhgesplnAAACLGSP-SIVALLSEDPADILTADS 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    366 NGHTplmeagsaghveVARLLLENgaginthsNEFKESALTLACykghlEMVRFLLEAGaDQEHKTDEMH--------TA 437
Cdd:TIGR00870  207 LGNT------------LLHLLVME--------NEFKAEYEELSC-----QMYNFALSLL-DKLRDSKELEvilnhqglTP 260
                          250
                   ....*....|....*..
gi 38683816    438 LMEACMDGHVEVARLLL 454
Cdd:TIGR00870  261 LKLAAKEGRIVLFRLKL 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
303-329 2.57e-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: 2.57e-04
                            10        20
                    ....*....|....*....|....*..
gi 38683816     303 TPLMAAANGGHVKIVKLLLAHKADVNA 329
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
271-364 2.69e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   271 LCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVV 350
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90
                  ....*....|....
gi 38683816   351 KVLleSGASIEDHN 364
Cdd:PTZ00322  165 QLL--SRHSQCHFE 176
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
1475-1551 3.07e-04

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 46.15  E-value: 3.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816 1475 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqkDktgDRIITIrGGT--ESTRQATQLINALIKDPdkEIDE 1551
Cdd:COG1185  549 RIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIE---D---DGTVKI-AATdgEAAEKAIERIEGITAEP--EVGE 618
Ank_5 pfam13857
Ankyrin repeats (many copies);
884-939 3.19e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 3.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816    884 LLDNG-ADIEAQsERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLA 939
Cdd:pfam13857    1 LLEHGpIDLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
951-1008 3.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 3.96e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816    951 LLNAGAeINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLA 1008
Cdd:pfam13857    1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK-DEEGLTALDLA 56
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
1475-1551 4.09e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.81  E-value: 4.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816  1475 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDPdkEIDE 1551
Cdd:PRK11824  554 RIETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIED------DGTVKIAATDgEAAEAAKERIEGITAEP--EVGE 623
PHA02946 PHA02946
ankyin-like protein; Provisional
842-1038 4.11e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   842 GGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKdTPLSLaCSGGRQEVVE---LL 918
Cdd:PHA02946   49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHK-TPLYY-LSGTDDEVIErinLL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   919 LARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEinSRTGSKLGISPL--MLAAMNGHTAAVKLLLDMGSDiNAQ 996
Cdd:PHA02946  127 VQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFE--ARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGIS-PSK 203
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 38683816   997 IETNRNTALTLACFQ--GRTEVVSLLLDrKANVEHRAKTGLTPL 1038
Cdd:PHA02946  204 PDHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPL 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
1095-1139 4.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 4.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 38683816   1095 IDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1139
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02884 PHA02884
ankyrin repeat protein; Provisional
346-443 4.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.59  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   346 YVDVVKVLLESGASIE---DHNENGHT-PLMEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLL 421
Cdd:PHA02884   45 YTDIIDAILKLGADPEapfPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
                          90       100
                  ....*....|....*....|..
gi 38683816   422 EAGADQEHKTDEMHTALMEACM 443
Cdd:PHA02884  125 SYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
630-657 4.73e-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: 4.73e-04
                           10        20
                   ....*....|....*....|....*...
gi 38683816    630 GRTPLMKAARAGHVCTVQFLISKGANVN 657
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
536-584 5.06e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 5.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683816    536 TALTLACCGGFLEVADFLIKAGADI---ELGCSTPLMEAAQEGHLELVKYLL 584
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADInavDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1101-1130 6.23e-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: 6.23e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683816   1101 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1130
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
515-725 6.87e-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: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  515 MVALLlgqgaNINAQTEETQETALTLACCGGFLEVadfLIKAGADIE-LGCSTPLMEAAQEGHLELVKYLLAAGANVHAt 593
Cdd:cd22194   99 MKALL-----NINENTKEIVRILLAFAEENGILDR---FINAEYTEEaYEGQTALNIAIERRQGDIVKLLIAKGADVNA- 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  594 TATGdtaltyacenghtdvadVLLQAgadlEHESEG---GRTPLMKAAraghvCT-----VQFLISKGANVNRTTANNDH 665
Cdd:cd22194  170 HAKG-----------------VFFNP----KYKHEGfyfGETPLALAA-----CTnqpeiVQLLMEKESTDITSQDSRGN 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816  666 TVL-SLACAG----GHLAVV-----ELLLAHGAD--PTHRLKDGSTMLIEAAKGGHTSVVCYLL-----DYPNNLLS 725
Cdd:cd22194  224 TVLhALVTVAedskTQNDFVkrmydMILLKSENKnlETIRNNEGLTPLQLAAKMGKAEILKYILsreikEKPNRSLS 300
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
435-462 7.65e-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: 7.65e-04
                            10        20
                    ....*....|....*....|....*...
