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Conserved domains on  [gi|1953314652|ref|XP_038513803|]
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ankyrin repeat and KH domain-containing protein 1 isoform X1 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
280-567 9.61e-57

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.41  E-value: 9.61e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  280 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 359
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  360 NThSNEFKESALTLACYKGHLDMVRFLLDAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 439
Cdd:COG0666     81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  440 AACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFL 519
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1953314652  520 IKAGADIELGC---STPLMEASQEGHLELVKYLLAAGANVHATTATGDTAL 567
Cdd:COG0666    239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1083-1376 2.48e-55

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.56  E-value: 2.48e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1083 ELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTKDTPLSLACSGGRQEVVDLLLARGANK 1162
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1163 EHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQiETNRNTAL 1242
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1243 TLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFC 1322
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIV 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1323 ELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPL 1376
Cdd:COG0666    236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
KH-I_ANKHD1 cd22503
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ...
 1713-1795 1.22e-49

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: 171.08  E-value: 1.22e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1713 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIP 1792
Cdd:cd22503      1 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIP 80


                   ...
gi 1953314652 1793 KNH 1795
Cdd:cd22503     81 RNH 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
139-404 4.36e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 4.36e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  139 ARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAENSHNAGQVDTRSLAEACSDGDVNAVRK 218
Cdd:COG0666     26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  219 LLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSA 298
Cdd:COG0666    106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  299 TGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKG 378
Cdd:COG0666    185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAG 263

                          250       260
                   ....*....|....*....|....*.
gi 1953314652  379 HLDMVRFLLDAGADQEHKTDEMHTAL 404
Cdd:COG0666    264 AALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
534-643 1.48e-21

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  534 LMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLDKQEDmktilegidpakhqehese 613
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN------------------- 60

                           90       100       110
                   ....*....|....*....|....*....|
gi 1953314652  614 gGRTPLMKAARAGHLCTVQFLISKGANVNR 643
Cdd:pfam12796   61 -GRTALHYAARSGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
619-704 1.15e-14

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 1.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  619 LMKAARAGHLCTVQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTNVV 698
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77


                   ....*.
gi 1953314652  699 SYLLDY 704
Cdd:pfam12796   78 KLLLEK 83
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 1797-2198 1.10e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1797 RTPASTKSIHANfSSGVGTTAASSKNAFPLGAPTlvtsqattlstfQPTNKLTKNVPANVRSSFPVSlPLAYPHPHFALL 1876
Cdd:PHA03247  2625 DPPPPSPSPAAN-EPDPHPPPTVPPPERPRDDPA------------PGRVSRPRRARRLGRAAQASS-PPQRPRRRAARP 2690

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1877 AAQTMQQIRHPRLPmaqfGGTFSPSPNTWG---PFPVRPVNPGNTNSSPKHNNAGRlPNQNGTVLPSESAGLATASCPIT 1953
Cdd:PHA03247  2691 TVGSLTSLADPPPP----PPTPEPAPHALVsatPLPPGPAAARQASPALPAAPAPP-AVPAGPATPGGPARPARPPTTAG 2765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1954 VSSVVAASQQLCV---TNTRTPSSVRKQLFACVPKTSPPATVISSVTSTCSSLPSvSSAPVTSGQVPTTFLPASTPQAQL 2030
Cdd:PHA03247  2766 PPAPAPPAAPAAGpprRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP-AASPAGPLPPPTSAQPTAPPPPPG 2844

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2031 SSQKMESFSAMPPPKEKVSTQDQAMAHLCTPSSTANSCSSSASNTPGAPETHPSSSPAPPSSNTQEevPPSSVSDLSPMS 2110
Cdd:PHA03247  2845 PPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQ--PQAPPPPQPQPQ 2922

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2111 MPFASNSEPAPLTLASPRLVAADNQDTSNL--PQLAVPAPRVSHRMQPRGSfysvVPNATIHQDPQSifVTNPVPLTPPQ 2188
Cdd:PHA03247  2923 PPPPPQPQPPPPPPPRPQPPLAPTTDPAGAgePSGAVPQPWLGALVPGRVA----VPRFRVPQPAPS--REAPASSTPPL 2996

                          410
                   ....*....|
gi 1953314652 2189 GPPAAVQLSS 2198
Cdd:PHA03247  2997 TGHSLSRVSS 3006
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
793-879 1.88e-04

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  793 VEETEGKLNELGQRISAIEKaqlksleliqgeplNKDKIEELKKNREEQVQKKKKILKELQKVERQLqmKTQQQFTKEYL 872
Cdd:PRK03918   233 LEELKEEIEELEKELESLEG--------------SKRKLEEKIRELEERIEELKKEIEELEEKVKEL--KELKEKAEEYI 296


                   ....*..
gi 1953314652  873 ETKGQKD 879
Cdd:PRK03918   297 KLSEFYE 303
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
280-567 9.61e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.41  E-value: 9.61e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  280 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 359
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  360 NThSNEFKESALTLACYKGHLDMVRFLLDAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 439
Cdd:COG0666     81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  440 AACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFL 519
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1953314652  520 IKAGADIELGC---STPLMEASQEGHLELVKYLLAAGANVHATTATGDTAL 567
Cdd:COG0666    239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1083-1376 2.48e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.56  E-value: 2.48e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1083 ELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTKDTPLSLACSGGRQEVVDLLLARGANK 1162
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1163 EHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQiETNRNTAL 1242
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1243 TLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFC 1322
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIV 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1323 ELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPL 1376
Cdd:COG0666    236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
KH-I_ANKHD1 cd22503
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ...
 1713-1795 1.22e-49

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: 171.08  E-value: 1.22e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1713 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIP 1792
Cdd:cd22503      1 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIP 80


                   ...
gi 1953314652 1793 KNH 1795
Cdd:cd22503     81 RNH 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
139-404 4.36e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 4.36e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  139 ARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAENSHNAGQVDTRSLAEACSDGDVNAVRK 218
Cdd:COG0666     26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  219 LLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSA 298
Cdd:COG0666    106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  299 TGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKG 378
Cdd:COG0666    185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAG 263

                          250       260
                   ....*....|....*....|....*.
gi 1953314652  379 HLDMVRFLLDAGADQEHKTDEMHTAL 404
Cdd:COG0666    264 AALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 206-526 1.92e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 115.89  E-value: 1.92e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  206 EACSDGDVNAVRKLLDEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVedrgNKGDI---TPLMA-ASSGG 278
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADV----NAPERcgfTPLHLyLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  279 YLDIVKLLLLHDADVNSQSATGNTALtYACAGGF---VDIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVL 352
Cdd:PHA03095    96 TLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  353 LDHGAGI-----------NTHSNEFKESAltlacykghlDMVRFLLDAGADQEHKTDEMHTALMEACMDGHVE--VARLL 419
Cdd:PHA03095   174 IDAGADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPL 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  420 LDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINA----- 494
Cdd:PHA03095   244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETvaatl 323

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1953314652  495 ----QTEETQETALTLACcggfseVADFLIKAGADI 526
Cdd:PHA03095   324 ntasVAGGDIPSDATRLC------VAKVVLRGAFSL 353
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1138-1426 3.22e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.38  E-value: 3.22e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1138 TPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYV-----NIIKILLNAGAEINSrtGSKLGISPLMLAA 1212
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA--PDNNGITPLLYAI 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1213 MN--GHVPAVKLLLDMGSDINAqietnrntaltlacfqgraevvsllldrkanvehRAKTGLTPLMEAASGGYA--EVGR 1288
Cdd:PHA03100   115 SKksNSYSIVEYLLDNGANVNI----------------------------------KNSDGENLLHLYLESNKIdlKILK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1289 VLLDKGADVNAppvpssrdtaltiaADKghykfCELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAA 1368
Cdd:PHA03100   161 LLIDKGVDINA--------------KNR-----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652 1369 DNRKITPLMSAFRKGHVkvvqYLVKEVNQFPSDIECM---------RYIATITDKELLKKCHQCVET 1426
Cdd:PHA03100   222 NKYGDTPLHIAILNNNK----EIFKLLLNNGPSIKTIietllyfkdKDLNTITKIKMLKKSIMYMFL 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
271-361 3.29e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 101.35  E-value: 3.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  271 LMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANieDHNENGHTPLMEAASAGHVEVAR 350
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1953314652  351 VLLDHGAGINT 361
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1208-1299 6.48e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 6.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1208 LMLAAMNGHVPAVKLLLDMGSDINAQiETNRNTALTLACFQGRAEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1287
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 1953314652 1288 RVLLDKGADVNA 1299
Cdd:pfam12796   78 KLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
534-643 1.48e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  534 LMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLDKQEDmktilegidpakhqehese 613
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN------------------- 60

                           90       100       110
                   ....*....|....*....|....*....|
gi 1953314652  614 gGRTPLMKAARAGHLCTVQFLISKGANVNR 643
Cdd:pfam12796   61 -GRTALHYAARSGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
204-296 4.15e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 4.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  204 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGNkgdiTPLMAASSGGYLDI 282
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNGR----TALHYAARSGHLEI 76

                           90
                   ....*....|....
gi 1953314652  283 VKLLLLHDADVNSQ 296
Cdd:pfam12796   77 VKLLLEKGADINVK 90
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 1714-1778 1.96e-15

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: 72.70  E-value: 1.96e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINA 1778
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
619-704 1.15e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 1.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  619 LMKAARAGHLCTVQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTNVV 698
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77


                   ....*.
gi 1953314652  699 SYLLDY 704
Cdd:pfam12796   78 KLLLEK 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 335-507 5.59e-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: 68.12  E-value: 5.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  335 TPLMEAASAGHVEVARVLLdhgagINTHSNEFK-----ESALTLACYKGHLDMVRFLLDAGAD--QEHKTDEMH---TAL 404
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLL-----KCPSCDLFQrgalgETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTAL 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  405 MEACMDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL 470
Cdd:cd22192     94 HIAVVNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1953314652  471 ----MEAAREGHEEMVALLLAQGANINAQTEETQE-----TALTLA 507
Cdd:cd22192    174 hilvLQPNKTFACQMYDLILSYDKEDDLQPLDLVPnnqglTPFKLA 219
KH smart00322
K homology RNA-binding domain;
1716-1780 2.79e-10

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 58.08  E-value: 2.79e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652  1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDkqKDKNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIP--GPGSEERVVEITGPPENVEKAAELILEIL 68
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 211-332 1.04e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 1.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  211 GDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR--------------GNKGDiTPLM 272
Cdd:PHA03100   119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsygvpinikDVYGF-TPLH 197

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  273 AASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 332
Cdd:PHA03100   198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 504-655 1.38e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  504 LTLACCGGfSEVADFLIKAGADIELGCS---TPLMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVAD 580
Cdd:PLN03192   530 LTVASTGN-AALLEELLKAKLDPDIGDSkgrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  581 VLLQ--------AGADL----DKQEDMKTILEGIDPAKHQEHESEGGRTPLMKAARAGHLCTVQFLISKGANVNRATANN 648
Cdd:PLN03192   609 ILYHfasisdphAAGDLlctaAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688


                   ....*..
gi 1953314652  649 DHTVVSL 655
Cdd:PLN03192   689 DFSPTEL 695
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 531-686 4.29e-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: 61.95  E-value: 4.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  531 STPLMEASQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDKQEDMKTILEgidpakhqe 609
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLYQ--------- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  610 hesegGRTPLMKAARAGHLCTVQFLISKGANVN--RATAN------------NDHTVVSLACAgGHLAVVELLLAHGADP 675
Cdd:cd22192     89 -----GETALHIAVVNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEHPLSFAACV-GNEEIVRLLIEHGADI 162

                          170
                   ....*....|.
gi 1953314652  676 THRLKDGSTML 686
Cdd:cd22192    163 RAQDSLGNTVL 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1171-1360 1.16e-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: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1171 TPLSLAASGGYVNIIKILL-NAGAEINSRtGSkLGISPLMLAAMNGHVPAVKLLLD---------MGSDINAQietnrNT 1240
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQR-GA-LGETALHVAALYDNLEAAVVLMEaapelvnepMTSDLYQG-----ET 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1241 ALTLACFQGRAEVVSLLLDRKANVE---------HRAKTGLT-----PLMEAASGGYAEVGRVLLDKGADVNAppvpssR 1306
Cdd:cd22192     92 ALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRA------Q 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1307 D----TALTIAADKGHYKF-CE---LLINRGAHID------VRNKKGNTPLWLASNGGHFDVVQLLVQ 1360
Cdd:cd22192    166 DslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 619-741 2.15e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 2.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  619 LMKAARAGHLCTVQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVV 698
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652  699 SYLLDY------------PNNVLSVPTT-DVSQLTSSSQDQSQVPRVPMHTLAMVV 741
Cdd:PTZ00322   165 QLLSRHsqchfelganakPDSFTGKPPSlEDSPISSHHPDFSAVPQPMMGSLIVIM 220
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 307-460 5.04e-06

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: 52.01  E-value: 5.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  307 ACAGGFVDIVKVLLNEGA--NIEDHNENGHTPLMEAASAG-HVEVARVLLDHGAGINThsnefkESALTLACYKGHLDMV 383
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV------GDTLLHAISLEYVDAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  384 ----RFLLDAGADQ-------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ES 435
Cdd:TIGR00870   98 eailLHLLAAFRKSgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgES 177

                          170       180
                   ....*....|....*....|....*
gi 1953314652  436 PLTLAACGGHVELAALLIERGANLE 460
Cdd:TIGR00870  178 PLNAAACLGSPSIVALLSEDPADIL 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 465-494 1.33e-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: 43.73  E-value: 1.33e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1953314652   465 EGYTPLMEAAREGHEEMVALLLAQGANINA 494
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1204-1232 6.85e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 6.85e-05
                            10        20
                    ....*....|....*....|....*....
gi 1953314652  1204 GISPLMLAAMNGHVPAVKLLLDMGSDINA 1232
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 563-591 9.10e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 9.10e-05
                            10        20
                    ....*....|....*....|....*....
gi 1953314652   563 GDTALTYACENGHTDVADVLLQAGADLDK 591
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1797-2198 1.10e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1797 RTPASTKSIHANfSSGVGTTAASSKNAFPLGAPTlvtsqattlstfQPTNKLTKNVPANVRSSFPVSlPLAYPHPHFALL 1876
Cdd:PHA03247  2625 DPPPPSPSPAAN-EPDPHPPPTVPPPERPRDDPA------------PGRVSRPRRARRLGRAAQASS-PPQRPRRRAARP 2690

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1877 AAQTMQQIRHPRLPmaqfGGTFSPSPNTWG---PFPVRPVNPGNTNSSPKHNNAGRlPNQNGTVLPSESAGLATASCPIT 1953
Cdd:PHA03247  2691 TVGSLTSLADPPPP----PPTPEPAPHALVsatPLPPGPAAARQASPALPAAPAPP-AVPAGPATPGGPARPARPPTTAG 2765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1954 VSSVVAASQQLCV---TNTRTPSSVRKQLFACVPKTSPPATVISSVTSTCSSLPSvSSAPVTSGQVPTTFLPASTPQAQL 2030
Cdd:PHA03247  2766 PPAPAPPAAPAAGpprRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP-AASPAGPLPPPTSAQPTAPPPPPG 2844

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2031 SSQKMESFSAMPPPKEKVSTQDQAMAHLCTPSSTANSCSSSASNTPGAPETHPSSSPAPPSSNTQEevPPSSVSDLSPMS 2110
Cdd:PHA03247  2845 PPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQ--PQAPPPPQPQPQ 2922

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2111 MPFASNSEPAPLTLASPRLVAADNQDTSNL--PQLAVPAPRVSHRMQPRGSfysvVPNATIHQDPQSifVTNPVPLTPPQ 2188
Cdd:PHA03247  2923 PPPPPQPQPPPPPPPRPQPPLAPTTDPAGAgePSGAVPQPWLGALVPGRVA----VPRFRVPQPAPS--REAPASSTPPL 2996

                          410
                   ....*....|
gi 1953314652 2189 GPPAAVQLSS 2198
Cdd:PHA03247  2997 TGHSLSRVSS 3006
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
793-879 1.88e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  793 VEETEGKLNELGQRISAIEKaqlksleliqgeplNKDKIEELKKNREEQVQKKKKILKELQKVERQLqmKTQQQFTKEYL 872
Cdd:PRK03918   233 LEELKEEIEELEKELESLEG--------------SKRKLEEKIRELEERIEELKKEIEELEEKVKEL--KELKEKAEEYI 296


                   ....*..
gi 1953314652  873 ETKGQKD 879
Cdd:PRK03918   297 KLSEFYE 303
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1930-2207 8.02e-04

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: 45.14  E-value: 8.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1930 LPNQNGTVLPSESAGLATASCPITVSSVVAASQQLCVTNTRTPSSVRKQlfacvpKTSPPATVI-SSVTSTCSSLPSVSS 2008
Cdd:pfam03154  174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ------STAAPHTLIqQTPTLHPQRLPSPHP 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2009 A--PVTSGQVPTTFLPASTPQAQLSSQ----------------------------KMESFSAMPPPKEKVSTQDQAMAHL 2058
Cdd:pfam03154  248 PlqPMTQPPPPSQVSPQPLPQPSLHGQmppmphslqtgpshmqhpvppqpfpltpQSSQSQVPPGPSPAAPGQSQQRIHT 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2059 CTPSSTANSCSSSASNT-PGAPETHP-----SSSPAPPSSNTQEEVPPSSVSDLSPMSM-----------PFAS------ 2115
Cdd:pfam03154  328 PPSQSQLQSQQPPREQPlPPAPLSMPhikppPTTPIPQLPNPQSHKHPPHLSGPSPFQMnsnlppppalkPLSSlsthhp 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2116 -NSEPAPLTL--ASPRLVAADNQDTSNLPQLAVPAPRVSHrmQPRGSFYSVVPNATIhqdPQSIFV-TNPVPLTPPQGPP 2191
Cdd:pfam03154  408 pSAHPPPLQLmpQSQQLPPPPAQPPVLTQSQSLPPPAASH--PPTSGLHQVPSQSPF---PQHPFVpGGPPPITPPSGPP 482

                          330
                   ....*....|....*.
gi 1953314652 2192 AavqlsSAMNIMNGSQ 2207
Cdd:pfam03154  483 T-----STSSAMPGIQ 493
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1073-1261 1.51e-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: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1073 LTLACAGGHEELVSVLIARDAKIEHRDKkgftpLILAATAGHVGVVE----ILLDKGGDI--------EAQSERTKD-TP 1139
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDAVEaillHLLAAFRKSgplelandQYTSEFTPGiTA 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1140 LSLACSGGRQEVVDLLLARGAN------------KEHRNVSDYT--PLSLAASGGYVNIIKILLNAGAEInsRTGSKLGI 1205
Cdd:TIGR00870  132 LHLAAHRQNYEIVKLLLERGASvparacgdffvkSQGVDSFYHGesPLNAAACLGSPSIVALLSEDPADI--LTADSLGN 209

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652 1206 SPLMLAAMNGHVPAV---------KLLLDMG--SDINAQIE--TNRN--TALTLACFQGRAEVVSLLLDRK 1261
Cdd:TIGR00870  210 TLLHLLVMENEFKAEyeelscqmyNFALSLLdkLRDSKELEviLNHQglTPLKLAAKEGRIVLFRLKLAIK 280
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 808-878 5.43e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 41.25  E-value: 5.43e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652  808 SAIEKAQLKSLELIQGEPLNKDKIEELKKNREEQVQKKKKILKELQKVERQLqmktqQQFTKEYLETKGQK 878
Cdd:COG4026    114 NAIIRAGLKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESEL-----EELREEYKKLREEN 179
NYD-SP28 pfam14772
Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in ...
 794-865 5.57e-03

Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in spermatogenic cell cytoplams and human spermatozoa tail. It is post-translationally modified during sperm capacitation and ultimately contributes to the success of fertilization.