gi 38683816     435 HTALMEACMDGHVEVARLLLDSGAQVNM 462
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
366-394 8.19e-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: 8.19e-04
                            10        20
                    ....*....|....*....|....*....
gi 38683816     366 NGHTPLMEAGSAGHVEVARLLLENGAGIN 394
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 ...
1479-1543 9.62e-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: 9.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816 1479 VSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTGDRIITIRGGTESTRQATQLINALIK 1543
Cdd:cd22500    6 IKVPSSAAGRVIGKGGKTVNELQNLTSAEVIVprDQTPDENEEVIVKIIGHFFASQTAQRKIREIVQ 72
Ank_5 pfam13857
Ankyrin repeats (many copies);
1019-1076 1.00e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816   1019 LLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIA 1076
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK--DEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
831-859 1.17e-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: 1.17e-03
                            10        20
                    ....*....|....*....|....*....
gi 38683816     831 NHDTALTLACAGGHEELVQTLLERGASIE 859
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1860-1992 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 38683816  1860 PPGSVSQEPRPPLQQSQVPPPevrmtVPPLATSSAPVAVPSTAPVTYPMPQTPmgcPQPTPKMETPAIRPPPhgttAPHK 1939
Cdd:PRK14951  373 AAPAEKKTPARPEAAAPAAAP-----VAQAAAAPAPAAAPAAAASAPAAPPAA---APPAPVAAPAAAAPAA----APAA 440
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 38683816  1940 NSASVQNSSVAvlSVNHIKRPHSVPSSVQlPSTLSTQSACQNSVHPANKPIAP 1992
Cdd:PRK14951  441 APAAVALAPAP--PAQAAPETVAIPVRVA-PEPAVASAAPAPAAAPAAARLTP 490
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
833-980 1.17e-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: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  833 DTALTLACAGGHEELVQTLLERGAS-----IEHRDKKGFTPLILAATAGHVGVVEILLDNGADIeaQSERTKDT------ 901
Cdd:cd22192   52 ETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLVRELIARGADV--VSPRATGTffrpgp 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  902 ---------PLSLACSGGRQEVVELLLARGANKEHRNVSDYTP---LSLAASGGYV-NIIKILLNAGAEINSRTGSKL-- 966
Cdd:cd22192  130 knliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVlhiLVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVpn 209
                        170
                 ....*....|....*.
gi 38683816  967 --GISPLMLAAMNGHT 980
Cdd:cd22192  210 nqGLTPFKLAAKEGNI 225
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1874-2068 1.32e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.31  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1874 QSQVPPPEVRMTVPPLATSSAPVAVPSTAPVTYPMPQTPmgcpqptpkmeTPAIRPPPHGTTaPHKNSASVQNSSVAvls 1953
Cdd:PRK10263  331 QSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTG-----------EPVIAPAPEGYP-QQSQYAQPAVQYNE--- 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1954 vnHIKRPHSVPSSVQLPSTLSTQSACQNSVHPAnKPIAPNFSAPLPFGPfstlfensptSAHAFWGGSVVSSQSTPESML 2033
Cdd:PRK10263  396 --PLQQPVQPQQPYYAPAAEQPAQQPYYAPAPE-QPAQQPYYAPAPEQP----------VAGNAWQAEEQQSTFAPQSTY 462
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 38683816  2034 SGKSSYLpnsDPLHQSDTSKAPGFRPPLQRPAPSP 2068
Cdd:PRK10263  463 QTEQTYQ---QPAAQEPLYQQPQPVEQQPVVEPEP 494
KH-I_Rnc1_rpt1 cd22455
first type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
1489-1538 1.32e-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: 1.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 38683816 1489 VIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLI 1538
Cdd:cd22455   15 IIGKGGENIARLRATTGVKAGVSKVVPGVHDRVLTVSGPLEGVAKAFGLI 64
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
932-959 1.33e-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: 1.33e-03
                            10        20
                    ....*....|....*....|....*...
gi 38683816     932 DYTPLSLAASGGYVNIIKILLNAGAEIN 959
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
836-1024 1.36e-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: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    836 LTLACAGGHEELVQTLLERGASIEHRDKkgftpLILAATAGHVGVVE----ILLDNGADI--------EAQSERTKD-TP 902
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDAVEaillHLLAAFRKSgplelandQYTSEFTPGiTA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    903 LSLACSGGRQEVVELLLARGAN------------KEHRNVSDYT--PLSLAASGGYVNIIKILLNAGAEInsRTGSKLGI 968
Cdd:TIGR00870  132 LHLAAHRQNYEIVKLLLERGASvparacgdffvkSQGVDSFYHGesPLNAAACLGSPSIVALLSEDPADI--LTADSLGN 209
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683816    969 SPLMLAAMNGHTAAV---------KLLLDMG--SDINAQIE--TNRN--TALTLACFQGRTEVVSLLLDRK 1024
Cdd:TIGR00870  210 TLLHLLVMENEFKAEyeelscqmyNFALSLLdkLRDSKELEviLNHQglTPLKLAAKEGRIVLFRLKLAIK 280
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
831-863 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 38683816    831 NHDTALTLACA-GGHEELVQTLLERGASIEHRDK 863
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
365-584 1.45e-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: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  365 ENGHTPLMEAgsaghvevarlLLEngagINTHSNEFKESALTLACYKGHLEmvRFLleaGADQEHKTDEMHTALMEACMD 444
Cdd:cd22194   92 DTGKTCLMKA-----------LLN----INENTKEIVRILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIER 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  445 GHVEVARLLLDSGAQVNMPA-----------DSF---ESPLTLAACGGHVELAALLIERGAsleevndegyTPLMEAARE 510
Cdd:cd22194  152 RQGDIVKLLIAKGADVNAHAkgvffnpkykhEGFyfgETPLALAACTNQPEIVQLLMEKES----------TDITSQDSR 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  511 GHEEMVALLlgqganINAQTEETQETALTlaccggflEVADFLIKAGADIELGCS------TPLMEAAQEGHLELVKYLL 584
Cdd:cd22194  222 GNTVLHALV------TVAEDSKTQNDFVK--------RMYDMILLKSENKNLETIrnneglTPLQLAAKMGKAEILKYIL 287
Ank_5 pfam13857
Ankyrin repeats (many copies);
917-974 1.45e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816    917 LLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLA 974
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE--GLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
846-959 1.79e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   846 ELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL---DNGADIEAQSERTKdTPLSLACSGGRQ---EVVELLL 919
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGF-TMLQVYLQSNHHidiEIIKLLL 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 38683816   920 ARGAN-KEHRNVSDYTPLSLAASGGY----VNIIKILLNAGAEIN 959
Cdd:PHA02798  169 EKGVDiNTHNNKEKYDTLHCYFKYNIdridADILKLFVDNGFIIN 213
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
834-885 1.80e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 1.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 38683816   834 TALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL 885
Cdd:PTZ00322  117 TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
616-671 1.90e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816    616 LLQAG-ADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDhTVLSLA 671
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
597-625 1.99e-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: 1.99e-03
                           10        20
                   ....*....|....*....|....*....