Pssm-ID: 464307 [Multi-domain]  Cd Length: 102  Bit Score: 38.73  E-value: 5.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652  794 EETEGKLNELGQRISAIeKAQLKSLELiqgeplnKDKIEELKKNREEQVQKKKKILKELQKverQLQMKTQQ 865
Cdd:pfam14772   30 KSSQEKFEKINQRWRSI-LRKNKPQEL-------REELEEQKQACERIIDRKDKLIKELQQ---ELKEADEQ 90
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 532-686 7.12e-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: 41.61  E-value: 7.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  532 TPLMEASQEG-HLELVKYLLAAGANVhattATGDTALTYACENGHTDVADVLLQAgadLDKQEDMKTILEGIDPAKHQEH 610
Cdd:TIGR00870   54 SALFVAAIENeNLELTELLLNLSCRG----AVGDTLLHAISLEYVDAVEAILLHL---LAAFRKSGPLELANDQYTSEFT 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  611 EsegGRTPLMKAARAGHLCTVQFLISKGANVNrATANNDHTV--------------VSLACAGGHLAVVELLLAHGADPT 676
Cdd:TIGR00870  127 P---GITALHLAAHRQNYEIVKLLLERGASVP-ARACGDFFVksqgvdsfyhgespLNAAACLGSPSIVALLSEDPADIL 202

                          170
                   ....*....|
gi 1953314652  677 HRLKDGSTML 686
Cdd:TIGR00870  203 TADSLGNTLL 212
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
280-567 9.61e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.41  E-value: 9.61e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  280 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 359
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  360 NThSNEFKESALTLACYKGHLDMVRFLLDAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 439
Cdd:COG0666     81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  440 AACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFL 519
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1953314652  520 IKAGADIELGC---STPLMEASQEGHLELVKYLLAAGANVHATTATGDTAL 567
Cdd:COG0666    239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
380-708 5.87e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.48  E-value: 5.87e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  380 LDMVRFLLDAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANL 459
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  460 EEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQetaltlaccggfsevadflikagadielgcsTPLMEASQ 539
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-------------------------------TPLHLAAY 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  540 EGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDKQedmktilegidpakhqeheSEGGRTPL 619
Cdd:COG0666    130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR-------------------DNDGETPL 190

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  620 MKAARAGHLCTVQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVVS 699
Cdd:COG0666    191 HLAAENGHLEIVKLLLEAGADVN-AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269


                   ....*....
gi 1953314652  700 YLLDYPNNV 708
Cdd:COG0666    270 LLLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1083-1376 2.48e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 195.56  E-value: 2.48e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1083 ELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTKDTPLSLACSGGRQEVVDLLLARGANK 1162
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1163 EHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQiETNRNTAL 1242
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1243 TLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFC 1322
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIV 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1323 ELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPL 1376
Cdd:COG0666    236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-431 6.56e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.40  E-value: 6.56e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  150 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAENSHNAGQVDTRSLAEACSDGDVNAVRKLLDEGRSVNEH 229
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  230 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACA 309
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  310 GGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHsNEFKESALTLACYKGHLDMVRFLLDA 389
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1953314652  390 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 431
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1120-1394 9.51e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.94  E-value: 9.51e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1120 ILLDKGGDIEAQSERTKDTPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRT 1199
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1200 gsKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQIEtNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAA 1279
Cdd:COG0666     85 --DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1280 SGGYAEVGRVLLDKGADVNAPPvpSSRDTALTIAADKGHYKFCELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLV 1359
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARD--NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1953314652 1360 QAGADVDAADNRKITPLMSAFRKGHVKVVQYLVKE 1394
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1059-1343 4.06e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.01  E-value: 4.06e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1059 VDIDAHTESNHDTALTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERtKDT 1138
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1139 PLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHVP 1218
Cdd:COG0666     90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTPLHLAAANGNLE 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1219 AVKLLLDMGSDINAQIEtNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVN 1298
Cdd:COG0666    168 IVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1953314652 1299 APpvPSSRDTALTIAADKGHYKFCELLINRGAHIDVRNKKGNTPL 1343
Cdd:COG0666    247 AK--DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1150-1393 7.62e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.76  E-value: 7.62e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1150 EVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHVPAVKLLLDMGSD 1229
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALA--DALGALLLLAAALAGDLLVALLLLAAGAD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1230 INAQIEtNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPvpSSRDTA 1309
Cdd:COG0666     80 INAKDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1310 LTIAADKGHYKFCELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQ 1389
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                   ....
gi 1953314652 1390 YLVK 1393
Cdd:COG0666    237 LLLE 240
KH-I_ANKHD1 cd22503
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ...
 1713-1795 1.22e-49

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: 171.08  E-value: 1.22e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1713 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIP 1792
Cdd:cd22503      1 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIP 80


                   ...
gi 1953314652 1793 KNH 1795
Cdd:cd22503     81 RNH 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
139-404 4.36e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 4.36e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  139 ARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAENSHNAGQVDTRSLAEACSDGDVNAVRK 218
Cdd:COG0666     26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  219 LLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSA 298
Cdd:COG0666    106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  299 TGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKG 378
Cdd:COG0666    185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAG 263

                          250       260
                   ....*....|....*....|....*.
gi 1953314652  379 HLDMVRFLLDAGADQEHKTDEMHTAL 404
Cdd:COG0666    264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1184-1393 6.79e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.73  E-value: 6.79e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1184 IIKILLNAGAEINSRTGSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQIEtNRNTALTLACFQGRAEVVSLLLDRKAN 1263
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADA-LGALLLLAAALAGDLLVALLLLAAGAD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1264 VEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLINRGAHIDVRNKKGNTPL 1343
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA--RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1344 WLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQYLVK 1393
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
KH-I_MASK cd22404
type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family ...
 1713-1783 7.31e-34

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: 125.40  E-value: 7.31e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652 1713 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDP 1783
Cdd:cd22404      1 KSKKVTVPNSAISRVIGRGGCNINAIREVSGAHIEIDKQKGEQGDRRITIKGSADATRQAAQLINALIKDP 71
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
 1713-1783 9.11e-33

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: 122.56  E-value: 9.11e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652 1713 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDP 1783
Cdd:cd22502      1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
 206-526 1.92e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 115.89  E-value: 1.92e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  206 EACSDGDVNAVRKLLDEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVedrgNKGDI---TPLMA-ASSGG 278
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADV----NAPERcgfTPLHLyLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  279 YLDIVKLLLLHDADVNSQSATGNTALtYACAGGF---VDIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVL 352
Cdd:PHA03095    96 TLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  353 LDHGAGI-----------NTHSNEFKESAltlacykghlDMVRFLLDAGADQEHKTDEMHTALMEACMDGHVE--VARLL 419
Cdd:PHA03095   174 IDAGADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPL 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  420 LDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINA----- 494
Cdd:PHA03095   244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETvaatl 323

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1953314652  495 ----QTEETQETALTLACcggfseVADFLIKAGADI 526
Cdd:PHA03095   324 ntasVAGGDIPSDATRLC------VAKVVLRGAFSL 353
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1138-1426 3.22e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.38  E-value: 3.22e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1138 TPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYV-----NIIKILLNAGAEINSrtGSKLGISPLMLAA 1212
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA--PDNNGITPLLYAI 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1213 MN--GHVPAVKLLLDMGSDINAqietnrntaltlacfqgraevvsllldrkanvehRAKTGLTPLMEAASGGYA--EVGR 1288
Cdd:PHA03100   115 SKksNSYSIVEYLLDNGANVNI----------------------------------KNSDGENLLHLYLESNKIdlKILK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1289 VLLDKGADVNAppvpssrdtaltiaADKghykfCELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAA 1368
Cdd:PHA03100   161 LLIDKGVDINA--------------KNR-----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652 1369 DNRKITPLMSAFRKGHVkvvqYLVKEVNQFPSDIECM---------RYIATITDKELLKKCHQCVET 1426
Cdd:PHA03100   222 NKYGDTPLHIAILNNNK----EIFKLLLNNGPSIKTIietllyfkdKDLNTITKIKMLKKSIMYMFL 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1083-1346 1.16e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 113.58  E-value: 1.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1083 ELVSVLIARDAKIEHRDKKGFTPL-ILAATAGHVG--VVEILLDKGGDIEAQsERTKDTPL-SLACSGGRQEVVDLLLAR 1158
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1159 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPLMLAAMNGHVPA--VKLLLDMGSDINAqI 1234
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLAVLLKSRNANVelLRLLIDAGADVYA-V 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1235 ETNRNTALTLAC--FQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssRD--- 1307
Cdd:PHA03095   184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA------RNryg 257

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1953314652 1308 -TALTIAADKGHYKFCELLINRGAHIDVRNKKGNTPLWLA 1346
Cdd:PHA03095   258 qTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
271-361 3.29e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 101.35  E-value: 3.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  271 LMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANieDHNENGHTPLMEAASAGHVEVAR 350
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1953314652  351 VLLDHGAGINT 361
Cdd:pfam12796   79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 413-590 1.22e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 106.67  E-value: 1.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  413 VEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-----ELAALLIERGANLEEVNDEGYTPLMEAARE--GHEEMVALL 485
Cdd:PHA03100    48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  486 LAQGANINAQTEeTQETALTLA--CCGGFSEVADFLIKAGADI----------ELGC---------STPLMEASQEGHLE 544
Cdd:PHA03100   128 LDNGANVNIKNS-DGENLLHLYleSNKIDLKILKLLIDKGVDInaknrvnyllSYGVpinikdvygFTPLHYAVYNNNPE 206

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1953314652  545 LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLD 590
Cdd:PHA03100   207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 255-494 1.08e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 103.59  E-value: 1.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  255 MHANVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFV-----DIVKVLLNEGANIEDH 329
Cdd:PHA03100    23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  330 NENGHTPLMEAASA--GHVEVARVLLDHGAGINTHSNEFKES-ALTLACYKGHLDMVRFLLDAGADQEHKTDemhtalme 406
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLlHLYLESNKIDLKILKLLIDKGVDINAKNR-------- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  407 acmdghVEvarLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLL 486
Cdd:PHA03100   175 ------VN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245


                   ....*...
gi 1953314652  487 AQGANINA 494
Cdd:PHA03100   246 NNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
304-396 1.34e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 1.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  304 LTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHgagINTHSNEFKESALTLACYKGHLDMV 383
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|...
gi 1953314652  384 RFLLDAGADQEHK 396
Cdd:pfam12796   78 KLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 192-589 5.02e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 103.99  E-value: 5.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  192 NSHNAGQVDTRSLAEACSDGDV--NAVRKLLDEGRSVNEHTEEGESLLclacsagyyelAQVLLAMHANVedrgNKGDI- 268
Cdd:PHA02876   113 NKHKLDEACIHILKEAISGNDIhyDKINESIEYMKLIKERIQQDELLI-----------AEMLLEGGADV----NAKDIy 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  269 --TPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIedhNENGHTpLMEAASAGHV 346
Cdd:PHA02876   178 ciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI---NKNDLS-LLKAIRNEDL 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  347 EVARVLLDHGAGINThSNEFKESALTLACYKGHLD-MVRFLLDAGADQEHKTDEMHTALMEACMDGH-VEVARLLLDSGA 424
Cdd:PHA02876   254 ETSLLLYDAGFSVNS-IDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGA 332

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  425 QVNMPADSFESPLTLAAC-GGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQeTA 503
Cdd:PHA02876   333 DVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TA 411

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  504 LTLACCGG--FSEVADfLIKAGADIELG---CSTPLMEASQEG-HLELVKYLLAAGANVHATTATGDTALTYACenGHTD 577
Cdd:PHA02876   412 LHFALCGTnpYMSVKT-LIDRGANVNSKnkdLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHG 488

                          410
                   ....*....|..
gi 1953314652  578 VADVLLQAGADL 589
Cdd:PHA02876   489 IVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1208-1299 6.48e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 6.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1208 LMLAAMNGHVPAVKLLLDMGSDINAQiETNRNTALTLACFQGRAEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1287
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 1953314652 1288 RVLLDKGADVNA 1299
Cdd:pfam12796   78 KLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
404-495 9.10e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 9.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  404 LMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANleEVNDEGYTPLMEAAREGHEEMVA 483
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1953314652  484 LLLAQGANINAQ 495
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 313-598 1.46e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 100.87  E-value: 1.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  313 VDIVKVLLNEGANIEDHNENGHTPL---MEAASAGHVEVARVLLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLDA 389
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  390 GADQEHKTDEMHTALmEACMDG---HVEVARLLLDSGAQVNmpaDSFESPLTLAAC-----GGHVELAALLIERGANLEE 461
Cdd:PHA03095   107 GADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVN---ALDLYGMTPLAVllksrNANVELLRLLIDAGADVYA 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  462 VNDEGYTPL---MEAAREgHEEMVALLLAQGANINAqTEETQETALTLACCGGF---SEVADFLIkAGADIE----LGcS 531
Cdd:PHA03095   183 VDDRFRSLLhhhLQSFKP-RARIVRELIRAGCDPAA-TDMLGNTPLHSMATGSSckrSLVLPLLI-AGISINarnrYG-Q 258

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652  532 TPLMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADvllqagADLDKQEDMKTI 598
Cdd:PHA03095   259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR------AALAKNPSAETV 319
Ank_2 pfam12796
Ankyrin repeats (3 copies);
534-643 1.48e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  534 LMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLDKQEDmktilegidpakhqehese 613
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN------------------- 60

                           90       100       110
                   ....*....|....*....|....*....|
gi 1953314652  614 gGRTPLMKAARAGHLCTVQFLISKGANVNR 643
Cdd:pfam12796   61 -GRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1098-1334 4.72e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 98.58  E-value: 4.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1098 RDKKGFTPLILAATAGHVGVVEILLDKGGDIeAQSERTKDTPLSLACSGGR-----QEVVDLLLARGANKEHRNVSDYTP 1172
Cdd:PHA03100    31 SYKKPVLPLYLAKEARNIDVVKILLDNGADI-NSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITP 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1173 LSLAASG--GYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHV--PAVKLLLDMGSDINAqieTNRntaltlacfq 1248
Cdd:PHA03100   110 LLYAISKksNSYSIVEYLLDNGANVNIKN--SDGENLLHLYLESNKIdlKILKLLIDKGVDINA---KNR---------- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1249 graevVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLINR 1328
Cdd:PHA03100   175 -----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL--VNKYGDTPLHIAILNNNKEIFKLLLNN 247


                   ....*.
gi 1953314652 1329 GAHIDV 1334
Cdd:PHA03100   248 GPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
337-427 6.13e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 6.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  337 LMEAASAGHVEVARVLLDHGAGINTHsNEFKESALTLACYKGHLDMVRFLLDaGADQEHKTDEMhTALMEACMDGHVEVA 416
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIV 77

                           90
                   ....*....|.
gi 1953314652  417 RLLLDSGAQVN 427
Cdd:pfam12796   78 KLLLEKGADIN 88
PHA03095 PHA03095
ankyrin-like protein; Provisional
 362-689 8.58e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.56  E-value: 8.58e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  362 HSNEFKESAL---TLACYKGHLDMVRFLLDAGADQEHK----TDEMHTALMEACMDGhVEVARLLLDSGAQVNMPADSFE 434
Cdd:PHA03095     6 SVDIIMEAALydyLLNASNVTVEEVRRLLAAGADVNFRgeygKTPLHLYLHYSSEKV-KDIVRLLLEAGADVNAPERCGF 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  435 SPLTLAACGGHVE-LAALLIERGANLEEVNDEGYTPLMEAAR--EGHEEMVALLLAQGANINAQTeetqetaltlacCGG 511
Cdd:PHA03095    85 TPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALD------------LYG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  512 FSEVADFLIKAGADIELgcstplmeasqeghlelVKYLLAAGANVHATTATGDTALTYACENGHTDvADVLlqagadldk 591
Cdd:PHA03095   153 MTPLAVLLKSRNANVEL-----------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPR-ARIV--------- 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  592 qedMKTILEGIDPAKHQEHesegGRTPLMKAArAGHLCT---VQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELL 668
Cdd:PHA03095   206 ---RELIRAGCDPAATDML----GNTPLHSMA-TGSSCKrslVLPLLIAGISIN-ARNRYGQTPLHYAAVFNNPRACRRL 276