gi 38683816    597 GDTALTYACENGHTDVADVLLQAGADLEH 625
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
869-1123 1.99e-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: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    869 LILAATAGHVGVVEILLDNGADIEAQS-ERTKDTPLSLACSGGR-QEVVELLLarganKEHRNVSDYTPLSLAASGGYVN 946
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEPKKLNINCpDRLGRSALFVAAIENEnLELTELLL-----NLSCRGAVGDTLLHAISLEYVD 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816    947 ----IIKILLNAGAE------INSRTGSKL--GISPLMLAAMNGHTAAVKLLLDMGSDINAQietnrntaltlAC---FQ 1011
Cdd:TIGR00870   96 aveaILLHLLAAFRKsgplelANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPAR-----------ACgdfFV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1012 GRTEVVSLLLDRkanvehraktglTPLMEAASGGYAEVGRVLLDKGADVNAppvpssRDT-------ALTIAAD-KGHYK 1083
Cdd:TIGR00870  165 KSQGVDSFYHGE------------SPLNAAACLGSPSIVALLSEDPADILT------ADSlgntllhLLVMENEfKAEYE 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683816   1084 F----C-ELLIGRGAHID-------VRNKKGNTPLWLAANGGHLDVVQLLVQ 1123
Cdd:TIGR00870  227 ElscqMyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLA 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
350-421 2.27e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 2.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683816   350 VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKeSALTLACYKGHLEMVRFLL 421
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLS 168
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
891-1119 2.33e-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: 43.21  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  891 IEAQSERTKDTPLSL--ACSGGRQEVVELLlargANKEHRN-------VSDYTPLSLAASG-GYVNIIKILLNagaeINS 960
Cdd:cd22194   36 AELAKEEQRDKKKRLkkVSEAAVEELGELL----KELKDLSrrrrktdVPDFLMHKLTASDtGKTCLMKALLN----INE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  961 RTGSklgISPLMLAAMNGHTAAVKLlldmgsdINAQIeTNRN----TALTLACFQGRTEVVSLLLDRKANVEHRAKT--- 1033
Cdd:cd22194  108 NTKE---IVRILLAFAEENGILDRF-------INAEY-TEEAyegqTALNIAIERRQGDIVKLLIAKGADVNAHAKGvff 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1034 -----------GLTPLMEAASGGYAEVGRVLLDKGADVNappvpSSRDT-------ALTIAAD--KGHYKFCE------L 1087
Cdd:cd22194  177 npkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDI-----TSQDSrgntvlhALVTVAEdsKTQNDFVKrmydmiL 251
                        250       260       270
                 ....*....|....*....|....*....|...
gi 38683816 1088 LIGRGAHID-VRNKKGNTPLWLAANGGHLDVVQ 1119
Cdd:cd22194  252 LKSENKNLEtIRNNEGLTPLQLAAKMGKAEILK 284
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
436-652 2.36e-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: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  436 TALMEACM---DGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAaLLIERgasleevndegytplmeaaREGH 512
Cdd:cd22193   31 TCLMKALLnlnPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEGQTALH-IAIER-------------------RQGD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  513 eeMVALLLGQGANINAQTeetqetaltlacCGGFLEVADflikAGADIELGcSTPLMEAAQEGHLELVKYLLA---AGAN 589
Cdd:cd22193   91 --IVALLVENGADVHAHA------------KGRFFQPKY----QGEGFYFG-ELPLSLAACTNQPDIVQYLLEnehQPAD 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816  590 VHATTATGDT---ALTYACENGHTDVA------DVLLQAGADLEHESE-------GGRTPLMKAARAGHVCTVQFLISK 652
Cdd:cd22193  152 IEAQDSRGNTvlhALVTVADNTKENTKfvtrmyDMILIRGAKLCPTVEleeirnnDGLTPLQLAAKMGKIEILKYILQR 230
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1773-2099 2.45e-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: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1773 PTNATYPMPTAkehypVSSPSSPSPPAQPGGVSRNSPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSS 1852
Cdd:pfam05109  455 PTNLTAPASTG-----PTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTT 529
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1853 AHSNQQQP------PGSVSQEPRP----PLQQSQVPPPEVrmTVPPLATSSAPVAVPSTAP-VTYPM-----PQTPMGCP 1916
Cdd:pfam05109  530 PTPNATSPtlgktsPTSAVTTPTPnatsPTPAVTTPTPNA--TIPTLGKTSPTSAVTTPTPnATSPTvgetsPQANTTNH 607
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1917 QPTPKMETPAI-RPPPHGTTAPHKNSASVQNSSVAVLSVnhikRPHSVPSSVQlPSTLSTQSACQNSVHPANKPIAPNFS 1995
Cdd:pfam05109  608 TLGGTSSTPVVtSPPKNATSAVTTGQHNITSSSTSSMSL----RPSSISETLS-PSTSDNSTSHMPLLTSAHPTGGENIT 682
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   1996 APLPfgpfstlfenSPTSAHafwggSVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFRPPLQRPAP-SPSGivnm 2074
Cdd:pfam05109  683 QVTP----------ASTSTH-----HVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPqAPSG---- 743
                          330       340
                   ....*....|....*....|....*
gi 38683816   2075 dspYGSVTPSSTHLGNFASNISGGQ 2099
Cdd:pfam05109  744 ---QKTAVPTVTSTGGKANSTTGGK 765
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
834-952 2.56e-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: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  834 TALTLACAGGHEELVQTLLERGASIEHRDKKGF-------------TPLILAATAGHVGVVEILLDNGADIEAQSER--- 897
Cdd:cd21882   75 TALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGAQPAALEAQdsl 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816  898 -----------TKDTP--LSLACSggrqeVVELLLARGANKEH-------RNVSDYTPLSLAASGGYVNIIKILL 952
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 ...