                          330       340
                   ....*....|....*....|.
gi 1953314652  669 LAHGADPTHRLKDGSTMLIEA 689
Cdd:PHA03095   277 IALGADINAVSSDGNTPLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1173-1267 3.30e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 3.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1173 LSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHVPAVKLLLDMgsdINAQIETNRNTALTLACFQGRAE 1252
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLE 75

                           90
                   ....*....|....*
gi 1953314652 1253 VVSLLLDRKANVEHR 1267
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1140-1233 1.86e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1140 LSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNaGAEINSRTGsklGISPLMLAAMNGHVPA 1219
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN---GRTALHYAARSGHLEI 76

                           90
                   ....*....|....
gi 1953314652 1220 VKLLLDMGSDINAQ 1233
Cdd:pfam12796   77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
437-528 3.72e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 3.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  437 LTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQgANINAQTEetQETALTLACCGGFSEVA 516
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 1953314652  517 DFLIKAGADIEL 528
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 315-704 5.31e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 94.36  E-value: 5.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  315 IVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEfKESALTLACYKGHLDMVRFLLDAGADQe 394
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAIIDNRSNI- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  395 HKTDemhTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-ELAALLIERGANLEEVNDEGYTPLMEA 473
Cdd:PHA02876   238 NKND---LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLM 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  474 AREGHE-EMVALLLAQGANINAqteetqetaltlaccggfsevADFLIkagadielgcSTPLMEASQ-EGHLELVKYLLA 551
Cdd:PHA02876   315 AKNGYDtENIRTLIMLGADVNA---------------------ADRLY----------ITPLHQASTlDRNKDIVITLLE 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  552 AGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDK-QEDMKTILegidpakhqeHESEGGRTPLMkaaraghlcT 630
Cdd:PHA02876   364 LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAlSQKIGTAL----------HFALCGTNPYM---------S 424

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652  631 VQFLISKGANVNraTANND-HTVVSLACAGG-HLAVVELLLAHGADPTH-RLKDGSTMLIEAakgGHTNVVSYLLDY 704
Cdd:PHA02876   425 VKTLIDRGANVN--SKNKDlSTPLHYACKKNcKLDVIEMLLDNGADVNAiNIQNQYPLLIAL---EYHGIVNILLHY 496
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 452-674 1.57e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  452 LIERGANLEEVNDEGY----TPLMEAAREGHEEMVALLLAQGANINaQTEETQETALTLACCGGFS-----EVADFLIKA 522
Cdd:PHA03100    17 NIKYIIMEDDLNDYSYkkpvLPLYLAKEARNIDVVKILLDNGADIN-SSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  523 GADIELG---CSTPLMEASQE--GHLELVKYLLAAGANVHATTATGDTALTYACENGHTD--VADVLLQAGADLDKQEDM 595
Cdd:PHA03100    96 GANVNAPdnnGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNRV 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  596 KTILE-GIdpakHQEHESEGGRTPLMKAARAGHLCTVQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHGAD 674
Cdd:PHA03100   176 NYLLSyGV----PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN-LVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
204-296 4.15e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 4.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  204 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGNkgdiTPLMAASSGGYLDI 282
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNGR----TALHYAARSGHLEI 76

                           90
                   ....*....|....
gi 1953314652  283 VKLLLLHDADVNSQ 296
Cdd:pfam12796   77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1275-1369 6.69e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 6.69e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1275 LMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLINrgaHIDVRNK-KGNTPLWLASNGGHFD 1353
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANL--QDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKdNGRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1953314652 1354 VVQLLVQAGADVDAAD 1369
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1310-1393 6.89e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 6.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1310 LTIAADKGHYKFCELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQaGADVDAADNRKiTPLMSAFRKGHVKVVQ 1389
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVK 78


                   ....
gi 1953314652 1390 YLVK 1393
Cdd:pfam12796   79 LLLE 82
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 280-590 7.79e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 90.51  E-value: 7.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  280 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 359
Cdd:PHA02876   158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  360 NTHsnefkESALTLACYKGHLDMVRFLLDAGADQEHKTDEMHTALMEACMDGhvEVARL---LLDSGAQVNMPADSFESP 436
Cdd:PHA02876   238 NKN-----DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAP--SLSRLvpkLLERGADVNAKNIKGETP 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  437 LTLAACGGH-VELAALLIERGANLEEVNDEGYTPLMEAAR-EGHEEMVALLLAQGANINAQtEETQETALTLACCGGFSE 514
Cdd:PHA02876   311 LYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNAR-DYCDKTPIHYAAVRNNVV 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  515 VADFLIKAGADIE-----LGCSTPLMEASQEGHLElVKYLLAAGANVHATTATGDTALTYACENG-HTDVADVLLQAGAD 588
Cdd:PHA02876   390 IINTLLDYGADIEalsqkIGTALHFALCGTNPYMS-VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468


                   ..
gi 1953314652  589 LD 590
Cdd:PHA02876   469 VN 470
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 302-589 1.68e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 87.71  E-value: 1.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  302 TALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGagINThsnefkeSALTLACYKGhlD 381
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDT-------SILPIPCIEK--D 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  382 MVRFLLDAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEE 461
Cdd:PHA02874   106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  462 VNDEGYTPLMEAAREGHEEMVALLLAQGANINAQteetqetaltlaCCGGFsevadflikagadielgcsTPLMEASQeg 541
Cdd:PHA02874   186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK------------CKNGF-------------------TPLHNAII-- 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953314652  542 HLELVKYLLAAGANVHATTATGDTALTYA----CEnghTDVADVLLQAGADL 589
Cdd:PHA02874   233 HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADI 281
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1071-1380 1.97e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.97  E-value: 1.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1071 TALTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQsertkDTPLSLACSGGRQE 1150
Cdd:PHA02876   180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN-----DLSLLKAIRNEDLE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1151 VVDLLLARGANKEHRNVSDYTPLSLAASGGYVN-IIKILLNAGAEINSRTGSklGISPLMLAAMNGH-VPAVKLLLDMGS 1228
Cdd:PHA02876   255 TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK--GETPLYLMAKNGYdTENIRTLIMLGA 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1229 DINAQiETNRNTALTLACFQGR-AEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRD 1307
Cdd:PHA02876   333 DVNAA-DRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA--LSQKIG 409

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652 1308 TALTIA-ADKGHYKFCELLINRGAHIDVRNKKGNTPLWLA-SNGGHFDVVQLLVQAGADVDAADNRKITPLMSAF 1380
Cdd:PHA02876   410 TALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYAcKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL 484
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1242-1336 2.72e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 2.72e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1242 LTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKgADVNappVPSSRDTALTIAADKGHYKF 1321
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN---LKDNGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 1953314652 1322 CELLINRGAHIDVRN 1336
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
504-592 2.91e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 2.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  504 LTLACCGGFSEVADFLIKAGADIELGCS---TPLMEASQEGHLELVKYLLA-AGANVhatTATGDTALTYACENGHTDVA 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKngrTALHLAAKNGHLEIVKLLLEhADVNL---KDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|...
gi 1953314652  580 DVLLQAGADLDKQ 592
Cdd:pfam12796   78 KLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1117-1431 5.31e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.17  E-value: 5.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1117 VVEILLDKGGDIEAQSERTKdTPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEin 1196
Cdd:PHA02874    17 IEKIIKNKGNCINISVDETT-TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD-- 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1197 srtgsklgISPLMLAAMNGHVpaVKLLLDMGSDINAQiETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLM 1276
Cdd:PHA02874    94 --------TSILPIPCIEKDM--IKTILDCGIDVNIK-DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1277 EAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIAADKGHYKFCELLINRGAHIDVRNKKGNTPLWLA---------- 1346
Cdd:PHA02874   163 IAIKHNFFDIIKLLLEKGAYANVK--DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiihnrsaiel 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1347 -----------SNGG---HF--------DVVQLLVQAGADVDAADNRKITPLMSAFRK-GHVKVVQ------YLVKEVNQ 1397
Cdd:PHA02874   241 linnasindqdIDGStplHHainppcdiDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKdiianaVLIKEADK 320

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1953314652 1398 FPsDIECMRYIATITDKELLKKCHQCVETIVKAK 1431
Cdd:PHA02874   321 LK-DSDFLEHIEIKDNKEFSDFIKECNEEIEDMK 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1073-1166 7.48e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 7.48e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1073 LTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKgGDIEAQSErtKDTPLSLACSGGRQEVV 1152
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1953314652 1153 DLLLARGANKEHRN 1166
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 338-670 8.63e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 8.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  338 MEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKGH---LDMVRFLLDAGADQEHKTDEMHTAL-MEACMDGHV 413
Cdd:PHA03095    19 LLNASNVTVEEVRRLLAAGADVN-FRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  414 EVARLLLDSGAQVNMPADSFESPLTLAACGG--HVELAALLIERGANLEEVNDEGYTPLMeaaregheemvALLLAQGAN 491
Cdd:PHA03095    98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLA-----------VLLKSRNAN 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  492 InaqteetqetaltlaccggfsEVADFLIKAGADI---ELGCSTPLmeasqEGHLE-------LVKYLLAAGANVHATTA 561
Cdd:PHA03095   167 V---------------------ELLRLLIDAGADVyavDDRFRSLL-----HHHLQsfkprarIVRELIRAGCDPAATDM 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  562 TGDTALTYA---CENGHTDVADvLLQAGADLDKQEDMktilegidpakhqehesegGRTPLMKAARAGHLCTVQFLISKG 638
Cdd:PHA03095   221 LGNTPLHSMatgSSCKRSLVLP-LLIAGISINARNRY-------------------GQTPLHYAAVFNNPRACRRLIALG 280

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1953314652  639 ANVNRATANNDhTVVSLACAGGHLAVVELLLA 670
Cdd:PHA03095   281 ADINAVSSDGN-TPLSLMVRNNNGRAVRAALA 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 303-525 2.59e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 83.89  E-value: 2.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  303 ALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEFkESALTLACYKGHLDM 382
Cdd:PHA02875     5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  383 VRFLLDAG--ADQEHKTDEMhTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLE 460
Cdd:PHA02875    84 VEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652  461 EVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTLACCGGFSEVADFLIKAGAD 525
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1250-1393 6.57e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 6.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1250 RAEVVSLLLDRKANVEHR---AKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALtiaadkgHYKFC---- 1322
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRgeyGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAP--ERCGFTPL-------HLYLYnatt 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1323 ----ELLINRGAHIDVRNKKGNTPL--WLASNGGHFDVVQLLVQAGADVDAADNRKITPLmSAFRKGH---VKVVQYLVK 1393
Cdd:PHA03095    97 ldviKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPL-AVLLKSRnanVELLRLLID 175
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 212-361 6.88e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 6.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  212 DVNAVRKLLDEGRSVNEHTEEGES-LLCLAC-SAGYYELAQVLLAMHANVEDRGNKGdITPLMAASSGGY--LDIVKLLL 287
Cdd:PHA03100    85 VKEIVKLLLEYGANVNAPDNNGITpLLYAISkKSNSYSIVEYLLDNGANVNIKNSDG-ENLLHLYLESNKidLKILKLLI 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  288 LHDADVN----------------SQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARV 351
Cdd:PHA03100   164 DKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                          170
                   ....*....|
gi 1953314652  352 LLDHGAGINT 361
Cdd:PHA03100   244 LLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1083-1236 7.80e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.41  E-value: 7.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1083 ELVSVLIARDAKIEHRDKKGFTPLILAATA--GHVGVVEILLDKGGDIEAQSERTKdTPLSLACSGGRQEV--------- 1151
Cdd:PHA03100    87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKIDLkilkllidk 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1152 ---------VDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHVPAVKL 1222
Cdd:PHA03100   166 gvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN--KYGDTPLHIAILNNNKEIFKL 243

                          170
                   ....*....|....
gi 1953314652 1223 LLDMGSDINAQIET 1236
Cdd:PHA03100   244 LLNNGPSIKTIIET 257
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1084-1297 1.19e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.19  E-value: 1.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1084 LVSVLIARDAKIEHRDKKGFTPLILAATAGH-VGVVEILLDKGGDIEAqSERTKDTPLSLACSGGR-QEVVDLLLARGAN 1161
Cdd:PHA02876   289 LVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNA-ADRLYITPLHQASTLDRnKDIVITLLELGAN 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1162 KEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgSKLGISplMLAAMNGHVP--AVKLLLDMGSDINAQiETNRN 1239
Cdd:PHA02876   368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS-QKIGTA--LHFALCGTNPymSVKTLIDRGANVNSK-NKDLS 443

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953314652 1240 TALTLACFQG-RAEVVSLLLDRKANVEHRAKTGLTPLMEAAsgGYAEVGRVLLDKGADV 1297
Cdd:PHA02876   444 TPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 278-528 1.38e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.58  E-value: 1.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  278 GYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGAnIEDHNENG-HTPLMEAASAGHVEVARVLLDHG 356
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  357 AGINTHSNEFKESALTLACYKGHLDMVRFLLDAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 436
Cdd:PHA02875    92 KFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  437 LTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHE-EMVALLLAQGANINAQTEETQETALTLA-----CCG 510
Cdd:PHA02875   172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNIMFMIEGEECTILDmicnmCTN 251

                          250
                   ....*....|....*...
gi 1953314652  511 GFSEVADFLIkagADIEL 528
Cdd:PHA02875   252 LESEAIDALI---ADIAI 266
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 1714-1778 1.96e-15

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: 72.70  E-value: 1.96e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINA 1778
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1071-1263 2.06e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.19  E-value: 2.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1071 TALTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTKDTPLSLACSGGRQE 1150
Cdd:PHA02875    37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLD 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1151 VVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGskLGISPLMLAAMNGHVPAVKLLLDMGSDI 1230
Cdd:PHA02875   117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC--CGCTPLIIAMAKGDIAICKMLLDSGANI 194

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1953314652 1231 NAqieTNRNTALTLACF---QGRAEVVSLLLDRKAN 1263
Cdd:PHA02875   195 DY---FGKNGCVAALCYaieNNKIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 212-408 2.80e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.81  E-value: 2.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  212 DVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDA 291
Cdd:PHA02875    47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  292 DVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEFKESAL 371
Cdd:PHA02875   127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1953314652  372 TLACYKGHLDMVRFLLDAGADQEHKT---DEMHTALMEAC 408
Cdd:PHA02875   207 CYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDMIC 246
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 258-439 5.15e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.45  E-value: 5.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  258 NVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL 337
Cdd:PLN03192   516 NGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  338 MEAASAGHVEVARVLLDHGAGINTHSNefkESALTLACYKGHLDMVRFLLDAGADQEHKTDEMHTALMEACMDGHVEVAR 417
Cdd:PLN03192   596 WNAISAKHHKIFRILYHFASISDPHAA---GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672

                          170       180
                   ....*....|....*....|...
gi 1953314652  418 LLLDSGAQVN-MPADSFESPLTL 439
Cdd:PLN03192   673 LLIMNGADVDkANTDDDFSPTEL 695
Ank_2 pfam12796
Ankyrin repeats (3 copies);
619-704 1.15e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 1.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  619 LMKAARAGHLCTVQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTNVV 698
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77


                   ....*.
gi 1953314652  699 SYLLDY 704
Cdd:pfam12796   78 KLLLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1138-1330 1.51e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.49  E-value: 1.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1138 TPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSrTGSKLGISPLMLAAMNGHV 1217
Cdd:PHA02875    37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADD-VFYKDGMTPLHLATILKKL 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1218 PAVKLLLDMGSDINAQiETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADV 1297
Cdd:PHA02875   116 DIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1953314652 1298 N----APPVpssrdTALTIAADKGHYKFCELLINRGA 1330
Cdd:PHA02875   195 DyfgkNGCV-----AALCYAIENNKIDIVRLFIKRGA 226
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 1715-1777 2.29e-14

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: 69.63  E-value: 2.29e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1715 KKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLIN 1777
Cdd:cd00105      1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGERVVTITGTPEAVEKAKELIE 63
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1143-1364 2.74e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 2.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1143 ACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGsklGI-SPLMLAAMNGHVPAVK 1221
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIeSELHDAVEEGDVKAVE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1222 LLLDMGSDINAQIETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPP 1301
Cdd:PHA02875    86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1302 VPSSrdTALTIAADKGHYKFCELLINRGAHIDVRNKKGN-TPLWLASNGGHFDVVQLLVQAGAD 1364
Cdd:PHA02875   166 CCGC--TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 480-712 3.50e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 3.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  480 EMVALLLAQGANINaQTEETQETALT--LAC-CGGFSEVADFLIKAGADIEL----GCsTPL---MEASQEghLELVKYL 549
Cdd:PHA03095    28 EEVRRLLAAGADVN-FRGEYGKTPLHlyLHYsSEKVKDIVRLLLEAGADVNApercGF-TPLhlyLYNATT--LDVIKLL 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  550 LAAGANVHATTATGDTAL-TYAC-ENGHTDVADVLLQAGADLdkqEDMKtilegidpakhqehesEGGRTPL---MKAAR 624
Cdd:PHA03095   104 IKAGADVNAKDKVGRTPLhVYLSgFNINPKVIRLLLRKGADV---NALD----------------LYGMTPLavlLKSRN 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  625 AgHLCTVQFLISKGANV-----NRATANNDHTVVSLACAgghlAVVELLLAHGADPTHRLKDGSTMLIEAAKGG---HTN 696
Cdd:PHA03095   165 A-NVELLRLLIDAGADVyavddRFRSLLHHHLQSFKPRA----RIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSL 239