1481-1538 2.57e-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: 2.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 38683816 1481 VPSTVISRVIGRGGCNINAIREFTGAHIDI-DKQKDKTGDRIITIRGGTESTRQATQLI 1538
Cdd:cd22402    7 IPNKAVGAIIGTKGSHIRYIKRFSGASIKIaPADSPDAPERKVTITGPPEAQWKAQLCI 65
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
303-329 2.72e-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: 2.72e-03
                           10        20
                   ....*....|....*....|....*..
gi 38683816    303 TPLMAAANGGHVKIVKLLLAHKADVNA 329
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
398-527 3.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.34  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   398 NEFKESALtLACY---KGHLEMVRFLLEAGADQEHKTDEMHTALMEACM----DGHVEVARLLLDSGAQVNMPADSFESP 470
Cdd:PHA02859   48 NDLYETPI-FSCLekdKVNVEILKFLIENGADVNFKTRDNNLSALHHYLsfnkNVEPEILKILIDSGSSITEEDEDGKNL 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816   471 L--TLAACGGHVELAALLIERGASLEEVNDEG----YTPLMeaaREGHEEMVALLLGQGANIN 527
Cdd:PHA02859  127 LhmYMCNFNVRINVIKLLIDSGVSFLNKDFDNnnilYSYIL---FHSDKKIFDFLTSLGIDIN 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
403-426 3.18e-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: 3.18e-03
                            10        20
                    ....*....|....*....|....
gi 38683816     403 SALTLACYKGHLEMVRFLLEAGAD 426
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 ...
1476-1542 3.33e-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: 3.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22480    2 TEEYKVPDKMVGFIIGRGGEQISRIQLESGCKIQIAPDSGGMPERPCVLTGTPESIEQAKRLLGQIV 68
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
334-365 3.75e-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: 3.75e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 38683816    334 GNTALTYACA-GGYVDVVKVLLESGASIEDHNE 365
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; ...
1479-1538 4.05e-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: 4.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1479 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLI 1538
Cdd:cd22408    4 VEVPKSQHRFVIGPRGSTIQEILEETGCSVEV--PPNDSDSETITLRGPADKLGAALTLV 61
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1034-1062 4.26e-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: 4.26e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683816   1034 GLTPLMEAA-SGGYAEVGRVLLDKGADVNA 1062
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
1909-2077 4.52e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 42.28  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1909 PQTPMGCPQPTPKMETPAIRPPPHgtTAPHKNSAS--------VQNSSVAVLSVNHIKRPHSVPSSVQLPSTLSTQS--- 1977
Cdd:PRK12727   60 SDTPATAAAPAPAPQAPTKPAAPV--HAPLKLSANanmsqrqrVASAAEDMIAAMALRQPVSVPRQAPAAAPVRAASips 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1978 -ACQNSVHPANKPIAPNFSAPLPFGPfSTLFENSPTSA----HAFWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDts 2052
Cdd:PRK12727  138 pAAQALAHAAAVRTAPRQEHALSAVP-EQLFADFLTTApvprAPVQAPVVAAPAPVPAIAAALAAHAAYAQDDDEQLD-- 214
                         170       180       190
                  ....*....|....*....|....*....|
gi 38683816  2053 kAPGFR-----PPLQRPAPSPSGIVNMDSP 2077
Cdd:PRK12727  215 -DDGFDlddalPQILPPAALPPIVVAPAAP 243
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
845-987 4.56e-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: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  845 EELVQTLLERG-----------ASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERT-------------KD 900
Cdd:cd22194  110 KEIVRILLAFAeengildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfGE 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  901 TPLSLACSGGRQEVVELLL-----------ARGANKEHR--NVSDytplslaASGGYVNIIK-----ILLNAGAEINSRT 962
Cdd:cd22194  190 TPLALAACTNQPEIVQLLMekestditsqdSRGNTVLHAlvTVAE-------DSKTQNDFVKrmydmILLKSENKNLETI 262
                        170       180
                 ....*....|....*....|....*
gi 38683816  963 GSKLGISPLMLAAMNGHTAAVKLLL 987
Cdd:cd22194  263 RNNEGLTPLQLAAKMGKAEILKYIL 287
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
934-1069 4.89e-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: 4.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  934 TPLSLAASGGYVNIIKILLNAGAEINSR-----------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNR- 1001
Cdd:cd21882   75 TALHIAIENRNLNLVRLLVENGADVSARatgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSl 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1002 -NTALTLACFQGR---------TEVVSLLLDRKANVEHRAK-------TGLTPLMEAASGGYAEVGRVLLDKgaDVNAPP 1064
Cdd:cd21882  155 gNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQR--EFSGPY 232

                 ....*
gi 38683816 1065 VPSSR 1069
Cdd:cd21882  233 QPLSR 237
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
913-1057 4.92e-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: 4.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  913 EVVELLLA---------RGANKEHRNvSDY---TPLSLAASGGYVNIIKILLNAGAEINSRT------------GSKLGI 968
Cdd:cd22194  111 EIVRILLAfaeengildRFINAEYTE-EAYegqTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykheGFYFGE 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  969 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNT---ALTLAC--FQGRTEVVSLLLD------RKANVEH-RAKTGLT 1036
Cdd:cd22194  190 TPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTvlhALVTVAedSKTQNDFVKRMYDmillksENKNLETiRNNEGLT 269
                        170       180
                 ....*....|....*....|....*.
gi 38683816 1037 PLMEAASGGYAEV-----GRVLLDKG 1057
Cdd:cd22194  270 PLQLAAKMGKAEIlkyilSREIKEKP 295
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
1474-1508 5.07e-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: 5.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 38683816 1474 RRSKKVSVPSTVISRVIGRGGCNINAIREFTGAHI 1508
Cdd:cd22421    2 RVTLKMDVSHTDHSHVIGKGGNNIKKVMEDTGCHI 36
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
566-592 5.26e-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: 5.26e-03
                           10        20
                   ....*....|....*....|....*..
gi 38683816    566 TPLMEAAQEGHLELVKYLLAAGANVHA 592
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_PEPPER_like_rpt3 cd22461
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1476-1542 5.63e-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: 5.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22461    3 SQQMQIPLSYADAIIGTAGANISYIRRTSGATITIQETRGAPGEMTVEIHGTQSQVQTAQQLIQNFM 69
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
864-893 5.75e-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: 5.75e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683816    864 KGFTPLILAATAGHVGVVEILLDNGADIEA 893
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_AtC3H36_like cd22464
type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana zinc finger CCCH ...
1478-1542 5.78e-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: 5.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683816 1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22464    2 KISVDASLAGAIIGKGGVNSKQICRETGVKLSIRDHERDPNLKNVELEGSFEQIKEASGMVRELI 66
KH-I_PCBP1_2_rpt2 cd22518
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
1478-1538 5.83e-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: 5.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683816 1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTgDRIITIRGGTESTRQATQLI 1538
Cdd:cd22518   10 RLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVagDMLPNST-ERAITIAGIPQSIIECVKQI 71
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
238-323 5.92e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVE--DRGIKgdiTPLMAAANGGHVK 315
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTllDKDGK---TPLELAEENGFRE 162

                  ....*...