                          250       260
                   ....*....|....*....|.
gi 1953314652  697 VVSYLL-----DYPNNVLSVP 712
Cdd:PHA03095   240 VLPLLIagisiNARNRYGQTP 260
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1064-1408 5.86e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.23  E-value: 5.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1064 HTESNHDTALTLACAGGHE-------ELVSVLIARDAKIEHRDKKGFTPL-ILAATAGHVGVVEILLDKGGDIEAQSERT 1135
Cdd:PHA02878    25 HTENYSTSASLIPFIPLHQavearnlDVVKSLLTRGHNVNQPDHRDLTPLhIICKEPNKLGMKEMIRSINKCSVFYTLVA 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1136 kdtpLSLACSGGRQEVVDLLLARGANKEHrnVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRTGSKLGiSPLMLAAM 1213
Cdd:PHA02878   105 ----IKDAFNNRNVEIFKIILTNRYKNIQ--TIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRHKGN-TALHYATE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1214 NGHVPAVKLLLDMGSDINAQIETNrNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMeaASGGYA---EVGRVL 1290
Cdd:PHA02878   178 NKDQRLTELLLSYGANVNIPDKTN-NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH--ISVGYCkdyDILKLL 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1291 LDKGADVNAppvpssRDTALTIAAdkghykfcellinrgAHIDVRNKkgntplwlasngghfDVVQLLVQAGADVDAADN 1370
Cdd:PHA02878   255 LEHGVDVNA------KSYILGLTA---------------LHSSIKSE---------------RKLKLLLEYGADINSLNS 298

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1953314652 1371 RKITPLMSAfrkghvkVVQYLVKEV-NQFPSDIECMRYI 1408
Cdd:PHA02878   299 YKLTPLSSA-------VKQYLCINIgRILISNICLLKRI 330
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1060-1302 5.97e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 5.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1060 DIDAhTESNHDTAL-TLACAGGHEELVSVLIARDAKIEHRDKKGFTPL--ILAATAGHVGVVEILLDKGGDIEAQSERTK 1136
Cdd:PHA03095    75 DVNA-PERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGM 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1137 dTPLS--------------LACSGG-----------------------RQEVVDLLLARGANKEHRNVSDYTPLSLAASG 1179
Cdd:PHA03095   154 -TPLAvllksrnanvellrLLIDAGadvyavddrfrsllhhhlqsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1180 GYVNIIKI--LLNAGAEINSRtgSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQIETNrNTALTLACFQGRAEVVSLL 1257
Cdd:PHA03095   233 SSCKRSLVlpLLIAGISINAR--NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG-NTPLSLMVRNNNGRAVRAA 309

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1258 LDRKANVEHRAKTgLTPLMEAASGGYAEVGR-----VLLDKGADVNAPPV 1302
Cdd:PHA03095   310 LAKNPSAETVAAT-LNTASVAGGDIPSDATRlcvakVVLRGAFSLLPEPI 358
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1151-1405 2.35e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.87  E-value: 2.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1151 VVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHVPAVKLLLDMGSDI 1230
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD--DLSVLECAVDSKNIDTIKAIIDNRSNI 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1231 NAQ----IETNRNTALtlacfqgraEVVSLLLDRKANVEHRAKTGLTPLMEAASG-GYAEVGRVLLDKGADVNAPPVPSs 1305
Cdd:PHA02876   238 NKNdlslLKAIRNEDL---------ETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKG- 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1306 rDTALTIAADKGH-YKFCELLINRGAHIDVRNKKGNTPLWLASNGGHF-DVVQLLVQAGADVDAADNRKITPLMSAFRKG 1383
Cdd:PHA02876   308 -ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                          250       260
                   ....*....|....*....|..
gi 1953314652 1384 HVKVVQYLVkevnQFPSDIECM 1405
Cdd:PHA02876   387 NVVIINTLL----DYGADIEAL 404
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
 1716-1780 5.73e-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: 65.73  E-value: 5.73e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22462      2 EILIPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDSATGERIVLISGTPDQARHAQNLIEAFI 66
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1176-1393 1.09e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.72  E-value: 1.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1176 AASGGYVNIIKILLNAGaeINSRTGSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQIETNRnTALTLACFQGRAEVVS 1255
Cdd:PHA02875     9 AILFGELDIARRLLDIG--INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDVKAVE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1256 LLLDRKANVEHRA-KTGLTPLMEAASGGYAEVGRVLLDKGADvnaPPVPSS-RDTALTIAADKGHYKFCELLINRGAHID 1333
Cdd:PHA02875    86 ELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGAD---PDIPNTdKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652 1334 VRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRK-ITPLMSAFRKGHVKVVQYLVK 1393
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 313-590 3.39e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 3.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  313 VDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLdhgAGINTHSNEFKESALTLACYKGHLDMVRFLLDAGAD 392
Cdd:PHA02878    50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYK 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  393 QEHKTDEMHtaLMEACMDGHVE--VARLLLDSGAQVNM-PADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTP 469
Cdd:PHA02878   127 NIQTIDLVY--IDKKSKDDIIEaeITKLLLSYGADINMkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  470 LMEAAREGHEEMVALLLAQGANINAQTEetqetaltlacCGgfsevadflikagadielgcSTPL-MEASQEGHLELVKY 548
Cdd:PHA02878   205 LHHAVKHYNKPIVHILLENGASTDARDK-----------CG--------------------NTPLhISVGYCKDYDILKL 253

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1953314652  549 LLAAGANVHA-TTATGDTALTYACENghTDVADVLLQAGADLD 590
Cdd:PHA02878   254 LLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADIN 294
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 413-591 3.58e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.21  E-value: 3.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  413 VEVARLLLDSGAQVNMPADSFeSPLTLAACGGHVELAALLieRGANLEEVND-EGYTPLMEAAREGHEEMVALLLAQGAN 491
Cdd:PLN03192   507 LNVGDLLGDNGGEHDDPNMAS-NLLTVASTGNAALLEELL--KAKLDPDIGDsKGRTPLHIAASKGYEDCVLVLLKHACN 583

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  492 INAQtEETQETALTLACCGGFSEVADFLIK--------AGADIelgcstpLMEASQEGHLELVKYLLAAGANVHATTATG 563
Cdd:PLN03192   584 VHIR-DANGNTALWNAISAKHHKIFRILYHfasisdphAAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655

                          170       180
                   ....*....|....*....|....*...
gi 1953314652  564 DTALTYACENGHTDVADVLLQAGADLDK 591
Cdd:PLN03192   656 ATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 270-526 4.71e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.06  E-value: 4.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  270 PLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEgaNIEDHNENGHTPLMEAASAGHVEVA 349
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  350 RVLLdhgagINTHSNEfKESALTLACYKGHLD-----MVRFLLDAGADQEHKT-DEMHTALMEACMDGHVEVARLLLDSG 423
Cdd:PHA02878   118 KIIL-----TNRYKNI-QTIDLVYIDKKSKDDiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  424 AQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL-MEAAREGHEEMVALLLAQGANINAQTEETQET 502
Cdd:PHA02878   192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLT 271

                          250       260
                   ....*....|....*....|....
gi 1953314652  503 ALTLACCGgfSEVADFLIKAGADI 526
Cdd:PHA02878   272 ALHSSIKS--ERKLKLLLEYGADI 293
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1055-1131 1.03e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 1.03e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652 1055 VYPSVDIDaHTESNHDTALTLACAGGHEELVSVLIARdAKIEHRDkKGFTPLILAATAGHVGVVEILLDKGGDIEAQ 1131
Cdd:pfam12796   17 LENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 202-392 1.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.52  E-value: 1.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  202 RSLAEACSDGDVNAVRKLLdegrsVNEHTEEGESLLCLACSAGY-----YELAQVLLAMHANVEDRGNKGDITPLMAASS 276
Cdd:PHA02878   103 VAIKDAFNNRNVEIFKIIL-----TNRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  277 GGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL-MEAASAGHVEVARVLLDH 355
Cdd:PHA02878   178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1953314652  356 GAGINTHSNEFKESALTLACYKGhlDMVRFLLDAGAD 392
Cdd:PHA02878   258 GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGAD 292
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1237-1393 1.54e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.25  E-value: 1.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1237 NRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGA--DVNAPPVPSSrdtaLTIAA 1314
Cdd:PHA02875     1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIESE----LHDAV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1315 DKGHYKFCELLINRGAHI-DVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQYLVK 1393
Cdd:PHA02875    77 EEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 398-691 2.31e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 2.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  398 DEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAnleevnDEGYTPLMEAareg 477
Cdd:PHA02874    33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGV------DTSILPIPCI---- 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  478 HEEMVALLLAQGANINAQTEETQeTALTLACCGGFSEVADFLIKAGADIEL----GCsTPLMEASQEGHLELVKYLLAAG 553
Cdd:PHA02874   103 EKDMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIeddnGC-YPIHIAIKHNFFDIIKLLLEKG 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  554 ANVHATTATGDTALTYACENGhtdvadvllqagadldkqeDMKTILEGIDPAKHQEHESEGGRTPLMKAARAGHlCTVQF 633
Cdd:PHA02874   181 AYANVKDNNGESPLHNAAEYG-------------------DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIEL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652  634 LISKgANVNRATANND---HTVVSLACAgghLAVVELLLAHGADPTHRLKDGSTMLIEAAK 691
Cdd:PHA02874   241 LINN-ASINDQDIDGStplHHAINPPCD---IDIIDILLYHKADISIKDNKGENPIDTAFK 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 403-674 2.47e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.48  E-value: 2.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  403 ALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAnLEEVNDEGY-TPLMEAAREGHEEM 481
Cdd:PHA02875     5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  482 VALLLAQGANINaqteetqetaltlaccggfsevaDFLIKAGadielgcSTPLMEASQEGHLELVKYLLAAGANVHATTA 561
Cdd:PHA02875    84 VEELLDLGKFAD-----------------------DVFYKDG-------MTPLHLATILKKLDIMKLLIARGADPDIPNT 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  562 TGDTALTYACENGHTDVADVLLQAGADLDKQEDMktilegidpakhqehesegGRTPLMKAARAGHLCTVQFLISKGANV 641
Cdd:PHA02875   134 DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC-------------------GCTPLIIAMAKGDIAICKMLLDSGANI 194

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1953314652  642 NRATANNDHTVVSLACAGGHLAVVELLLAHGAD 674
Cdd:PHA02875   195 DYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 335-507 5.59e-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: 68.12  E-value: 5.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  335 TPLMEAASAGHVEVARVLLdhgagINTHSNEFK-----ESALTLACYKGHLDMVRFLLDAGAD--QEHKTDEMH---TAL 404
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLL-----KCPSCDLFQrgalgETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTAL 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  405 MEACMDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL 470
Cdd:cd22192     94 HIAVVNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1953314652  471 ----MEAAREGHEEMVALLLAQGANINAQTEETQE-----TALTLA 507
Cdd:cd22192    174 hilvLQPNKTFACQMYDLILSYDKEDDLQPLDLVPnnqglTPFKLA 219
Ank_4 pfam13637
Ankyrin repeats (many copies);
530-583 6.07e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 6.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652  530 CSTPLMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLL 583
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 280-497 6.25e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 67.55  E-value: 6.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  280 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFV---DIVKVLLNEGANIEDHNENGHTPLMEAASAGH---VEVARVLL 353
Cdd:PHA02798    89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  354 DHGAGINTHSNEFKESalTLACY------KGHLDMVRFLLDAG-----ADQEHKTDemhtaLMEACMDghvevarLLLDS 422
Cdd:PHA02798   169 EKGVDINTHNNKEKYD--TLHCYfkynidRIDADILKLFVDNGfiinkENKSHKKK-----FMEYLNS-------LLYDN 234

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652  423 GaqvNMPADSFEspltlaacgghvelaalLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTE 497
Cdd:PHA02798   235 K---RFKKNILD-----------------FIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
 1714-1779 1.20e-10

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: 59.17  E-value: 1.20e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINAL 1779
Cdd:cd22439      3 TQEITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEDGSTERSVTITGTPEAVSLAQYLINAR 68
Ank_2 pfam12796
Ankyrin repeats (3 copies);
655-706 1.29e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 1.29e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953314652  655 LACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVVSYLLDYPN 706
Cdd:pfam12796    3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 204-440 2.46e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 2.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  204 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAG-----------------YYELAQVLLAMH---------- 256
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPnklgmkemirsinkcsvFYTLVAIKDAFNnrnveifkii 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  257 -ANVEDRGNKGDITPLMAASSGGYLD--IVKLLLLHDADVNSQSA-TGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 332
Cdd:PHA02878   121 lTNRYKNIQTIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  333 GHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLAC-YKGHLDMVRFLLDAGADQEHKTDEMH-TALMEACMD 410
Cdd:PHA02878   201 NNSPLHHAVKHYNKPIVHILLENGASTD-ARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKS 279

                          250       260       270
                   ....*....|....*....|....*....|
gi 1953314652  411 GhvEVARLLLDSGAQVNMPADSFESPLTLA 440
Cdd:PHA02878   280 E--RKLKLLLEYGADINSLNSYKLTPLSSA 307
KH-I_TDRKH_rpt2 cd22429
second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
 1714-1790 2.70e-10

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: 58.89  E-value: 2.70e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGE--RMITIRGgtesTRYAVQLINALIQDPAKELEDL 1790
Cdd:cd22429      3 TEELHVPQRAVGRIIGRGGETIRSICRTSGAKVKCDRESDDTLDlvRLITITG----TKKEVDAAKSLILEKVSEEEEF 77
KH smart00322
K homology RNA-binding domain;
1716-1780 2.79e-10

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 58.08  E-value: 2.79e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652  1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDkqKDKNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIP--GPGSEERVVEITGPPENVEKAAELILEIL 68
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 201-364 4.24e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 4.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  201 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLL-------------------------AM 255
Cdd:PHA02874    36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdmiktildcGI 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  256 HANVEDRGNKgdiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHT 335
Cdd:PHA02874   116 DVNIKDAELK---TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                          170       180
                   ....*....|....*....|....*....
gi 1953314652  336 PLMEAASAGHVEVARVLLDHGAGINTHSN 364
Cdd:PHA02874   193 PLHNAAEYGDYACIKLLIDHGNHIMNKCK 221
Ank_4 pfam13637
Ankyrin repeats (many copies);
333-387 4.87e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 4.87e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652  333 GHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKGHLDMVRFLL 387
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
1339-1392 7.21e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 7.21e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1339 GNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQYLV 1392
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
269-320 7.28e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 7.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953314652  269 TPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLL 320
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 211-332 1.04e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 1.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  211 GDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR--------------GNKGDiTPLM 272
Cdd:PHA03100   119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsygvpinikDVYGF-TPLH 197

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  273 AASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 332
Cdd:PHA03100   198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1343-1397 1.18e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 1.18e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652 1343 LWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQYLVKEVNQ 1397
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV 55
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 504-655 1.38e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  504 LTLACCGGfSEVADFLIKAGADIELGCS---TPLMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVAD 580
Cdd:PLN03192   530 LTVASTGN-AALLEELLKAKLDPDIGDSkgrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  581 VLLQ--------AGADL----DKQEDMKTILEGIDPAKHQEHESEGGRTPLMKAARAGHLCTVQFLISKGANVNRATANN 648
Cdd:PLN03192   609 ILYHfasisdphAAGDLlctaAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688


                   ....*..
gi 1953314652  649 DHTVVSL 655
Cdd:PLN03192   689 DFSPTEL 695
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1206-1369 1.88e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.35  E-value: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1206 SPLMLAAMNGHVPAVKLLLDMGSDINAQIETNRnTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAE 1285
Cdd:PLN03192   527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1286 VGRVLLDKGADVNappvPSSRDTALTIAADKGHYKFCELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADV 1365
Cdd:PLN03192   606 IFRILYHFASISD----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681


                   ....
gi 1953314652 1366 DAAD 1369
Cdd:PLN03192   682 DKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
1306-1359 1.97e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.97e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1306 RDTALTIAADKGHYKFCELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLV 1359
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
435-486 4.28e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 4.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953314652  435 SPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLL 486
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 531-686 4.29e-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: 61.95  E-value: 4.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  531 STPLMEASQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDKQEDMKTILEgidpakhqe 609
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLYQ--------- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  610 hesegGRTPLMKAARAGHLCTVQFLISKGANVN--RATAN------------NDHTVVSLACAgGHLAVVELLLAHGADP 675
Cdd:cd22192     89 -----GETALHIAVVNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEHPLSFAACV-GNEEIVRLLIEHGADI 162

                          170
                   ....*....|.
gi 1953314652  676 THRLKDGSTML 686
Cdd:cd22192    163 RAQDSLGNTVL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 199-340 5.11e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 5.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  199 VDTRSLAEACSDGDVnaVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDItPLMAASSGG 278
Cdd:PHA02874    92 VDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY-PIHIAIKHN 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652  279 YLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEA 340
Cdd:PHA02874   169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
651-702 8.57e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 8.57e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953314652  651 TVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVVSYLL 702
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
 1715-1780 9.07e-09

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: 54.26  E-value: 9.07e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1715 KKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQ--KDKNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22428      7 IEMKVPREAVGLIIGRQGATIKQIQKETGARIDFKDEgsGGELPERVLLIQGNPVQAQRAEEAIHQII 74
Ank_4 pfam13637
Ankyrin repeats (many copies);
400-453 1.11e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.11e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652  400 MHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLI 453
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1171-1360 1.16e-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: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1171 TPLSLAASGGYVNIIKILL-NAGAEINSRtGSkLGISPLMLAAMNGHVPAVKLLLD---------MGSDINAQietnrNT 1240
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQR-GA-LGETALHVAALYDNLEAAVVLMEaapelvnepMTSDLYQG-----ET 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1241 ALTLACFQGRAEVVSLLLDRKANVE---------HRAKTGLT-----PLMEAASGGYAEVGRVLLDKGADVNAppvpssR 1306
Cdd:cd22192     92 ALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRA------Q 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1307 D----TALTIAADKGHYKF-CE---LLINRGAHID------VRNKKGNTPLWLASNGGHFDVVQLLVQ 1360
Cdd:cd22192    166 DslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
 1715-1776 1.29e-08

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: 53.23  E-value: 1.29e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1715 KKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQK-DKNGERMITIRGGTESTRYAVQLI 1776
Cdd:cd22457      1 QNISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAKAPhDETGERMFTITGTPEANDRALRLL 63
KH-I_FUBP_rpt4 cd22399
fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 1718-1777 1.36e-08

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: 53.38  E-value: 1.36e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652 1718 SVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKN-GERMITIRGGTESTRYAVQLIN 1777
Cdd:cd22399      5 LVPANKCGLVIGKGGETIRQINQQSGAHVELDRNPPPNpNEKLFIIRGNPQQIEHAKQLIR 65
KH-I_NOVA_rpt3 cd09031
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
 1715-1776 1.40e-08

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: 53.35  E-value: 1.40e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652 1715 KKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKD-----KNgeRMITIRGGTESTRYAVQLI 1776
Cdd:cd09031      3 IELEVPENLVGAILGKGGKTLVEIQELTGARIQISKKGEfvpgtRN--RKVTITGTPAAVQAAQYLI 67
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1175-1277 1.85e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 1.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1175 LAASGGYVNIiKILLNAGAEINSRTGSklGISPLMLAAMNGHVPAVKLLLDMGSDINAqIETNRNTALTLACFQGRAEVV 1254
Cdd:PTZ00322    89 LAASGDAVGA-RILLTGGADPNCRDYD--GRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVV 164

                           90       100       110
                   ....*....|....*....|....*....|
gi 1953314652 1255 SLLL-------DRKANVEHRAKTGLTPLME 1277
Cdd:PTZ00322   165 QLLSrhsqchfELGANAKPDSFTGKPPSLE 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
300-353 2.19e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 2.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652  300 GNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLL 353
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 279-584 2.36e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 59.37  E-value: 2.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  279 YLDIVKLLLLHDADVNSQSaTGNTALTYACAGGFV--DIVKVLLNEGANIedhNENGH--TPL------MEAASAGHVEV 348
Cdd:PHA02989    15 DKNALEFLLRTGFDVNEEY-RGNSILLLYLKRKDVkiKIVKLLIDNGADV---NYKGYieTPLcavlrnREITSNKIKKI 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  349 ARVLLDHGAGINTHSneFKESAlTLAC--YKGH---LDMVRFLLDAGADQEHKTDE-----MHTALmEACMDgHVEVARL 418
Cdd:PHA02989    91 VKLLLKFGADINLKT--FNGVS-PIVCfiYNSNinnCDMLRFLLSKGINVNDVKNSrgynlLHMYL-ESFSV-KKDVIKI 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  419 LLDSGAQVNMPADSFE-SPLTL----AACGGHVELAALLIERGANLEEvNDEGYTPLMEAAREGHEEMValllaqganin 493
Cdd:PHA02989   166 LLSFGVNLFEKTSLYGlTPMNIylrnDIDVISIKVIKYLIKKGVNIET-NNNGSESVLESFLDNNKILS----------- 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  494 aqteeTQETaltlaccggfsEVADFL---IKAGADIELGCsTPLMEASQEGHLELVKYLLAAGANVHATTATGDTALTYA 570
Cdd:PHA02989   234 -----KKEF-----------KVLNFIlkyIKINKKDKKGF-NPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296

                          330
                   ....*....|....
gi 1953314652  571 CENGHTDVADVLLQ 584
Cdd:PHA02989   297 IKHGNIDMLNRILQ 310
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1206-1393 2.51e-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: 59.26  E-value: 2.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1206 SPLMLAAMNGHVPAVKLLLDMGSDINAQIETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKT-----GLTPLMEAAS 1280
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1281 GGYAEVGRVLLDKGADVNAPPV------PSSR------DTALTIAADKGHYKFCELLINRGAHIDVRNKKGNTPLwlasn 1348
Cdd:cd22192     99 NQNLNLVRELIARGADVVSPRAtgtffrPGPKnliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL----- 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1349 ggHFDVVQ------------LLVQAGADVDAA-----DNRKITPLMSAFRKGHVKVVQYLVK 1393
Cdd:cd22192    174 --HILVLQpnktfacqmydlILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQ 233
KH-I_NOVA_rpt2 cd22436
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
 1716-1776 5.75e-08

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: 51.85  E-value: 5.75e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNG--ERMITIRGGTESTRYAVQLI 1776
Cdd:cd22436      4 KILVPNSTAGMIIGKGGATIKAIMEQSGARVQISQKPESINlqERVVTVTGEPEANRKAVSLI 66
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1712-1782 6.55e-08

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


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 52.02  E-value: 6.55e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953314652 1712 RRSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQK-------DKNGERM-ITIRGGTESTRYAVQLINALIQD 1782
Cdd:cd22446      6 KVTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNeegnydeDDDDETVeISIEGDAEGVELAKKEIEAIVKE 84
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 444-709 7.20e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 7.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  444 GHVELAALLIERGANLEEVN-DEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTlACCGGFSEVADFLIKA 522
Cdd:PHA02874    12 GDIEAIEKIIKNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLT-AIKIGAHDIIKLLIDN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  523 GADIELgCSTPLMEAsqeghlELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDKQEDmktilegi 602
Cdd:PHA02874    91 GVDTSI-LPIPCIEK------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD-------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  603 dpakhqeheseGGRTPLMKAARAGHLCTVQFLISKGANVNratANNDHtvvslacagghlavvelllahgadpthrlkdG 682
Cdd:PHA02874   156 -----------NGCYPIHIAIKHNFFDIIKLLLEKGAYAN---VKDNN-------------------------------G 190

                          250       260
                   ....*....|....*....|....*..
gi 1953314652  683 STMLIEAAKGGHTNVVSYLLDYPNNVL 709
Cdd:PHA02874   191 ESPLHNAAEYGDYACIKLLIDHGNHIM 217
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 1719-1780 7.65e-08

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: 51.49  E-value: 7.65e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1719 VPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22396      7 VPDKMVGLIIGRGGEQINRLQAESGAKIQIAPDSGGLPERPCTLTGTPDAIETAKRLIDQIV 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
466-520 7.91e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 7.91e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652  466 GYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFLI 520
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 1150-1388 9.12e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 57.44  E-value: 9.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1150 EVVDLLLARGANKEHRNVSDyTPL------SLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHVPAV--- 1220
Cdd:PHA02989    51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFN--GVSPIVCFIYNSNINNCdml 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1221 KLLLDMGSDINAQIETNRNTAL--TLACFQGRAEVVSLLLDRKANV-EHRAKTGLTP----LMEAASGGYAEVGRVLLDK 1293
Cdd:PHA02989   128 RFLLSKGINVNDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKK 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1294 GADVNAPPVPSSRDTALTIAADKGHYKFCELLIN---RGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADN 1370
Cdd:PHA02989   208 GVNIETNNNGSESVLESFLDNNKILSKKEFKVLNfilKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSK 287

                          250
                   ....*....|....*...
gi 1953314652 1371 RKITPLMSAFRKGHVKVV 1388
Cdd:PHA02989   288 DGDTVLTYAIKHGNIDML 305
Ank_4 pfam13637
Ankyrin repeats (many copies);
1206-1258 1.29e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 1.29e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1206 SPLMLAAMNGHVPAVKLLLDMGSDINAQIEtNRNTALTLACFQGRAEVVSLLL 1258
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
369-420 1.36e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 1.36e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953314652  369 SALTLACYKGHLDMVRFLLDAGADQEHKTDEMHTALMEACMDGHVEVARLLL 420
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1060-1230 1.43e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 1.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1060 DIDAhTESNHDTALTLACA-GGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTkDT 1138
Cdd:PHA02876   333 DVNA-ADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKI-GT 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1139 PLSLACSGGRQEV-VDLLLARGANKEHRNVSDYTPLSLAASGG-YVNIIKILLNAGAEINSrtgskLGIS---PLMLAAm 1213
Cdd:PHA02876   411 ALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA-----INIQnqyPLLIAL- 484

                          170
                   ....*....|....*..
gi 1953314652 1214 nGHVPAVKLLLDMGSDI 1230
Cdd:PHA02876   485 -EYHGIVNILLHYGAEL 500
Ank_4 pfam13637
Ankyrin repeats (many copies);
1069-1122 1.47e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 1.47e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1069 HDTALTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILL 1122
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_IGF2BP_rpt4 cd22403
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
 1717-1775 1.73e-07

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: 50.32  E-value: 1.73e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652 1717 LSVPASVVSRIMGRGGCNITAIQDVTGAHIDV--DKQKDKNGERMITIRGgtesTRYAVQL 1775
Cdd:cd22403      4 IRVPSSMVGRIIGKGGQNVRELQRLTGAIIKLprDQTPDEGDEVPVEIIG----NFYATQS 60
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 619-741 2.15e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 2.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  619 LMKAARAGHLCTVQFLISKGANVNrATANNDHTVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVV 698
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652  699 SYLLDY------------PNNVLSVPTT-DVSQLTSSSQDQSQVPRVPMHTLAMVV 741
Cdd:PTZ00322   165 QLLSRHsqchfelganakPDSFTGKPPSlEDSPISSHHPDFSAVPQPMMGSLIVIM 220
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1227-1392 2.86e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 2.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1227 GSDINAQIETNRNTALTLacfqGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSsr 1306
Cdd:PLN03192   518 GEHDDPNMASNLLTVAST----GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG-- 591

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1307 DTALTIAADKGHYKFCELLINRgAHIDVRNKKGNTpLWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVK 1386
Cdd:PLN03192   592 NTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669


                   ....*.
gi 1953314652 1387 VVQYLV 1392
Cdd:PLN03192   670 MVRLLI 675
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 203-373 3.04e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  203 SLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDI 282
Cdd:PLN03192   528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN-TALWNAISAKHHKI 606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  283 VKlLLLHDADVNSQSATGNTaLTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGInTH 362
Cdd:PLN03192   607 FR-ILYHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV-DK 683

                          170
                   ....*....|..
gi 1953314652  363 SNEFKE-SALTL 373
Cdd:PLN03192   684 ANTDDDfSPTEL 695
KH-I_IGF2BP_rpt1 cd22400
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
 1716-1776 3.35e-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: 49.58  E-value: 3.35e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKqKDKNG--ERMITIRGGTESTRYAVQLI 1776
Cdd:cd22400      3 RILVPSEFVGAIIGKGGATIRQITQQTGARIDIHR-KENAGaaEKAITIYGTPEGCSSACKQI 64
Ank_4 pfam13637
Ankyrin repeats (many copies);
615-669 3.72e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 3.72e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652  615 GRTPLMKAARAGHLCTVQFLISKGANVNRATANNDhTVVSLACAGGHLAVVELLL 669
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 515-713 4.24e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 4.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  515 VADFLIKAGADI---ELGCSTPLMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDK 591
Cdd:PHA02876   160 IAEMLLEGGADVnakDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  592 ----------QEDMKTILEGIDPAKHQEHESEGGRTPLMKAARAGHLCT-VQFLISKGANVNRATANNDHTVVSLACAGG 660
Cdd:PHA02876   240 ndlsllkairNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGY 319

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652  661 HLAVVELLLAHGAD----------PTH------RLKDGSTMLIEAakGGHTNVVSYLLDYP-------NNVLSVPT 713
Cdd:PHA02876   320 DTENIRTLIMLGADvnaadrlyitPLHqastldRNKDIVITLLEL--GANVNARDYCDKTPihyaavrNNVVIINT 393
Ank_4 pfam13637
Ankyrin repeats (many copies);
563-635 4.31e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 4.31e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953314652  563 GDTALTYACENGHTDVADVLLQAGADLDKQEDmktilegidpakhqeheseGGRTPLMKAARAGHLCTVQFLI 635
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-------------------NGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 514-839 5.59e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 5.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  514 EVADFLIK-AGADIELGCSTPLMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDkq 592
Cdd:PLN03192   508 NVGDLLGDnGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH-- 585

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  593 edmktiLEGIDpakhqehesegGRTPLMKAARAGHLCTVQFLiskganVNRATANNDHT---VVSLACAGGHLAVVELLL 669
Cdd:PLN03192   586 ------IRDAN-----------GNTALWNAISAKHHKIFRIL------YHFASISDPHAagdLLCTAAKRNDLTAMKELL 642

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  670 AHGADPTHRLKDGSTMLIEAAKGGHTNVVSYLLDYPNNVLSVPTTDvsQLTSSSQDQSQVPRVPMHTLAMV--VPPQEPD 747
Cdd:PLN03192   643 KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD--DFSPTELRELLQKRELGHSITIVdsVPADEPD 720

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  748 RTSQEsspallGVQKGTSKQKSSSLQVADQDVLPPFHPYQPLECIVEETeGKLNELgqrisaieKAQLKSLELIQGEPLN 827
Cdd:PLN03192   721 LGRDG------GSRPGRLQGTSSDNQCRPRVSIYKGHPLLRNERCCNEA-GKLINL--------PPSLEELKAIAGEKLG 785

                          330
                   ....*....|..
gi 1953314652  828 KDKIEELKKNRE 839
Cdd:PLN03192   786 FDARKAMVTNEE 797
Ank_4 pfam13637
Ankyrin repeats (many copies);
1170-1224 6.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 6.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652 1170 YTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHVPAVKLLL 1224
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGN--GETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 290-506 6.85e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 6.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  290 DADVNSQSATGNTALtyacaggfvdiVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINthsnefkes 369
Cdd:PLN03192   526 ASNLLTVASTGNAAL-----------LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH--------- 585

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  370 altlacykghldmvrfLLDAGADqehktdemhTALMEACMDGHVEVARLLLDSGAQVNMPADSfeSPLTLAACGGHVELA 449
Cdd:PLN03192   586 ----------------IRDANGN---------TALWNAISAKHHKIFRILYHFASISDPHAAG--DLLCTAAKRNDLTAM 638

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652  450 ALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTL 506
Cdd:PLN03192   639 KELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPTEL 695
KH-I_PCBP4_rpt3 cd22523
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
 1714-1778 7.60e-07

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: 48.35  E-value: 7.60e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINA 1778
Cdd:cd22523      3 SQEFLIPNDLIGCVIGRQGSKISEIRQMSGAHIKIGNQTEGTSERHVTITGSPVSITLAQYLITT 67
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1258-1393 7.98e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 7.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1258 LDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCE---LLINRGAHIDV 1334
Cdd:PHA03095     1 DEEDESVDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNA 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1335 RNKKGNTPLWL-ASNGGHFDVVQLLVQAGADVDAADNRKITPL---MSAFRKgHVKVVQYLVK 1393
Cdd:PHA03095    79 PERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvyLSGFNI-NPKVIRLLLR 140
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
 1713-1783 8.35e-07

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: 48.24  E-value: 8.35e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1713 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKqkdkngERMITIRGGT-ESTRYAVQLINALIQDP 1783
Cdd:cd02393      4 RITTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIED------DGTVTIFATDkESAEAAKAMIEDIVAEP 69
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1078-1156 1.04e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 1.04e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953314652 1078 AGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAqSERTKDTPLSLACSGGRQEVVDLLL 1156
Cdd:PTZ00322    91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLS 168
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1717-1780 1.08e-06

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: 48.57  E-value: 1.08e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1717 LSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNG------ERM--ITIRGGTESTRYAVQLINALI 1780
Cdd:cd22447      8 VPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAApadeddDTMveVTITGDEFNVQHAKQRIEEII 79
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
 1719-1780 1.49e-06

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: 47.70  E-value: 1.49e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1719 VPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22454     10 IPNADVGKVIGKGGETIKRIEALTDTVITFERVNGGSPNREVQITGSPDNVAAAKRLIEDTI 71
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
 1714-1789 1.56e-06

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: 47.70  E-value: 1.56e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTEstryavQLINA--LIQDPAKELED 1789
Cdd:cd22434      3 TTQVTIPKDLAGSIIGKGGQRIRQIRHESGASIKIDEPLPGSEDRIITITGTQD------QIQNAqyLLQNSVKQYSG 74
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1338-1370 1.95e-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: 46.13  E-value: 1.95e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1953314652 1338 KGNTPLWLAS-NGGHFDVVQLLVQAGADVDAADN 1370
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1716-1780 1.97e-06

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: 47.26  E-value: 1.97e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDkqkDKNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22449      7 KFDVPAKYVPHIIGKKGANINKLREEYGVKIDFE---DKTGEGNVEIKGSKKNVEEAKKRILSQI 68
Ank_5 pfam13857
Ankyrin repeats (many copies);
261-307 2.29e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 2.29e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1953314652  261 DRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYA 307
Cdd:pfam13857   10 NRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
 1716-1780 2.45e-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: 47.26  E-value: 2.45e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNG-ERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd02396      5 RLLVPASQCGSLIGKGGSKIKEIRESTGASVQVASEMLPNStERAVTISGSPEAITKCVEQICCVM 70
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
 1716-1778 2.47e-06

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: 47.22  E-value: 2.47e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDK---NGERMITIRGGTESTRYAVQLINA 1778
Cdd:cd22401      3 KILAHNNLCGRLIGKDGRNIKKIMEDTNTKITISSLQDLtsyNPERTITIKGSLEAMSEAESLISE 68
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 465-497 3.63e-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: 45.36  E-value: 3.63e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1953314652  465 EGYTPLMEAA-REGHEEMVALLLAQGANINAQTE 497
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1060-1248 3.74e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 3.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1060 DIDAHTESNHDTALTLACAGGHEELVSVLIARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKggdieaqsertkdtp 1139
Cdd:PHA02878   159 DINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN--------------- 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1140 lslacsggrqevvdlllarGANKEHRNVSDYTPLSLAAsgGYV---NIIKILLNAGAEINSRTgSKLGISPLMLAAMNGH 1216
Cdd:PHA02878   224 -------------------GASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKS-YILGLTALHSSIKSER 281

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1953314652 1217 VpaVKLLLDMGSDINAqIETNRNTALTLACFQ 1248
Cdd:PHA02878   282 K--LKLLLEYGADINS-LNSYKLTPLSSAVKQ 310
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1071-1190 4.36e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 4.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1071 TALTLACAGGHEELVSVLIARDAKIE---------HRDKK-----GFTPLILAATAGHVGVVEILLDKGGDIEAQsERTK 1136
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLG 169

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953314652 1137 DTPL---------SLACsggrqEVVDLLLARGANK-----EH-RNVSDYTPLSLAASGGYVNIIKILLN 1190
Cdd:cd22192    170 NTVLhilvlqpnkTFAC-----QMYDLILSYDKEDdlqplDLvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 307-460 5.04e-06

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: 52.01  E-value: 5.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  307 ACAGGFVDIVKVLLNEGA--NIEDHNENGHTPLMEAASAG-HVEVARVLLDHGAGINThsnefkESALTLACYKGHLDMV 383
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV------GDTLLHAISLEYVDAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  384 ----RFLLDAGADQ-------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ES 435
Cdd:TIGR00870   98 eailLHLLAAFRKSgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgES 177

                          170       180
                   ....*....|....*....|....*
gi 1953314652  436 PLTLAACGGHVELAALLIERGANLE 460
Cdd:TIGR00870  178 PLNAAACLGSPSIVALLSEDPADIL 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1275-1358 6.28e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 6.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1275 LMEAASGGYAEVGRVLLDKGADvnappvPSSRD----TALTIAADKGHYKFCELLINRGAHIDVRNKKGNTPLWLASNGG 1350
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGAD------PNCRDydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159


                   ....*...
gi 1953314652 1351 HFDVVQLL 1358
Cdd:PTZ00322   160 FREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1324-1391 6.49e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 6.49e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1324 LLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPLMSAFRKGHVKVVQYL 1391
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
1138-1189 6.59e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 6.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1138 TPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILL 1189
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 388-486 6.72e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 6.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  388 DAGADQEHKTDE------MHTALMEAC---MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAN 458
Cdd:PTZ00322    61 DATPDHNLTTEEvidpvvAHMLTVELCqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140

                           90       100
                   ....*....|....*....|....*...
gi 1953314652  459 LEEVNDEGYTPLMEAAREGHEEMVALLL 486
Cdd:PTZ00322   141 PTLLDKDGKTPLELAEENGFREVVQLLS 168
KH-I_FUBP2_rpt4 cd22488
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
 1717-1776 7.62e-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: 45.86  E-value: 7.62e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1717 LSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGE---RMITIRGGTESTRYAVQLI 1776
Cdd:cd22488      4 FSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQPPPNGDpnfKLFIIRGSPQQIDHAKQLI 66
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1060-1244 7.84e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 7.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1060 DIDAHTESNHDTALTLACAGGHEELVSVliARDAKIEhrDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQsERTKDTP 1139
Cdd:PLN03192   520 HDDPNMASNLLTVASTGNAALLEELLKA--KLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR-DANGNTA 594

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1140 LSLACSGGRQEVVDLLLARGANKEHRNVSDYtpLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHVPA 1219
Cdd:PLN03192   595 LWNAISAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSE--DHQGATALQVAMAEDHVDM 670

                          170       180
                   ....*....|....*....|....*
gi 1953314652 1220 VKLLLDMGSDINAQIETNRNTALTL 1244
Cdd:PLN03192   671 VRLLIMNGADVDKANTDDDFSPTEL 695
Ank_5 pfam13857
Ankyrin repeats (many copies);
352-404 8.36e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 8.36e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953314652  352 LLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLDAGADQEHKTDEMHTAL 404
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1717-1778 9.23e-06

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: 45.39  E-value: 9.23e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1717 LSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKqKDKNGErMITIRGGTESTRYAVQLINA 1778
Cdd:cd22452      6 IKVSPRYFGRIIGPGGSNINQIREKSGCFINVPK-KNKESD-VITLRGTKEGVEKAEEMIKK 65
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 212-487 9.80e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 50.90  E-value: 9.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  212 DVNAVRKLLDEGRSVNEhTEEGESLLCLACSAGYY--ELAQVLLAMHANVEDRGNKGdiTPLMAA------SSGGYLDIV 283
Cdd:PHA02989    15 DKNALEFLLRTGFDVNE-EYRGNSILLLYLKRKDVkiKIVKLLIDNGADVNYKGYIE--TPLCAVlrnreiTSNKIKKIV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  284 KLLLLHDADVNSQSATGNTALT---YACAGGFVDIVKVLLNEGANIED-HNENGHTPL---MEAASAgHVEVARVLLDHG 356
Cdd:PHA02989    92 KLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRFLLSKGINVNDvKNSRGYNLLhmyLESFSV-KKDVIKILLSFG 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  357 AGINTHSNEFKESALTLacYKGH------LDMVRFLLDAGADQEhKTDEMHTALMEACMDGH-------VEVARLLLdSG 423
Cdd:PHA02989   171 VNLFEKTSLYGLTPMNI--YLRNdidvisIKVIKYLIKKGVNIE-TNNNGSESVLESFLDNNkilskkeFKVLNFIL-KY 246

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953314652  424 AQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLA 487
Cdd:PHA02989   247 IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
1271-1326 9.86e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 9.86e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652 1271 GLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLI 1326
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1716-1782 9.89e-06

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: 45.28  E-value: 9.89e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVdKQKDKNGERMITIRGGTESTRYAVQLINALIQD 1782
Cdd:cd22417      4 TVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQF-PDKGDENDDEITITGYEKNAEAAKDAILKIVQE 69
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 1719-1780 1.29e-05

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: 44.94  E-value: 1.29e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1719 VPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22398      6 VPRFAVGVVIGKGGEMIKKIQNETGARVQFKPDDGNSPDRICVITGPPDQVQHAARMIQELI 67
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 465-494 1.33e-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: 43.73  E-value: 1.33e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1953314652   465 EGYTPLMEAAREGHEEMVALLLAQGANINA 494
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
KH-I_PCBP3_rpt3 cd22522
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
 1714-1778 1.38e-05

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: 45.10  E-value: 1.38e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINA 1778
Cdd:cd22522     10 THELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGSPANISLAQYLINA 74
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 332-360 1.41e-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: 43.73  E-value: 1.41e-05
                            10        20
                    ....*....|....*....|....*....
gi 1953314652   332 NGHTPLMEAASAGHVEVARVLLDHGAGIN 360
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
KH-I_NOVA_rpt1 cd22435
first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
 1716-1776 1.47e-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: 44.84  E-value: 1.47e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKD---KNGERMITIRGGTESTRYAVQLI 1776
Cdd:cd22435      5 KLLVPNYAAGSIIGKGGQTIAQLQKETGARIKLSKNNDfypGTTERVCLIQGEVEAVNAVLDFI 68
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 283-366 1.56e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  283 VKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLL-----DHGA 357
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqcHFEL 177


                   ....*....
gi 1953314652  358 GINTHSNEF 366
Cdd:PTZ00322   178 GANAKPDSF 186
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1117-1299 1.67e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1117 VVEILLDKGGDieaQSERTKDTPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 1196
Cdd:PLN03192   509 VGDLLGDNGGE---HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1197 SRTGSklGISPLMLAAMNGHVPAVKLLLDMGSDINAQIETNrntALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLM 1276
Cdd:PLN03192   586 IRDAN--GNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660

                          170       180
                   ....*....|....*....|...
gi 1953314652 1277 EAASGGYAEVGRVLLDKGADVNA 1299
Cdd:PLN03192   661 VAMAEDHVDMVRLLIMNGADVDK 683
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1204-1232 2.20e-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: 43.40  E-value: 2.20e-05
                           10        20
                   ....*....|....*....|....*....
gi 1953314652 1204 GISPLMLAAMNGHVPAVKLLLDMGSDINA 1232
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
 1716-1762 2.68e-05

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: 44.14  E-value: 2.68e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITI 1762
Cdd:cd22459      5 RLLCPVSKAGSVIGKGGEIIKQLRQETGARIKVEDGVPGTEERVITI 51
KH-I_PCBP1_2_rpt3 cd22521
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
 1714-1784 3.22e-05

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: 44.28  E-value: 3.22e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPA 1784
Cdd:cd22521      6 SHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINARLSSEK 76
Ank_5 pfam13857
Ankyrin repeats (many copies);
1090-1143 3.27e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 3.27e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1090 ARDAKIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTKdTPLSLA 1143
Cdd:pfam13857    4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 204-359 3.69e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.24  E-value: 3.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  204 LAEACSDGDVNAVRKLLdEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAmhaNVEDRGN--------KGDiTPLMA 273
Cdd:cd22192     21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLME---AAPELVNepmtsdlyQGE-TALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  274 ASSGGYLDIVKLLLLHDADVNSQSATGntalTYacaggFVDIVKVLLNEGanieDHnenghtPLMEAASAGHVEVARVLL 353
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVSPRATG----TF-----FRPGPKNLIYYG----EH------PLSFAACVGNEEIVRLLI 156


                   ....*.
gi 1953314652  354 DHGAGI 359
Cdd:cd22192    157 EHGADI 162
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
 1719-1776 4.19e-05

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: 43.66  E-value: 4.19e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1719 VPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLI 1776
Cdd:cd22395      6 VPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYTQNFQICSIEGTQQQIDKALKLI 63
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 337-441 4.86e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  337 LMEAASAGHVEVARVLLDHGAgiNTHSNEFKESA-LTLACYKGHLDMVRFLLDAGADQEHKTDEMHTALMEACMDGHVEV 415
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGA--DPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1953314652  416 ARLLL-----DSGAQVNMPADSF--------ESPLTLAA 441
Cdd:PTZ00322   164 VQLLSrhsqcHFELGANAKPDSFtgkppsleDSPISSHH 202
Ank_5 pfam13857
Ankyrin repeats (many copies);
452-507 5.04e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 5.04e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652  452 LIERG-ANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETqETALTLA 507
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1204-1232 6.85e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 6.85e-05
                            10        20
                    ....*....|....*....|....*....
gi 1953314652  1204 GISPLMLAAMNGHVPAVKLLLDMGSDINA 1232
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
KH-I_FUBP3_rpt4 cd22489
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
 1718-1777 7.07e-05

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: 42.99  E-value: 7.07e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1718 SVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGE---RMITIRGGTESTRYAVQLIN 1777
Cdd:cd22489      5 TIPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNTDpnvRIFTIRGVPQQIEHARQLID 67
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1117-1348 7.07e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.91  E-value: 7.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1117 VVEILLDKGGDIEAQsERTKDTPLSLACSGGRQ-----EVVDLLLARGANKEHRNVSDYTPLSLAASGGYVN---IIKIL 1188
Cdd:PHA02798    53 IVKLFINLGANVNGL-DNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINnleILLFM 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1189 LNAGAEINSRtgSKLGISPLMLAAMNGH---VPAVKLLLDMGSDINaqIETNRNTALTLACFQGR------AEVVSLLLD 1259
Cdd:PHA02798   132 IENGADTTLL--DKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDIN--THNNKEKYDTLHCYFKYnidridADILKLFVD 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1260 -----RKANVEHRAKtgLTPLMEAASGGYAEVGRVLLD---KGADVNAPPVPSSrdTALTIAADKGHYKFCELLINRGAH 1331
Cdd:PHA02798   208 ngfiiNKENKSHKKK--FMEYLNSLLYDNKRFKKNILDfifSYIDINQVDELGF--NPLYYSVSHNNRKIFEYLLQLGGD 283

                          250
                   ....*....|....*..
gi 1953314652 1332 IDVRNKKGNTPLWLASN 1348
Cdd:PHA02798   284 INIITELGNTCLFTAFE 300
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 383-452 7.63e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 7.63e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  383 VRFLLDAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALL 452
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 217-455 7.72e-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: 48.15  E-value: 7.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  217 RKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLL----AMHANVEDRGNKGDItpLMAASSGGYLDIVKLLLLHDAD 292
Cdd:TIGR00870    1 RGPLDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLeepkKLNINCPDRLGRSAL--FVAAIENENLELTELLLNLSCR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  293 VnsqsATGNTALtYACAGGFVDIVKVLLN-------EGANIEDHNEN-------GHTPLMEAASAGHVEVARVLLDHGAG 358
Cdd:TIGR00870   79 G----AVGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGAS 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  359 INT--HSNEFKESALT---------LACYK--GHLDMVRFLLDAGADQEhKTDEM-----HTALMEA------------C 408
Cdd:TIGR00870  154 VPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelscqM 232

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1953314652  409 MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 455
Cdd:TIGR00870  233 YNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 465-494 8.43e-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: 41.47  E-value: 8.43e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953314652  465 EGYTPLMEAAREGHEEMVALLLAQGANINA 494
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1204-1360 9.07e-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: 47.95  E-value: 9.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1204 GISPLMLAAMN---GHVPAVKLLLDMGSD-------INAQIETNR---NTALTLACFQGRAEVVSLLLDRKANVEHRA-- 1268
Cdd:cd21882     26 GKTCLHKAALNlndGVNEAIMLLLEAAPDsgnpkelVNAPCTDEFyqgQTALHIAIENRNLNLVRLLVENGADVSARAtg 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1269 ----KTGLT-------PLMEAASGGYAEVGRVLLDKGADvnaPPVPSSRDT-------ALTIAADK--GHYKFC----EL 1324
Cdd:cd21882    106 rffrKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQ---PAALEAQDSlgntvlhALVLQADNtpENSAFVcqmyNL 182

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1953314652 1325 LINRGAHID-------VRNKKGNTPLWLASNGGHFDVVQLLVQ 1360
Cdd:cd21882    183 LLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 563-591 9.10e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 9.10e-05
                            10        20
                    ....*....|....*....|....*....
gi 1953314652   563 GDTALTYACENGHTDVADVLLQAGADLDK 591
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 336-675 9.75e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 9.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  336 PLMEAASAGHVEVARVLLDHGAGINTHSNEFKeSALTLACYKGHLDMVRFLLdaGADQEHKTDEMHTALMEACMDGHVEV 415
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDL-TPLHIICKEPNKLGMKEMI--RSINKCSVFYTLVAIKDAFNNRNVEI 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  416 ARLLLdsgaqvnmpADSFESpltlaacgghvelaalliERGANLEEVNDEGYTPLMEAaregheEMVALLLAQGANINAQ 495
Cdd:PHA02878   117 FKIIL---------TNRYKN------------------IQTIDLVYIDKKSKDDIIEA------EITKLLLSYGADINMK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  496 TEETQetaltlaccggfsevadflikagadielgcSTPLMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACENGH 575
Cdd:PHA02878   164 DRHKG------------------------------NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  576 TDVADVLLQAGADLDkqedmktilegidpakhqeHESEGGRTPL-MKAARAGHLCTVQFLISKGANVNRATANNDHTVVS 654
Cdd:PHA02878   214 KPIVHILLENGASTD-------------------ARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALH 274

                          330       340
                   ....*....|....*....|.
gi 1953314652  655 LACAGGHlaVVELLLAHGADP 675
Cdd:PHA02878   275 SSIKSER--KLKLLLEYGADI 293
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1714-1777 9.85e-05

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: 42.19  E-value: 9.85e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVdkQKDKNGERMITIRGGTESTRYAVQLIN 1777
Cdd:cd22411      1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDL--PEENSDSDVITITGKKEDVEKARERIL 62
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 332-360 9.99e-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: 41.51  E-value: 9.99e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953314652  332 NGHTPLMEAA-SAGHVEVARVLLDHGAGIN 360
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
525-570 1.02e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1953314652  525 DIELGCSTPLMEASQEGHLELVKYLLAAGANVHATTATGDTALTYA 570
Cdd:pfam13857   11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
 1717-1782 1.02e-04

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: 42.27  E-value: 1.02e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652 1717 LSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDkngERMITIRGGTESTRYAVQLINALIQD 1782
Cdd:cd22430      4 FKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQ---EAEVKIFGSDEAQQKAKELIDELVGR 66
Ank_5 pfam13857
Ankyrin repeats (many copies);
285-337 1.04e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953314652  285 LLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL 337
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1797-2198 1.10e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1797 RTPASTKSIHANfSSGVGTTAASSKNAFPLGAPTlvtsqattlstfQPTNKLTKNVPANVRSSFPVSlPLAYPHPHFALL 1876
Cdd:PHA03247  2625 DPPPPSPSPAAN-EPDPHPPPTVPPPERPRDDPA------------PGRVSRPRRARRLGRAAQASS-PPQRPRRRAARP 2690

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1877 AAQTMQQIRHPRLPmaqfGGTFSPSPNTWG---PFPVRPVNPGNTNSSPKHNNAGRlPNQNGTVLPSESAGLATASCPIT 1953
Cdd:PHA03247  2691 TVGSLTSLADPPPP----PPTPEPAPHALVsatPLPPGPAAARQASPALPAAPAPP-AVPAGPATPGGPARPARPPTTAG 2765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1954 VSSVVAASQQLCV---TNTRTPSSVRKQLFACVPKTSPPATVISSVTSTCSSLPSvSSAPVTSGQVPTTFLPASTPQAQL 2030
Cdd:PHA03247  2766 PPAPAPPAAPAAGpprRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP-AASPAGPLPPPTSAQPTAPPPPPG 2844

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2031 SSQKMESFSAMPPPKEKVSTQDQAMAHLCTPSSTANSCSSSASNTPGAPETHPSSSPAPPSSNTQEevPPSSVSDLSPMS 2110
Cdd:PHA03247  2845 PPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQ--PQAPPPPQPQPQ 2922

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2111 MPFASNSEPAPLTLASPRLVAADNQDTSNL--PQLAVPAPRVSHRMQPRGSfysvVPNATIHQDPQSifVTNPVPLTPPQ 2188
Cdd:PHA03247  2923 PPPPPQPQPPPPPPPRPQPPLAPTTDPAGAgePSGAVPQPWLGALVPGRVA----VPRFRVPQPAPS--REAPASSTPPL 2996

                          410
                   ....*....|
gi 1953314652 2189 GPPAAVQLSS 2198
Cdd:PHA03247  2997 TGHSLSRVSS 3006
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 300-328 1.26e-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: 1.26e-04
                            10        20
                    ....*....|....*....|....*....
gi 1953314652   300 GNTALTYACAGGFVDIVKVLLNEGANIED 328
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
KH-I_RCF3_like_rpt5 cd22463
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
 1717-1780 1.35e-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: 1.35e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652 1717 LSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKD--KNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22463      6 FQIPEAVVGLIIGKSGNTIKQISERSGAFVAIVQDRYplEETQKILRISGTEEQLKRAQSLVEGLI 71
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1212-1301 1.41e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1212 AMNGHVPAVKLLLDMGSDINAQiETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1291
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168

                           90
                   ....*....|....*
gi 1953314652 1292 -----DKGADVNAPP 1301
Cdd:PTZ00322   169 rhsqcHFELGANAKP 183
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 615-642 1.42e-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: 1.42e-04
                            10        20
                    ....*....|....*....|....*...
gi 1953314652   615 GRTPLMKAARAGHLCTVQFLISKGANVN 642
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
319-374 1.46e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 1.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652  319 LLNEG-ANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINThSNEFKESALTLA 374
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 314-486 1.46e-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: 47.45  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  314 DIVKVLLNegANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGIN----------THSNE---FKESALTLACYKGHL 380
Cdd:cd22194    124 GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEgfyFGETPLALAACTNQP 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  381 DMVRFLLDAGADQEHKTDEMHTALMEACmdghVEVARlllDSGAQVNMPADSFESPLTlaACGGHvelaalliergaNLE 460
Cdd:cd22194    202 EIVQLLMEKESTDITSQDSRGNTVLHAL----VTVAE---DSKTQNDFVKRMYDMILL--KSENK------------NLE 260

                          170       180
                   ....*....|....*....|....*..
gi 1953314652  461 EV-NDEGYTPLMEAAREGHEEMVALLL 486
Cdd:cd22194    261 TIrNNEGLTPLQLAAKMGKAEILKYIL 287
Ank_4 pfam13637
Ankyrin repeats (many copies);
235-287 1.51e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 1.51e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953314652  235 SLLCLACSAGYYELAQVLLAMHANVEDRgNKGDITPLMAASSGGYLDIVKLLL 287
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 615-645 1.55e-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: 1.55e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1953314652  615 GRTPLMKAA-RAGHLCTVQFLISKGANVNRAT 645
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1338-1367 1.58e-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: 1.58e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1953314652  1338 KGNTPLWLASNGGHFDVVQLLVQAGADVDA 1367
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1108-1212 1.67e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1108 LAATAGHVGVvEILLDKGGDIEAQsERTKDTPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLAASGGYVNIIKI 1187
Cdd:PTZ00322    89 LAASGDAVGA-RILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1953314652 1188 LL---------NAGAEINSRTG--SKLGISPLMLAA 1212
Cdd:PTZ00322   167 LSrhsqchfelGANAKPDSFTGkpPSLEDSPISSHH 202
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
 1716-1776 1.79e-04

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: 41.82  E-value: 1.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNG---ERMITIRGGTESTRYAVQLI 1776
Cdd:cd22437      2 RLLVPNSSCGLIIGKGGSTIKELREDSNANIKISPKDQLLPgssERIVTITGSFDQVVKAVALI 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
793-879 1.88e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  793 VEETEGKLNELGQRISAIEKaqlksleliqgeplNKDKIEELKKNREEQVQKKKKILKELQKVERQLqmKTQQQFTKEYL 872
Cdd:PRK03918   233 LEELKEEIEELEKELESLEG--------------SKRKLEEKIRELEERIEELKKEIEELEEKVKEL--KELKEKAEEYI 296


                   ....*..
gi 1953314652  873 ETKGQKD 879
Cdd:PRK03918   297 KLSEFYE 303
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 332-361 1.88e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 1.88e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953314652  332 NGHTPLMEAASAGHVEVARVLLDHGAGINT 361
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
1188-1245 1.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 1.96e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1188 LLNAGAeINSRTGSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQiETNRNTALTLA 1245
Cdd:pfam13857    1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK-DEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 313-573 2.03e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  313 VDIVKVLLNEGANIEDHNENGHTPLMEAAS-----AGHVEVARVLLDHGAGINTHSnefKESALTLAC-----YKGHLDM 382
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKN---SDGETPLYCllsngYINNLEI 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  383 VRFLLDAGADQEHKTDEMHTALMEACMDGH---VEVARLLLDSGAQVNMPA-----DSFESPLTLAACGGHVELAALLIE 454
Cdd:PHA02798   128 LLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNnkekyDTLHCYFKYNIDRIDADILKLFVD 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  455 RGANLEEVNDEGYTPLMeaaregheEMVALLLAQGANINaqteetqetaltlaccggfSEVADFLIKAgADI----ELGC 530
Cdd:PHA02798   208 NGFIINKENKSHKKKFM--------EYLNSLLYDNKRFK-------------------KNILDFIFSY-IDInqvdELGF 259

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1953314652  531 sTPLMEASQEGHLELVKYLLAAGANVHATTATGDTALTYACEN 573
Cdd:PHA02798   260 -NPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 201-300 2.11e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  201 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVE--DRGNKgdiTPLMAASSGG 278
Cdd:PTZ00322    83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTllDKDGK---TPLELAEENG 159

                           90       100
                   ....*....|....*....|..
gi 1953314652  279 YLDIVKLLLLHDADVNSQSATG 300
Cdd:PTZ00322   160 FREVVQLLSRHSQCHFELGANA 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1204-1233 2.37e-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: 2.37e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1953314652 1204 GISPLMLAA-MNGHVPAVKLLLDMGSDINAQ 1233
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
 1716-1781 2.48e-04

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: 41.45  E-value: 2.48e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKqKDKN------GERMITIRGGTESTRYAVQLINALIQ 1781
Cdd:cd22460      3 RLLVASSQAGSLIGKGGAIIKQIREESGASVRILP-EEELppcaspDDRVVQISGEAQAVKKALELVSSRLR 73
Ank_4 pfam13637
Ankyrin repeats (many copies);
1104-1156 2.90e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 2.90e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1104 TPLILAATAGHVGVVEILLDKGGDIEAQSERtKDTPLSLACSGGRQEVVDLLL 1156
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 532-560 3.15e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 3.15e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953314652  532 TPLMEAS-QEGHLELVKYLLAAGANVHATT 560
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 1150-1234 3.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1150 EVVDLLLARGANKE----HRNVSDYTPLSLAASGGYVNIIKILLNAGAEINsRTGSKLGISPLMLAAMNGHVPAVKLLLD 1225
Cdd:PHA02884    47 DIIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVN-RYAEEAKITPLYISVLHGCLKCLEILLS 125


                   ....*....
gi 1953314652 1226 MGSDINAQI 1234
Cdd:PHA02884   126 YGADINIQT 134
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1101-1130 3.56e-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: 39.88  E-value: 3.56e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1953314652  1101 KGFTPLILAATAGHVGVVEILLDKGGDIEA 1130
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 216-337 3.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  216 VRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGdITPLMAASSggYLDIVKLLLLHDADVNS 295
Cdd:PHA02874   173 IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG-FTPLHNAII--HNRSAIELLINNASIND 249

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1953314652  296 QSATGNTALTYA----CAggfVDIVKVLLNEGANIEDHNENGHTPL 337
Cdd:PHA02874   250 QDIDGSTPLHHAinppCD---IDIIDILLYHKADISIKDNKGENPI 292
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 312-409 3.77e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.97  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  312 FVDIVKVLLNEGANIE---DHNENGHT-PLMEAASAGHVEVARVLLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLL 387
Cdd:PHA02884    45 YTDIIDAILKLGADPEapfPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124

                           90       100
                   ....*....|....*....|..
gi 1953314652  388 DAGADQEHKTDEMHTALMEACM 409
Cdd:PHA02884   125 SYGADINIQTNDMVTPIELALM 146
Ank_4 pfam13637
Ankyrin repeats (many copies);
1238-1291 4.73e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 4.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953314652 1238 RNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1291
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_BTR1_rpt3 cd22514
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ...
 1714-1780 4.96e-04

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: 40.48  E-value: 4.96e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKD---KNGERMITIRGGTEstryAVQLINALI 1780
Cdd:cd22514      2 SVTIGVPDEHIGAILGRGGRTINEIQQHSGARIKISDRGDfvsGTRNRKVTITGPQD----AVQMAQYLL 67
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 615-642 4.98e-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: 4.98e-04
                           10        20
                   ....*....|....*....|....*...
gi 1953314652  615 GRTPLMKAARAGHLCTVQFLISKGANVN 642
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 532-558 5.54e-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: 39.11  E-value: 5.54e-04
                            10        20
                    ....*....|....*....|....*..
gi 1953314652   532 TPLMEASQEGHLELVKYLLAAGANVHA 558
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 269-296 6.59e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 6.59e-04
                           10        20
                   ....*....|....*....|....*....
gi 1953314652  269 TPLM-AASSGGYLDIVKLLLLHDADVNSQ 296
Cdd:pfam00023    4 TPLHlAAGRRGNLEIVKLLLSKGADVNAR 32
KH-I_PCBP_rpt1 cd22438
first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
 1724-1789 6.86e-04

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: 39.93  E-value: 6.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953314652 1724 VSRIMGRGGCNITAIQDVTGAHIDVdkqkdKNG---ERMITIRGGTESTRYAVQLInaliqdpAKELED 1789
Cdd:cd22438     10 VGSIIGKKGETIKKFREESGARINI-----SDGscpERIVTVTGTTDAVFKAFELI-------CRKLEE 66
Ank_5 pfam13857
Ankyrin repeats (many copies);
1324-1376 6.90e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 6.90e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1324 LLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGADVDAADNRKITPL 1376
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1930-2207 8.02e-04

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: 45.14  E-value: 8.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1930 LPNQNGTVLPSESAGLATASCPITVSSVVAASQQLCVTNTRTPSSVRKQlfacvpKTSPPATVI-SSVTSTCSSLPSVSS 2008
Cdd:pfam03154  174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ------STAAPHTLIqQTPTLHPQRLPSPHP 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2009 A--PVTSGQVPTTFLPASTPQAQLSSQ----------------------------KMESFSAMPPPKEKVSTQDQAMAHL 2058
Cdd:pfam03154  248 PlqPMTQPPPPSQVSPQPLPQPSLHGQmppmphslqtgpshmqhpvppqpfpltpQSSQSQVPPGPSPAAPGQSQQRIHT 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2059 CTPSSTANSCSSSASNT-PGAPETHP-----SSSPAPPSSNTQEEVPPSSVSDLSPMSM-----------PFAS------ 2115
Cdd:pfam03154  328 PPSQSQLQSQQPPREQPlPPAPLSMPhikppPTTPIPQLPNPQSHKHPPHLSGPSPFQMnsnlppppalkPLSSlsthhp 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2116 -NSEPAPLTL--ASPRLVAADNQDTSNLPQLAVPAPRVSHrmQPRGSFYSVVPNATIhqdPQSIFV-TNPVPLTPPQGPP 2191
Cdd:pfam03154  408 pSAHPPPLQLmpQSQQLPPPPAQPPVLTQSQSLPPPAASH--PPTSGLHQVPSQSPF---PQHPFVpGGPPPITPPSGPP 482

                          330
                   ....*....|....*.
gi 1953314652 2192 AavqlsSAMNIMNGSQ 2207
Cdd:pfam03154  483 T-----STSSAMPGIQ 493
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 201-294 8.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 8.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  201 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDITPLMAASSGGYL 280
Cdd:PHA02875   136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKI 215

                           90
                   ....*....|....
gi 1953314652  281 DIVKLLLLHDADVN 294
Cdd:PHA02875   216 DIVRLFIKRGADCN 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1101-1131 8.34e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 8.34e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1953314652 1101 KGFTPLILAAT-AGHVGVVEILLDKGGDIEAQ 1131
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 401-428 8.37e-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: 8.37e-04
                            10        20
                    ....*....|....*....|....*...
gi 1953314652   401 HTALMEACMDGHVEVARLLLDSGAQVNM 428
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 331-550 8.60e-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: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  331 ENGHTPLMEAasaghvevarvLLDhgagINTHSNEFKESALTLACYKGHLDmvRFLldaGADQEHKTDEMHTALMEACMD 410
Cdd:cd22194     92 DTGKTCLMKA-----------LLN----INENTKEIVRILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIER 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  411 GHVEVARLLLDSGAQVNMPA-----------DSF---ESPLTLAACGGHVELAALLIERGANLEEVNDE-GYTPLmeaar 475
Cdd:cd22194    152 RQGDIVKLLIAKGADVNAHAkgvffnpkykhEGFyfgETPLALAACTNQPEIVQLLMEKESTDITSQDSrGNTVL----- 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  476 egHeemvALLLAqganinAQTEETQETALTlaccggfsEVADFLIKAGADIELGCS------TPLMEASQEGHLELVKYL 549
Cdd:cd22194    227 --H----ALVTV------AEDSKTQNDFVK--------RMYDMILLKSENKNLETIrnneglTPLQLAAKMGKAEILKYI 286


                   .
gi 1953314652  550 L 550
Cdd:cd22194    287 L 287
KH-I_IGF2BP2_rpt4 cd22500
fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
 1717-1781 9.46e-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: 9.46e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652 1717 LSVPASVVSRIMGRGGCNITAIQDVTGAHIDV--DKQKDKNGERMITIRGGTESTRYAVQLINALIQ 1781
Cdd:cd22500      6 IKVPSSAAGRVIGKGGKTVNELQNLTSAEVIVprDQTPDENEEVIVKIIGHFFASQTAQRKIREIVQ 72
KH-I_FUBP1_rpt4 cd22487
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
 1717-1780 1.02e-03

fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 1 (FUBP1) and similar proteins; 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. FUBP1 contains four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411915  Cd Length: 72  Bit Score: 39.94  E-value: 1.02e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652 1717 LSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGE---RMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22487      6 FIVPTGKTGLIIGKGGETIKSISQQSGARIELQRNPPPNADpnmKLFTIRGSPQQIDYARQLIEEKI 72
KH-I_IGF2BP2_rpt2 cd22494
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
 1722-1779 1.02e-03

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


Pssm-ID: 411922  Cd Length: 77  Bit Score: 40.01  E-value: 1.02e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1722 SVVSRIMGRGGCNITAIQDVTGAHIDVDKQKD---KNGERMITIRGGTES-TRYAVQLINAL 1779
Cdd:cd22494      9 SLVGRLIGKEGRNLKKIEQDTGTKITISSLQDltiYNPERTITVKGSIEAcSSAEVEIMKKL 70
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 596-708 1.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.27  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  596 KTILE-GIDPAKHQEHESeggrTPLMKAARAGHLCT-----VQFLISKGANVNratANNDHTVVSLACAG----GHLAVV 665
Cdd:PHA03100    52 KILLDnGADINSSTKNNS----TPLHYLSNIKYNLTdvkeiVKLLLEYGANVN---APDNNGITPLLYAIskksNSYSIV 124

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1953314652  666 ELLLAHGADPTHRLKDGSTMLIEAAKGGH--TNVVSYLLDYPNNV 708
Cdd:PHA03100   125 EYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDI 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
1256-1313 1.17e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1256 LLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIA 1313
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK--DEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1285-1391 1.28e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1285 EVGRVLLDKGADVNAPPVPSSrdtALTIAAdKGHYKFCELLINRGAHIDVRNKKGNTPLWLASNGGHFDVVQLLVQAGAD 1364
Cdd:PLN03192   508 NVGDLLGDNGGEHDDPNMASN---LLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                           90       100
                   ....*....|....*....|....*..
gi 1953314652 1365 VDAADNRKITPLMSAFRKGHVKVVQYL 1391
Cdd:PLN03192   584 VHIRDANGNTALWNAISAKHHKIFRIL 610
KH-I_PCBP1_2_rpt2 cd22518
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
 1716-1776 1.30e-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: 39.72  E-value: 1.30e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNG-ERMITIRGGTESTRYAVQLI 1776
Cdd:cd22518     10 RLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNStERAITIAGIPQSIIECVKQI 71
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1169-1196 1.45e-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: 1.45e-03
                            10        20
                    ....*....|....*....|....*...
gi 1953314652  1169 DYTPLSLAASGGYVNIIKILLNAGAEIN 1196
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
KH-I_IGF2BP_rpt3 cd22402
third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
 1717-1768 1.49e-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: 39.16  E-value: 1.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953314652 1717 LSVPASVVSRIMGRGGCNITAIQDVTGAHIDV-DKQKDKNGERMITIRGGTES 1768
Cdd:cd22402      5 LYIPNKAVGAIIGTKGSHIRYIKRFSGASIKIaPADSPDAPERKVTITGPPEA 57
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1073-1261 1.51e-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: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1073 LTLACAGGHEELVSVLIARDAKIEHRDKkgftpLILAATAGHVGVVE----ILLDKGGDI--------EAQSERTKD-TP 1139
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDAVEaillHLLAAFRKSgplelandQYTSEFTPGiTA 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1140 LSLACSGGRQEVVDLLLARGAN------------KEHRNVSDYT--PLSLAASGGYVNIIKILLNAGAEInsRTGSKLGI 1205
Cdd:TIGR00870  132 LHLAAHRQNYEIVKLLLERGASvparacgdffvkSQGVDSFYHGesPLNAAACLGSPSIVALLSEDPADI--LTADSLGN 209

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652 1206 SPLMLAAMNGHVPAV---------KLLLDMG--SDINAQIE--TNRN--TALTLACFQGRAEVVSLLLDRK 1261
Cdd:TIGR00870  210 TLLHLLVMENEFKAEyeelscqmyNFALSLLdkLRDSKELEviLNHQglTPLKLAAKEGRIVLFRLKLAIK 280
PHA03379 PHA03379
EBNA-3A; Provisional
 1899-2298 1.57e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 43.89  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1899 SPSPNTWGPFPV----RPVNPGNTNSSPKHNNAgRLPnQNGTVLPSESAGL----ATASCPitVSSVVAASQQLCVTNTR 1970
Cdd:PHA03379   408 ASEPTYGTPRPPvekpRPEVPQSLETATSHGSA-QVP-EPPPVHDLEPGPLhdqhSMAPCP--VAQLPPGPLQDLEPGDQ 483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1971 TPSSVRKQLFACVPKTSPPATVISSVTSTCSSLPSVSSAPVTSGQVPTTFLPASTPQAQLSSQKMESFSAMPPPKEKVST 2050
Cdd:PHA03379   484 LPGVVQDGRPACAPVPAPAGPIVRPWEASLSQVPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQGPGETSGI 563

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2051 QDQAMAHLC-----TPSSTANSCSSSASNTPGAPETHPSSSPAPPSSNTQEEVPPSsvsdlSPMSMPFASNSEPAPltlA 2125
Cdd:PHA03379   564 VRVRERWRPapwtpNPPRSPSQMSVRDRLARLRAEAQPYQASVEVQPPQLTQVSPQ-----QPMEYPLEPEQQMFP---G 635

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2126 SPRLVAADNQDTSNLPQLAvPAPRVSHRMQPRGSFYSVVP-NATIHQDPqsifvtnPVPLTPPQGppAAVQLSSAMNiMN 2204
Cdd:PHA03379   636 SPFSQVADVMRAGGVPAMQ-PQYFDLPLQQPISQGAPLAPlRASMGPVP-------PVPATQPQY--FDIPLTEPIN-QG 704

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2205 GSQMHINPANKSLPPTFGPATLFNHFSSLFDSSQVPANQGWGDGPLS---SRVAADASFTVQSAFLGNSVlghlenvhPD 2281
Cdd:PHA03379   705 ASAAHFLPQQPMEGPLVPERWMFQGATLSQSVRPGVAQSQYFDLPLTqpiNHGAPAAHFLHQPPMEGPWV--------PE 776

                          410
                   ....*....|....*..
gi 1953314652 2282 NSKAPGFRPSQRVSTSP 2298
Cdd:PHA03379   777 QWMFQGAPPSQGTDVVQ 793
KH-I_PEPPER_like_rpt3 cd22461
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
 1714-1780 1.64e-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: 39.07  E-value: 1.64e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22461      3 SQQMQIPLSYADAIIGTAGANISYIRRTSGATITIQETRGAPGEMTVEIHGTQSQVQTAQQLIQNFM 69
Ank_5 pfam13857
Ankyrin repeats (many copies);
1154-1211 1.67e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1154 LLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLA 1211
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE--GLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 280-394 1.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  280 LDIVKLLLLHDADVNSQSATGNTAL--TYACAGGFV--DIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVL 352
Cdd:PHA02859    66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV-RINVIKLL 144

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1953314652  353 LDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLDAGADQE 394
Cdd:PHA02859   145 IDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDIN 186
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 1061-1190 1.88e-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: 43.59  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1061 IDA-HTESNHD--TALTLACAGGHEELVSVLIARDAKIEHRDKKGF--------------TPLILAATAGHVGVVEILLD 1123
Cdd:cd22194    130 INAeYTEEAYEgqTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLME 209

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953314652 1124 KGGDIEAQSERTKDTPL---------SLACSGGRQEVVDLLLARGANKE---HRNVSDYTPLSLAASGGYVNIIKILLN 1190
Cdd:cd22194    210 KESTDITSQDSRGNTVLhalvtvaedSKTQNDFVKRMYDMILLKSENKNletIRNNEGLTPLQLAAKMGKAEILKYILS 288
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 473-583 1.94e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  473 AAREGHEEMVAlllaqGANINAQTEETQETA----LTLACC----GGFSEVADFLIKAGAD---IELGCSTPLMEASQEG 541
Cdd:PTZ00322    52 EALEATENKDA-----TPDHNLTTEEVIDPVvahmLTVELCqlaaSGDAVGARILLTGGADpncRDYDGRTPLHIACANG 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1953314652  542 HLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLL 583
Cdd:PTZ00322   127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 369-392 2.11e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 2.11e-03
                            10        20
                    ....*....|....*....|....
gi 1953314652   369 SALTLACYKGHLDMVRFLLDAGAD 392
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGAD 27
KH-I_IGF2BP1_rpt4 cd22499
fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
 1717-1782 2.16e-03

fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1) and similar proteins; IGF2BP1, also called IGF2 mRNA-binding protein 1 (IMP-1), or coding region determinant-binding protein (CRD-BP), or IGF-II mRNA-binding protein 1, or VICKZ family member 1 (VICKZ1), or zipcode-binding protein 1 (ZBP-1), 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 regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. IGF2BP1 can form homodimers and heterodimers with IGF2BP1 and IGF2BP3. 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: 411927  Cd Length: 76  Bit Score: 39.24  E-value: 2.16e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1717 LSVPASVVSRIMGRGGCNITAIQDVTGAHIDV--DKQKDKNGERMITIRGGTestrYAVQLINALIQD 1782
Cdd:cd22499      6 IKVPASAAGRVIGKGGKTVNELQNLTAAEVVVprDQTPDENDQVIVKIIGHF----YASQMAQRKIRD 69
KH-I_PCBP4_rpt2 cd22520
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
 1716-1780 2.21e-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: 38.85  E-value: 2.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652 1716 KLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNG-ERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22520      5 RLVIPASQCGSLIGKAGSKIKEIRESTGAQVQVAGDLLPNStERAVTVSGVPDAIIQCVRQICAVI 70
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
794-879 2.28e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  794 EETEGKLNELGQRISAIEKaqlkslELIQGEPLNKdKIEELKKNREEQVQKKKKILKELQKV------ERQLQMKTQQQF 867
Cdd:PRK03918   528 EKLKEKLIKLKGEIKSLKK------ELEKLEELKK-KLAELEKKLDELEEELAELLKELEELgfesveELEERLKELEPF 600

                           90
                   ....*....|..
gi 1953314652  868 TKEYLETKGQKD 879
Cdd:PRK03918   601 YNEYLELKDAEK 612
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 563-591 2.31e-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: 2.31e-03
                           10        20
                   ....*....|....*....|....*....
gi 1953314652  563 GDTALTYACENGHTDVADVLLQAGADLDK 591
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_PNPT1 cd09033
type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide ...
 1714-1749 2.50e-03

type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide nucleotidyltransferase 1 (PNPT1) and similar proteins; PNPT1, also called 3'-5' RNA exonuclease OLD35, or PNPase old-35, or polynucleotide phosphorylase 1, or PNPase 1, or polynucleotide phosphorylase-like protein, is an RNA-binding protein implicated in numerous RNA metabolic processes. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. It acts as a mitochondrial intermembrane factor with RNA-processing exoribonulease activity. PNPT1 is a component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. It is involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules and required for correct processing and polyadenylation of mitochondrial mRNAs. PNPT1 also plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix.


Pssm-ID: 411809 [Multi-domain]  Cd Length: 67  Bit Score: 38.33  E-value: 2.50e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHID-VD 1749
Cdd:cd09033      7 TETLEVPPSKRAKFVGPGGYNIKKLQAETGVTITqVD 43
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 563-592 2.61e-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: 37.65  E-value: 2.61e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1953314652  563 GDTALTYACE-NGHTDVADVLLQAGADLDKQ 592
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank_5 pfam13857
Ankyrin repeats (many copies);
1290-1346 2.96e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 2.96e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953314652 1290 LLDKG-ADVNAPPvpSSRDTALTIAADKGHYKFCELLINRGAHIDVRNKKGNTPLWLA 1346
Cdd:pfam13857    1 LLEHGpIDLNRLD--GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 1715-1781 3.26e-03

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: 38.32  E-value: 3.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652 1715 KKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGErmITIRGGTESTRYAVQLINALIQ 1781
Cdd:cd02394      4 TTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDE--IRIEGSPEGVKKAKAEILELVD 68
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 269-294 3.35e-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: 3.35e-03
                            10        20
                    ....*....|....*....|....*.
gi 1953314652   269 TPLMAASSGGYLDIVKLLLLHDADVN 294
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 378-458 3.77e-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: 42.56  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  378 GHLDMVRFLLDAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA--DSF----------- 433
Cdd:cd21882     40 GVNEAIMLLLEAAPDSgnpkelvnAPCTDEFyqgQTALHIAIENRNLNLVRLLVENGADVSARAtgRFFrkspgnlfyfg 119

                           90       100
                   ....*....|....*....|....*
gi 1953314652  434 ESPLTLAACGGHVELAALLIERGAN 458
Cdd:cd21882    120 ELPLSLAACTNQEEIVRLLLENGAQ 144
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1338-1367 3.88e-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: 36.85  E-value: 3.88e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953314652 1338 KGNTPLWLASNGGHFDVVQLLVQAGADVDA 1367
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
789-860 4.60e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 4.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652  789 LECIVEETEGKLNELGQRISAIEKaQLKSLELIQGEplnKDKIEELKKNREEQVQKKKKILKELQKVERQLQ 860
Cdd:PRK03918   257 LEEKIRELEERIEELKKEIEELEE-KVKELKELKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
Ank_5 pfam13857
Ankyrin repeats (many copies);
1132-1176 4.94e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 4.94e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1953314652 1132 SERTKDTPLSLACSGGRQEVVDLLLARGANKEHRNVSDYTPLSLA 1176
Cdd:pfam13857   12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1271-1299 5.35e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 5.35e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953314652 1271 GLTPLMEAA-SGGYAEVGRVLLDKGADVNA 1299
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 808-878 5.43e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 41.25  E-value: 5.43e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652  808 SAIEKAQLKSLELIQGEPLNKDKIEELKKNREEQVQKKKKILKELQKVERQLqmktqQQFTKEYLETKGQK 878
Cdd:COG4026    114 NAIIRAGLKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESEL-----EELREEYKKLREEN 179
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1801-2189 5.57e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 41.87  E-value: 5.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1801 STKSIHANFSSgvgTTAASSKNAFPLG--APTLVTSQATTLSTFQPTNKLTKNVPANVRSSFPVSLPLAyPHPHFALLAA 1878
Cdd:pfam17823   52 NKSSEQ*NFCA---ATAAPAPVTLTKGtsAAHLNSTEVTAEHTPHGTDLSEPATREGAADGAASRALAA-AASSSPSSAA 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1879 QTMQqirhprlpmaqfgGTFSPSPNTWGPFPVRPVNPGNTNSSPKHNNAGRLPNQNGTVLPSESAGLATASCPITVSSVV 1958
Cdd:pfam17823  128 QSLP-------------AAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSA 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1959 AASQQLCVTNTRTPSSVrkqlfacvPKTSPPATVISSVTSTCSSLPSVSSAPVTSGQVPTTFLPASTPQAQLSSQKMESF 2038
Cdd:pfam17823  195 PTTAASSAPATLTPARG--------ISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASA 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 2039 SAMPPPKEKVSTqdqamahlcTPSSTANSCSSSASNTPGAPethpssspappsSNTQEEVPPSSVSDLSPMsmpfaSNSE 2118
Cdd:pfam17823  267 AGTINMGDPHAR---------RLSPAKHMPSDTMARNPAAP------------MGAQAQGPIIQVSTDQPV-----HNTA 320

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652 2119 PAPLTLASPRLVAADNQDTSNLPQLAVPAPRVSHRMQPRGSFYSVVPNATIHQDPQSIFVTNPVPLTPPQG 2189
Cdd:pfam17823  321 GEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLPTQG 391
NYD-SP28 pfam14772
Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in ...
 794-865 5.57e-03

Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in spermatogenic cell cytoplams and human spermatozoa tail. It is post-translationally modified during sperm capacitation and ultimately contributes to the success of fertilization.


Pssm-ID: 464307 [Multi-domain]  Cd Length: 102  Bit Score: 38.73  E-value: 5.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953314652  794 EETEGKLNELGQRISAIeKAQLKSLELiqgeplnKDKIEELKKNREEQVQKKKKILKELQKverQLQMKTQQ 865
Cdd:pfam14772   30 KSSQEKFEKINQRWRSI-LRKNKPQEL-------REELEEQKQACERIIDRKDKLIKELQQ---ELKEADEQ 90
PHA02795 PHA02795
ankyrin-like protein; Provisional
 280-350 5.75e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.90  E-value: 5.75e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953314652  280 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVAR 350
Cdd:PHA02795   201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARR 271
KH-I_FUBP2_rpt1 cd22479
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
 1714-1780 6.51e-03

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: 37.61  E-value: 6.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALI 1780
Cdd:cd22479      2 TEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGSPEAVQKAKMMLDDIV 68
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 378-651 6.60e-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: 41.79  E-value: 6.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  378 GHLDMVRFLLDAGADQEHKTDEmhTALMEACM---DGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIE 454
Cdd:cd21882      6 GLLECLRWYLTDSAYQRGATGK--TCLHKAALnlnDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQTALHIAIEN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  455 RGANLeevndegytplmeaaregheemVALLLAQGANINAqteetqetaltlACCGgfsevaDFLIKAGADIELGCSTPL 534
Cdd:cd21882     84 RNLNL----------------------VRLLVENGADVSA------------RATG------RFFRKSPGNLFYFGELPL 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  535 MEASQEGHLELVKYLLAAGANVHATTAT---GDTAL---------TYACENGHTDVADVLLQAGADLDKQEDMKTIlegi 602
Cdd:cd21882    124 SLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLhalvlqadnTPENSAFVCQMYNLLLSYGAHLDPTQQLEEI---- 199

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1953314652  603 dpAKHQehesegGRTPLMKAARAGHLCTVQFLISKGANVNRATANNDHT 651
Cdd:cd21882    200 --PNHQ------GLTPLKLAAVEGKIVMFQHILQREFSGPYQPLSRKFT 240
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 402-526 6.61e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 6.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  402 TALMEACMDGHVE-VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIE---RGANLEEVND--EGYTPLMEAAR 475
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVV 98

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953314652  476 EGHEEMVALLLAQGAN-INAQTEET------------QETALTLACCGGFSEVADFLIKAGADI 526
Cdd:cd22192     99 NQNLNLVRELIARGADvVSPRATGTffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADI 162
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 439-545 6.92e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  439 LAACGGHVElAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAqTEETQETALTLACCGGFSEVADF 518
Cdd:PTZ00322    89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQL 166

                           90       100
                   ....*....|....*....|....*....
gi 1953314652  519 LIK-AGADIELG-CSTPLMEASQEGHLEL 545
Cdd:PTZ00322   167 LSRhSQCHFELGaNAKPDSFTGKPPSLED 195
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 237-330 6.97e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 6.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  237 LCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIV 316
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                           90
                   ....*....|....
gi 1953314652  317 KVLLneGANIEDHN 330
Cdd:PTZ00322   165 QLLS--RHSQCHFE 176
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 532-686 7.12e-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: 41.61  E-value: 7.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  532 TPLMEASQEG-HLELVKYLLAAGANVhattATGDTALTYACENGHTDVADVLLQAgadLDKQEDMKTILEGIDPAKHQEH 610
Cdd:TIGR00870   54 SALFVAAIENeNLELTELLLNLSCRG----AVGDTLLHAISLEYVDAVEAILLHL---LAAFRKSGPLELANDQYTSEFT 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652  611 EsegGRTPLMKAARAGHLCTVQFLISKGANVNrATANNDHTV--------------VSLACAGGHLAVVELLLAHGADPT 676
Cdd:TIGR00870  127 P---GITALHLAAHRQNYEIVKLLLERGASVP-ARACGDFFVksqgvdsfyhgespLNAAACLGSPSIVALLSEDPADIL 202

                          170
                   ....*....|
gi 1953314652  677 HRLKDGSTML 686
Cdd:TIGR00870  203 TADSLGNTLL 212
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 1714-1788 7.79e-03

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: 37.18  E-value: 7.79e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953314652 1714 SKKLSVPASVVSRIMGRGGCNITAI-QDVTGAHIDVDKQKDKngermITIRGGTEStryaVQLINALIQDPAKELE 1788
Cdd:cd22409      3 VAEVSAPSWLHRFIIGKKGANIKKItQDLPKVHIEFTEGEDK-----IELEGPPEE----VEVVREQLEAIVKELV 69
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 402-428 7.89e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 7.89e-03
                           10        20
                   ....*....|....*....|....*..
gi 1953314652  402 TALMEACMDGHVEVARLLLDSGAQVNM 428
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 300-331 7.94e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 7.94e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1953314652  300 GNTALTYACA-GGFVDIVKVLLNEGANIEDHNE 331
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1288-1397 7.95e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 7.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953314652 1288 RVLLDKGADVNAppVPSSRDTAL-TIAADKGHYK----FCELLINRGAHIDVRNKKGNTPLW-LASNG--GHFDVVQLLV 1359
Cdd:PHA02798    55 KLFINLGANVNG--LDNEYSTPLcTILSNIKDYKhmldIVKILIENGADINKKNSDGETPLYcLLSNGyiNNLEILLFMI 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1953314652 1360 QAGADVDAADNRKITPLMSAFRKGH---VKVVQYLVK---EVNQ 1397
Cdd:PHA02798   133 ENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEkgvDINT 176
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 401-427 8.10e-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: 8.10e-03
                           10        20
                   ....*....|....*....|....*...
gi 1953314652  401 HTALMEAC-MDGHVEVARLLLDSGAQVN 427
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 300-326 9.51e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 9.51e-03
                           10        20
                   ....*....|....*....|....*..
gi 1953314652  300 GNTALTYACAGGFVDIVKVLLNEGANI 326
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADI 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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