gi 38683816   316 IVKLLLAH 323
Cdd:PTZ00322  163 VVQLLSRH 170
KH-I_FUBP3_rpt3 cd22486
third type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1476-1542 6.11e-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: 37.62  E-value: 6.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816 1476 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22486    4 SIEVSVPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGISPERVAQVMGPPDRCQHAAHIINELI 70
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
1807-1942 6.17e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.68  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1807 NSPLDCGSASPnkvaSSSEQEAGSPPVVETTNTRPPNSSSssgsssahsNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTV 1886
Cdd:PRK14971  361 QLTQKGDDASG----GRGPKQHIKPVFTQPAAAPQPSAAA---------AASPSPSQSSAAAQPSAPQSATQPAGTPPTV 427
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 38683816  1887 PPLATSSAPVAVPSTAPVTYPMPQTPMgcPQPTPKMETPAIRPPphgTTAPHKNSA 1942
Cdd:PRK14971  428 SVDPPAAVPVNPPSTAPQAVRPAQFKE--EKKIPVSKVSSLGPS---TLRPIQEKA 478
Ank_5 pfam13857
Ankyrin repeats (many copies);
1053-1109 6.18e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 6.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683816   1053 LLDKG-ADVNAPPvpSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLA 1109
Cdd:pfam13857    1 LLEHGpIDLNRLD--GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
KH-I_PCBP4_rpt2 cd22520
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
1478-1542 6.30e-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: 6.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816 1478 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTgDRIITIRGGTESTRQATQLINALI 1542
Cdd:cd22520    5 RLVIPASQCGSLIGKAGSKIKEIRESTGAQVQVagDLLPNST-ERAVTVSGVPDAIIQCVRQICAVI 70
PHA02798 PHA02798
ankyrin-like protein; Provisional
380-538 6.35e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   380 VEVARLLLENGAGINTHSNEFKESALTLAC----YKGHLEMVRFLLEAGADQEHKTDEMHTALMeaCMdghvevarllLD 455
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdYKHMLDIVKILIENGADINKKNSDGETPLY--CL----------LS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   456 SGAQVNMpadsfespltlaacgghvELAALLIERGASLEEVNDEGYTPLMEAAREGHE---EMVALLLGQGANINAQTEE 532
Cdd:PHA02798  119 NGYINNL------------------EILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNK 180

                  ....*.
gi 38683816   533 TQETAL 538
Cdd:PHA02798  181 EKYDTL 186
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
435-461 6.38e-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: 6.38e-03
                           10        20
                   ....*....|....*....|....*...
gi 38683816    435 HTALMEAC-MDGHVEVARLLLDSGAQVN 461
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
609-715 6.57e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.12  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816   609 HTDVADVLLQAGADLEHE---SEGGRT-PLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLL 684
Cdd:PHA02884   45 YTDIIDAILKLGADPEAPfplSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
                          90       100       110
                  ....*....|....*....|....*....|.
gi 38683816   685 AHGADPTHRLKDGSTMlIEAAkgghtSVVCY 715
Cdd:PHA02884  125 SYGADINIQTNDMVTP-IELA-----LMICN 149
PHA02798 PHA02798
ankyrin-like protein; Provisional
1051-1160 6.97e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816  1051 RVLLDKGADVNAppVPSSRDTAL-TIAADKGHYK----FCELLIGRGAHIDVRNKKGNTPLW-LAANG--GHLDVVQLLV 1122
Cdd:PHA02798   55 KLFINLGANVNG--LDNEYSTPLcTILSNIKDYKhmldIVKILIENGADINKKNSDGETPLYcLLSNGyiNNLEILLFMI 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 38683816  1123 QAGADVDAADNRKITPLMAAFRKGH---VKVVRYLVK---EVNQ 1160
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEkgvDINT 176
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
436-462 7.21e-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: 7.21e-03
                           10        20
                   ....*....|....*....|....*..
gi 38683816    436 TALMEACMDGHVEVARLLLDSGAQVNM 462
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
420-474 7.83e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 7.83e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 38683816    420 LLEAG-ADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLA 474
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
353-408 8.47e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 8.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 38683816    353 LLESG-ASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINThSNEFKESALTLA 408
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
SCS2 COG5066
VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and ...
1825-1931 9.05e-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: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683816 1825 EQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPV 1904
Cdd:COG5066  121 SEEEISKNVHECSEDRGAAVLLVEMPTLLNILYLEVRFFVNQKEVPAEPETQPPVQVKKEEVPPVTQKTVPHENEKQTSV 200
                         90       100
                 ....*....|....*....|....*..
gi 38683816 1905 TYPMPQTPMGCPQPTPKmETPAIRPPP 1931
Cdd:COG5066  201 STPKPQNQIKEAATVPA-ENEPSSMPI 226
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
597-623 9.74e-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: 9.74e-03
                           10        20
                   ....*....|....*....|....*...
gi 38683816    597 GDTALTYACE-NGHTDVADVLLQAGADL 623
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH