NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|38683807|ref|NP_115593|]
View 

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

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
385-666 1.79e-59

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 207.50  E-value: 1.79e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  385 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 464
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  465 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 544
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  545 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 621
Cdd:COG0666  164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 38683807  622 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 666
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1102-1390 2.38e-56

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.64  E-value: 2.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1102 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 1181
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1182 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1261
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1262 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1341
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 38683807 1342 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1390
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-465 4.24e-56

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.87  E-value: 4.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  184 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 263
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  264 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 343
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  344 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 423
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 38683807  424 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 465
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
1726-1796 1.56e-40

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


:

Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 144.51  E-value: 1.56e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683807 1726 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1796
Cdd:cd22502    1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
Ank_2 pfam12796
Ankyrin repeats (3 copies);
634-719 5.23e-15

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 5.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    634 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 713
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 38683807    714 CYLLDY 719
Cdd:pfam12796   78 KLLLEK 83
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
2082-2337 1.91e-08

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


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.17  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2082 PPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMT-------VPPLATSSAPVAVPSTAP 2154
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTpqssqsqVPPGPSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2155 VTYPMPQTPMGCP---QPTPK--METPAIRPPPHGTTAPHKNSASvqnssvavlsvnHIKRPH-SVPSSVQLPSTLSTQS 2228
Cdd:pfam03154  327 TPPSQSQLQSQQPpreQPLPPapLSMPHIKPPPTTPIPQLPNPQS------------HKHPPHlSGPSPFQMNSNLPPPP 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2229 ACQN----------SVHPANKPIAPNfSAPLPFGPFS----TLFENSPTSAhafwggsvvsSQSTPESMLSGKSSYLPNs 2294
Cdd:pfam03154  395 ALKPlsslsthhppSAHPPPLQLMPQ-SQQLPPPPAQppvlTQSQSLPPPA----------ASHPPTSGLHQVPSQSPF- 462
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 38683807   2295 dPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDSPyGSVTPSST 2337
Cdd:pfam03154  463 -PQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPP-SSASVSSS 503
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
794-893 2.02e-07

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


:

Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 52.19  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    794 DVQgYITNQSPEsiVEEAQGKLTELEQRIKEAIE-KNAQLQSL--ELahadQLTKEKIEELNKTREEQIQKKQKILEELQ 870
Cdd:pfam03938    6 DMQ-KILEESPE--GKAAQAQLEKKFKKRQAELEaKQKELQKLyeEL----QKDGALLEEEREEKEQELQKKEQELQQLQ 78
                           90       100
                   ....*....|....*....|....
gi 38683807    871 -KVERELQLKTQQQLKKQYLEVKA 893
Cdd:pfam03938   79 qKAQQELQKKQQELLQPIQDKINK 102
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
805-1008 5.89e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  805 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTR-----EEQIQKKQKILEELQKVERELQLK 879
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEA 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  880 TQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLLTPVGVGEQLSEGDYARLQQVDPVLLKDEPQQtAAQMGFAPIQPLAMP 959
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLE 508
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 38683807  960 QALPLAAGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQ 1008
Cdd:COG1196  509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
Ank_2 super family cl48147
Ankyrin repeats (3 copies);
1075-1113 1.04e-03

Ankyrin repeats (3 copies);


The actual alignment was detected with superfamily member pfam12796:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 1.04e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 38683807   1075 IDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRD 1113
Cdd:pfam12796   53 ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
385-666 1.79e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 207.50  E-value: 1.79e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  385 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 464
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  465 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 544
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  545 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 621
Cdd:COG0666  164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 38683807  622 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 666
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1102-1390 2.38e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.64  E-value: 2.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1102 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 1181
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1182 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1261
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1262 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1341
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 38683807 1342 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1390
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-465 4.24e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.87  E-value: 4.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  184 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 263
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  264 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 343
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  344 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 423
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 38683807  424 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 465
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
1726-1796 1.56e-40

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


Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 144.51  E-value: 1.56e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683807 1726 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1796
Cdd:cd22502    1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
1097-1403 1.23e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 116.28  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1097 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVG--VVEILLDNGADIEAQsERTKDTPL-SLACSGGRQEVVELLLAR 1172
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1173 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPL--MLAAMNGHTAAVKLLLDMGSDINAqI 1248
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLavLLKSRNANVELLRLLIDAGADVYA-V 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1249 ETNRNTALTLAC--FQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssrdtal 1324
Cdd:PHA03095  184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA----------- 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807  1325 tiaadkghykfcelligrgahidvRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVR 1403
Cdd:PHA03095  253 ------------------------RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
240-560 1.88e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.73  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   240 EACSEGDVNAVRKLLIEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGIKGDiTPLMA-AANGGHVK 315
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   316 IVKLLLAHKADVNAQSSTGNTALtYACAGGY---VDVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLLLEN 389
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   390 GAGI-----------NTHSNEFKESAltlacykghlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 456
Cdd:PHA03095  177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   457 GAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQgaNINAQT-EETQE 535
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK--NPSAETvAATLN 324
                         330       340
                  ....*....|....*....|....*....
gi 38683807   536 TA----LTLACCGGFLEVADFLIKAGADI 560
Cdd:PHA03095  325 TAsvagGDIPSDATRLCVAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
305-395 2.85e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 2.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    305 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASieDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 38683807    385 LLLENGAGINT 395
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
568-659 4.68e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.26  E-value: 4.68e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    568 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHVCTVQ 647
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 38683807    648 FLISKGANVNRT 659
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1222-1313 6.24e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 6.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1222 LMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1301
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 38683807   1302 RVLLDKGADVNA 1313
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
250-463 1.52e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   250 VRKLLIEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVeDRGIKGDITPLMAAANG--GHVKIVKLLLA 322
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV-NAPDNNGITPLLYAISKksNSYSIVEYLLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   323 HKADVNAQSSTGNTALTYACAGGYVDV------------------VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PHA03100  130 NGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   385 LLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 456
Cdd:PHA03100  210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287

                  ....*..
gi 38683807   457 GAQVNMP 463
Cdd:PHA03100  288 GFYKNRK 294
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1727-1791 5.11e-17

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


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 77.32  E-value: 5.11e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807   1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1791
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
634-719 5.23e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 5.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    634 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 713
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 38683807    714 CYLLDY 719
Cdd:pfam12796   78 KLLLEK 83
KH smart00322
K homology RNA-binding domain;
1729-1793 3.37e-13

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 66.55  E-value: 3.37e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807    1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIP--GPGSEERVVEITGPPENVEKAAELILEIL 68
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
565-743 1.83e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 69.66  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  565 STPLMEAAQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 638
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  639 RAGHVCTVQFLISKGANVN--RTTAN------------NDHtVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 704
Cdd:cd22192   98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 38683807  705 AKGGHTSVVCYLLDYpnnLLSAPPPDvtQLTPPSHDLNR 743
Cdd:cd22192  177 VLQPNKTFACQMYDL---ILSYDKED--DLQPLDLVPNN 210
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1145-1374 2.35e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1145 QSERTKDTPLSLACSGGRQEVVELLL--------ARGANKEhrnvsdyTPLSLAASGGYVNIIKILLNAGAE-INSRTGS 1215
Cdd:cd22192   12 QQKRISESPLLLAAKENDVQAIKKLLkcpscdlfQRGALGE-------TALHVAALYDNLEAAVVLMEAAPElVNEPMTS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1216 KL--GISPLMLAAMNGHTAAVKLLLDMGSDINaqieTNRNTALtlaCFqgrtevvsllLDRKANV----EHraktgltPL 1289
Cdd:cd22192   85 DLyqGETALHIAVVNQNLNLVRELIARGADVV----SPRATGT---FF----------RPGPKNLiyygEH-------PL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1290 MEAASGGYAEVGRVLLDKGADVNAppvpssRD----TALTIAADKGHYKF-CE---LLIGRGAHID------VRNKKGNT 1355
Cdd:cd22192  141 SFAACVGNEEIVRLLIEHGADIRA------QDslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLT 214
                        250
                 ....*....|....*....
gi 38683807 1356 PLWLAANGGHLDVVQLLVQ 1374
Cdd:cd22192  215 PFKLAAKEGNIVMFQHLVQ 233
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
2082-2337 1.91e-08

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.17  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2082 PPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMT-------VPPLATSSAPVAVPSTAP 2154
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTpqssqsqVPPGPSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2155 VTYPMPQTPMGCP---QPTPK--METPAIRPPPHGTTAPHKNSASvqnssvavlsvnHIKRPH-SVPSSVQLPSTLSTQS 2228
Cdd:pfam03154  327 TPPSQSQLQSQQPpreQPLPPapLSMPHIKPPPTTPIPQLPNPQS------------HKHPPHlSGPSPFQMNSNLPPPP 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2229 ACQN----------SVHPANKPIAPNfSAPLPFGPFS----TLFENSPTSAhafwggsvvsSQSTPESMLSGKSSYLPNs 2294
Cdd:pfam03154  395 ALKPlsslsthhppSAHPPPLQLMPQ-SQQLPPPPAQppvlTQSQSLPPPA----------ASHPPTSGLHQVPSQSPF- 462
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 38683807   2295 dPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDSPyGSVTPSST 2337
Cdd:pfam03154  463 -PQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPP-SSASVSSS 503
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
794-893 2.02e-07

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 52.19  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    794 DVQgYITNQSPEsiVEEAQGKLTELEQRIKEAIE-KNAQLQSL--ELahadQLTKEKIEELNKTREEQIQKKQKILEELQ 870
Cdd:pfam03938    6 DMQ-KILEESPE--GKAAQAQLEKKFKKRQAELEaKQKELQKLyeEL----QKDGALLEEEREEKEQELQKKEQELQQLQ 78
                           90       100
                   ....*....|....*....|....
gi 38683807    871 -KVERELQLKTQQQLKKQYLEVKA 893
Cdd:pfam03938   79 qKAQQELQKKQQELLQPIQDKINK 102
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
794-893 2.60e-07

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 52.92  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  794 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEKI---EELNKTREEQIQKKQKILEEL 869
Cdd:COG2825   30 DVQ-RILQESPE--GKAAQKKLeKEFKKRQAELQKLEKELQALQ----EKLQKEAAtlsEEERQKKERELQKKQQELQRK 102
                         90       100
                 ....*....|....*....|....*
gi 38683807  870 -QKVERELQLKTQQQLKKQYLEVKA 893
Cdd:COG2825  103 qQEAQQDLQKRQQELLQPILEKIQK 127
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
238-421 2.77e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.17  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  238 LAEACSEGDVNAVRKLLiEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDI----TPLMAAANG 311
Cdd:cd22192   21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLyqgeTALHIAVVN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  312 GHVKIVKLLLAHKADVNAQSST--------------GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL----ME 373
Cdd:cd22192  100 QNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvLQ 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 38683807  374 AGSAGHVEVARLLLENGAGINTHS-----NEFKESALTLACYKGHLEMVRFLL 421
Cdd:cd22192  180 PNKTFACQMYDLILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1069-1305 1.08e-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: 54.32  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1069 IYPAIDIDaqtESNHDTALTLACAGGHEELVQTLLERGAS--IEHRDKKGFTPLILAATAG-HVGVVEILLDNGADIEaq 1145
Cdd:TIGR00870    6 IVPAEESP---LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1146 serTKDTPLsLACSGGRQEVVELLLA-------RGANKEHRNVS-------DYTPLSLAASGGYVNIIKILLNAGAEINS 1211
Cdd:TIGR00870   81 ---VGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1212 R------------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIE---------------TNRNTALTLACFQgr 1264
Cdd:TIGR00870  157 RacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSlgntllhllvmenefKAEYEELSCQMYN-- 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 38683807   1265 tEVVSLL--LDRKANVEH-RAKTGLTPLMEAASGGYAEVGRVLL 1305
Cdd:TIGR00870  235 -FALSLLdkLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
634-738 2.12e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   634 LMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVV 713
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90       100
                  ....*....|....*....|....*...
gi 38683807   714 CYLLDYPNNLLSA---PPPDVTQLTPPS 738
Cdd:PTZ00322  165 QLLSRHSQCHFELganAKPDSFTGKPPS 192
PHA03247 PHA03247
large tegument protein UL36; Provisional
2025-2457 2.26e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2025 TNATYPMPTAKEHYPVSSPSSPSPPAQPGGVSRNSPLDcGSASPNKVASSSeqeaGSPPVVETTNTRPPNSSSSSGSSSA 2104
Cdd:PHA03247 2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRL----GRAAQASSPPQRPRRRAARPTVGSL 2695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2105 HSNQQQPPGSVSQEPRPPLQQSQVPPPEV----RMTVPPLATSSAPVAVPST-----APVTYPMPQTPMGCPQPTPKMET 2175
Cdd:PHA03247 2696 TSLADPPPPPPTPEPAPHALVSATPLPPGpaaaRQASPALPAAPAPPAVPAGpatpgGPARPARPPTTAGPPAPAPPAAP 2775
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2176 PAirPPPHGTTAPHKNSASVQNSSVAVLSvnhikRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIAPNfSAPLPFGPFS 2255
Cdd:PHA03247 2776 AA--GPPRRLTRPAVASLSESRESLPSPW-----DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT-APPPPPGPPP 2847
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2256 TlfensPTSAhafwGGSVVssqstPESMLSGKSsylpnsdPLHQSDTSKAPGFRPP---LQRPAPSPSGIVNMDSPYGSV 2332
Cdd:PHA03247 2848 P-----SLPL----GGSVA-----PGGDVRRRP-------PSRSPAAKPAAPARPPvrrLARPAVSRSTESFALPPDQPE 2906
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2333 TPssthlgnfasnisggqmygpgaplggapaaanfnRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSP-APSSVPLGS 2411
Cdd:PHA03247 2907 RP----------------------------------PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPlAPTTDPAGA 2952
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 38683807  2412 EKPSNVSQDRKVPVPIGTERSARIRQTGTSAPSVIGSNLSTSVGHS 2457
Cdd:PHA03247 2953 GEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTG 2998
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
774-887 9.00e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.17  E-value: 9.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    774 IRNKAASKQKSSSHLPANSQDVQGYITNQSPE--SIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTK-EKIEE 850
Cdd:TIGR04523  326 IQNQISQNNKIISQLNEQISQLKKELTNSESEnsEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiQNQEK 405
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 38683807    851 LNKTREEQIQKKQKILEELQK-VERELQLKTQQQ-----LKKQ 887
Cdd:TIGR04523  406 LNQQKDEQIKKLQQEKELLEKeIERLKETIIKNNseikdLTNQ 448
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1352-1381 1.21e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 1.21e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 38683807    1352 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1381
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
499-528 1.26e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 1.26e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 38683807     499 EGYTPLMEAAREGHEEMVALLLGQGANINA 528
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
804-886 2.44e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.83  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   804 PESIVEEAQGKLTELEQRIKEAIEKNAQLQ-SLE--LAHADQLtkekIEELNKTREEQIQKKQKILEELQKVERELQLKT 880
Cdd:PRK00409  500 PENIIEEAKKLIGEDKEKLNELIASLEELErELEqkAEEAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA 575

                  ....*.
gi 38683807   881 QQQLKK 886
Cdd:PRK00409  576 QQAIKE 581
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
236-489 3.13e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 49.69  E-value: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    236 RSLAEACSEGDVNAVRKLLIEGRSVNEHTEE--GESLLCLACSAG-YYELAQVLLamhaNVEDRGIKGDiTPLMAAANGg 312
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLL----NLSCRGAVGD-TLLHAISLE- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    313 HVKIVKLLLAHKADvnAQSSTGNTALTYACAGG--YVDvvkvllesgasiedhnengHTPLMEAGSAGHVEVARLLLENG 390
Cdd:TIGR00870   93 YVDAVEAILLHLLA--AFRKSGPLELANDQYTSefTPG-------------------ITALHLAAHRQNYEIVKLLLERG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    391 AGINT--HSNEFKESALT---------LACYK--GHLEMVRFLLEAGADQEhKTDEM-----HTALMEA----------- 441
Cdd:TIGR00870  152 ASVPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelsc 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 38683807    442 -CMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 489
Cdd:TIGR00870  231 qMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
341-494 5.43e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 5.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    341 ACAGGYVDVVKVLLESGAS--IEDHNENGHTPLMEAGSAG-HVEVARLLLENGAGINThsnefKESALTLAC--YKGHLE 415
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV-----GDTLLHAISleYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    416 MVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ESP 470
Cdd:TIGR00870   99 AILLHLLAAFRKsgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgESP 178
                          170       180
                   ....*....|....*....|....
gi 38683807    471 LTLAACGGHVELAALLIERGASLE 494
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADIL 202
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
794-886 7.99e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.88  E-value: 7.99e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807     794 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEK---IEELNKTREEQIQKKQKILEEL 869
Cdd:smart00935    5 DVQ-KILQESPA--GKAAQKQLeKEFKKRQAELEKLEKELQKLK----EKLQKDAatlSEAAREKKEKELQKKVQEFQRK 77
                            90
                    ....*....|....*...
gi 38683807     870 QKV-ERELQLKTQQQLKK 886
Cdd:smart00935   78 QQKlQQDLQKRQQEELQK 95
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
334-362 2.02e-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: 2.02e-04
                            10        20
                    ....*....|....*....|....*....
gi 38683807     334 GNTALTYACAGGYVDVVKVLLESGASIED 362
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
1726-1802 3.42e-04

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 46.15  E-value: 3.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807 1726 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqkDktgDRIITIrGGT--ESTRQATQLINALIKDPdkEIDE 1802
Cdd:COG1185  549 RIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIE---D---DGTVKI-AATdgEAAEKAIERIEGITAEP--EVGE 618
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
822-887 4.02e-04

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 40.71  E-value: 4.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807  822 IKEaiEKNAQLQSLElahaDQLTKEKIEElNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQ 887
Cdd:cd22249    7 IRE--EYEAQLKKLE----EERRKEREEE-EKASEELIRKLQEEEERQRKREREEQLKQDEELAKQ 65
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
1726-1802 4.56e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.81  E-value: 4.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807  1726 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDPdkEIDE 1802
Cdd:PRK11824  554 RIETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIED------DGTVKIAATDgEAAEAAKERIEGITAEP--EVGE 623
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
805-1008 5.89e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  805 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTR-----EEQIQKKQKILEELQKVERELQLK 879
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEA 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  880 TQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLLTPVGVGEQLSEGDYARLQQVDPVLLKDEPQQtAAQMGFAPIQPLAMP 959
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLE 508
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 38683807  960 QALPLAAGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQ 1008
Cdd:COG1196  509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1075-1113 1.04e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 1.04e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 38683807   1075 IDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRD 1113
Cdd:pfam12796   53 ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1082-1110 1.29e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.29e-03
                            10        20
                    ....*....|....*....|....*....
gi 38683807    1082 NHDTALTLACAGGHEELVQTLLERGASIE 1110
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SCS2 COG5066
VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and ...
2076-2182 9.89e-03

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


Pssm-ID: 227398 [Multi-domain]  Cd Length: 242  Bit Score: 40.33  E-value: 9.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 2076 EQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPV 2155
Cdd:COG5066  121 SEEEISKNVHECSEDRGAAVLLVEMPTLLNILYLEVRFFVNQKEVPAEPETQPPVQVKKEEVPPVTQKTVPHENEKQTSV 200
                         90       100
                 ....*....|....*....|....*..
gi 38683807 2156 TYPMPQTPMGCPQPTPKmETPAIRPPP 2182
Cdd:COG5066  201 STPKPQNQIKEAATVPA-ENEPSSMPI 226
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
385-666 1.79e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 207.50  E-value: 1.79e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  385 LLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPA 464
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  465 DSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCG 544
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAAN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  545 GFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGA 621
Cdd:COG0666  164 GNLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 38683807  622 DLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHT 666
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
414-699 5.08e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 206.34  E-value: 5.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  414 LEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASL 493
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  494 EEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLIKAGADIEL---GCSTPLME 570
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAqdnDGNTPLHL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  571 AAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLI 650
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 38683807  651 SKGANVNRtTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGST 699
Cdd:COG0666  240 EAGADLNA-KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1102-1390 2.38e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.64  E-value: 2.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1102 LLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNV 1181
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1182 SDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACF 1261
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1262 QGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIG 1341
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 38683807 1342 RGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1390
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-465 4.24e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.87  E-value: 4.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  184 IGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEH 263
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  264 TEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACA 343
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  344 GGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEA 423
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 38683807  424 GADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 465
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
347-634 4.99e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.48  E-value: 4.99e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  347 VDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFkESALTLACYKGHLEMVRFLLEAGAD 426
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALG-ALLLLAAALAGDLLVALLLLAAGAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  427 QEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLME 506
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  507 AAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLIKAGADIELGCS---TPLMEAAQEGHLELVKYL 583
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNdgkTALDLAAENGNLEIVKLL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 38683807  584 LAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPL 634
Cdd:COG0666  239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
314-601 4.31e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.79  E-value: 4.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  314 VKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGI 393
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  394 NThSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 473
Cdd:COG0666   81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  474 AACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFL 553
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 38683807  554 IKAGADIELGC---STPLMEAAQEGHLELVKYLLAAGANVHATTATGDTAL 601
Cdd:COG0666  239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1065-1313 4.59e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 191.71  E-value: 4.59e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1065 AMLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEA 1144
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1145 QSERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLML 1224
Cdd:COG0666  116 RDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR--DNDGETPLHL 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1225 AAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVL 1304
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271

                 ....*....
gi 38683807 1305 LDKGADVNA 1313
Cdd:COG0666  272 LLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1066-1357 1.83e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.17  E-value: 1.83e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1066 MLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQ 1145
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1146 SERtKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLA 1225
Cdd:COG0666   84 DDG-GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1226 AMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1305
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 38683807 1306 DKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPL 1357
Cdd:COG0666  240 EAGADLNAK--DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-438 3.92e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 174.76  E-value: 3.92e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  153 LLLSGTADGADLRTVDPETQARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQ 232
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  233 SDNRSLAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGG 312
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  313 HVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAG 392
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 38683807  393 INtHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTAL 438
Cdd:COG0666  245 LN-AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1198-1407 2.63e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 2.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1198 IIKILLNAGAEINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLLDRKAN 1277
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADA-LGALLLLAAALAGDLLVALLLLAAGAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1278 VEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPL 1357
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA--RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 38683807 1358 WLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVK 1407
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
1726-1796 1.56e-40

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


Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 144.51  E-value: 1.56e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683807 1726 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1796
Cdd:cd22502    1 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 71
KH-I_ANKHD1 cd22503
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ...
1726-1807 3.24e-37

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


Pssm-ID: 411931  Cd Length: 83  Bit Score: 135.65  E-value: 3.24e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1726 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDKEIDELIP 1805
Cdd:cd22503    1 RSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIP 80

                 ..
gi 38683807 1806 KN 1807
Cdd:cd22503   81 RN 82
KH-I_MASK cd22404
type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family ...
1726-1796 8.07e-37

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


Pssm-ID: 411832 [Multi-domain]  Cd Length: 71  Bit Score: 133.87  E-value: 8.07e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683807 1726 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1796
Cdd:cd22404    1 KSKKVTVPNSAISRVIGRGGCNINAIREVSGAHIEIDKQKGEQGDRRITIKGSADATRQAAQLINALIKDP 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
1097-1403 1.23e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 116.28  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1097 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVG--VVEILLDNGADIEAQsERTKDTPL-SLACSGGRQEVVELLLAR 1172
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLhLYLHYSSEKVkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1173 GANKEHRNVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRtgSKLGISPL--MLAAMNGHTAAVKLLLDMGSDINAqI 1248
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNAL--DLYGMTPLavLLKSRNANVELLRLLIDAGADVYA-V 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1249 ETNRNTALTLAC--FQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRV--LLDKGADVNAppvpssrdtal 1324
Cdd:PHA03095  184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA----------- 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807  1325 tiaadkghykfcelligrgahidvRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVR 1403
Cdd:PHA03095  253 ------------------------RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1152-1438 3.36e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.38  E-value: 3.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1152 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYV-----NIIKILLNAGAEINSrtGSKLGISPLMLAA 1226
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA--PDNNGITPLLYAI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1227 MN--GHTAAVKLLLDMGSDINAqietnrntaltlacfqgrtevvsllldrkanvehRAKTGLTPLMEAASGGYA--EVGR 1302
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNI----------------------------------KNSDGENLLHLYLESNKIdlKILK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1303 VLLDKGADVNAppvpssrdtaltiaADKghykfCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAA 1382
Cdd:PHA03100  161 LLIDKGVDINA--------------KNR-----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683807  1383 DNRKITPLMAAFRKGHVKVVRYLvkeVNQFPSDS---ECMRY-----IATITDKEMLKKCHLCM 1438
Cdd:PHA03100  222 NKYGDTPLHIAILNNNKEIFKLL---LNNGPSIKtiiETLLYfkdkdLNTITKIKMLKKSIMYM 282
PHA03095 PHA03095
ankyrin-like protein; Provisional
240-560 1.88e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.73  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   240 EACSEGDVNAVRKLLIEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGIKGDiTPLMA-AANGGHVK 315
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   316 IVKLLLAHKADVNAQSSTGNTALtYACAGGY---VDVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLLLEN 389
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   390 GAGI-----------NTHSNEFKESAltlacykghlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 456
Cdd:PHA03095  177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   457 GAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQgaNINAQT-EETQE 535
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK--NPSAETvAATLN 324
                         330       340
                  ....*....|....*....|....*....
gi 38683807   536 TA----LTLACCGGFLEVADFLIKAGADI 560
Cdd:PHA03095  325 TAsvagGDIPSDATRLCVAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
305-395 2.85e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 2.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    305 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASieDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 38683807    385 LLLENGAGINT 395
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
568-659 4.68e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.26  E-value: 4.68e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    568 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQaGADLEHESEgGRTPLMKAARAGHVCTVQ 647
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 38683807    648 FLISKGANVNRT 659
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
447-625 7.26e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 107.06  E-value: 7.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   447 VEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-----ELAALLIERGASLEEVNDEGYTPLMEAARE--GHEEMVALL 519
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   520 LGQGANINAQTEeTQETALTLA--CCGGFLEVADFLIKAGADI----------ELGC---------STPLMEAAQEGHLE 578
Cdd:PHA03100  128 LDNGANVNIKNS-DGENLLHLYleSNKIDLKILKLLIDKGVDInaknrvnyllSYGVpinikdvygFTPLHYAVYNNNPE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 38683807   579 LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEH 625
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
438-529 5.94e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 5.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    438 LMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASleEVNDEGYTPLMEAAREGHEEMVA 517
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 38683807    518 LLLGQGANINAQ 529
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1222-1313 6.24e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 6.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1222 LMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDrKANVEHRAKtGLTPLMEAASGGYAEVG 1301
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 38683807   1302 RVLLDKGADVNA 1313
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
396-704 8.12e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 101.64  E-value: 8.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   396 HSNEFKESAL---TLACYKGHLEMVRFLLEAGADQEHK----TDEMHTALMEACMDGhVEVARLLLDSGAQVNMPADSFE 468
Cdd:PHA03095    6 SVDIIMEAALydyLLNASNVTVEEVRRLLAAGADVNFRgeygKTPLHLYLHYSSEKV-KDIVRLLLEAGADVNAPERCGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   469 SPLTLAACGGHVE-LAALLIERGASLEEVNDEGYTPLMEAAR--EGHEEMVALLLGQGANINAqTEETQETALtlaccgg 545
Cdd:PHA03095   85 TPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNA-LDLYGMTPL------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   546 flevADFLIKAGADIELgcstplmeaaqeghlelVKYLLAAGANVHATTATGDTALTYACENGHTDVADV--LLQAGADL 623
Cdd:PHA03095  157 ----AVLLKSRNANVEL-----------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDP 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   624 EHESEGGRTPLMKAArAGHVCT---VQFLISKGANVNRTTaNNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTM 700
Cdd:PHA03095  216 AATDMLGNTPLHSMA-TGSSCKrslVLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                  ....
gi 38683807   701 LIEA 704
Cdd:PHA03095  294 LSLM 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
238-623 1.27e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 102.83  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   238 LAEACSEGDV--NAVRKLLIEGRSVNEHTEEGESLLclacsagyyelAQVLLAMHANVEDRGIKGdITPLMAAANGGHVK 315
Cdd:PHA02876  125 LKEAISGNDIhyDKINESIEYMKLIKERIQQDELLI-----------AEMLLEGGADVNAKDIYC-ITPIHYAAERGNAK 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   316 IVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIedhNENGHTpLMEAGSAGHVEVARLLLENGAGINT 395
Cdd:PHA02876  193 MVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI---NKNDLS-LLKAIRNEDLETSLLLYDAGFSVNS 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   396 hSNEFKESALTLACYKGHL-EMVRFLLEAGADQEHKTDEMHTALMEACMDGH-VEVARLLLDSGAQVNMPADSFESPLTL 473
Cdd:PHA02876  269 -IDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQ 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   474 AAC-GGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQeTALTLACCGG--FLEVA 550
Cdd:PHA02876  348 ASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTnpYMSVK 426
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807   551 DfLIKAGADIELG---CSTPLMEAAQEG-HLELVKYLLAAGANVHATTATGDTALTYACenGHTDVADVLLQAGADL 623
Cdd:PHA02876  427 T-LIDRGANVNSKnkdLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
338-430 4.76e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 4.76e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    338 LTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENgagINTHSNEFKESALTLACYKGHLEMV 417
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 38683807    418 RFLLEAGADQEHK 430
Cdd:pfam12796   78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
371-461 8.13e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 8.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    371 LMEAGSAGHVEVARLLLENGAGINTHsNEFKESALTLACYKGHLEMVRFLLEaGADQEHKTDEMhTALMEACMDGHVEVA 450
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIV 77
                           90
                   ....*....|.
gi 38683807    451 RLLLDSGAQVN 461
Cdd:pfam12796   78 KLLLEKGADIN 88
PHA03100 PHA03100
ankyrin repeat protein; Provisional
289-528 1.12e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   289 MHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYV-----DVVKVLLESGASIEDH 363
Cdd:PHA03100   23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   364 NENGHTPLMEAGSA--GHVEVARLLLENGAGINTHSNEFKES-ALTLACYKGHLEMVRFLLEAGADQEHKTDemhtalme 440
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLlHLYLESNKIDLKILKLLIDKGVDINAKNR-------- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   441 acmdghVEvarLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLL 520
Cdd:PHA03100  175 ------VN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245

                  ....*...
gi 38683807   521 GQGANINA 528
Cdd:PHA03100  246 NNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
1098-1394 1.56e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 98.98  E-value: 1.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1098 LVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIE------------AQSERTKDT------------- 1152
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvlecAVDSKNIDTikaiidnrsnink 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1153 -PLSL--ACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVN-IIKILLNAGAEINSRTGSklGISPLMLAAMN 1228
Cdd:PHA02876  240 nDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK--GETPLYLMAKN 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1229 GH-TAAVKLLLDMGSDINAQiETNRNTALTLACFQGR-TEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLD 1306
Cdd:PHA02876  318 GYdTENIRTLIMLGADVNAA-DRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1307 KGADVNAppVPSSRDTALTIA-ADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAA-NGGHLDVVQLLVQAGADVDAADN 1384
Cdd:PHA02876  397 YGADIEA--LSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINI 474
                         330
                  ....*....|
gi 38683807  1385 RKITPLMAAF 1394
Cdd:PHA02876  475 QNQYPLLIAL 484
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1187-1281 2.54e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 2.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1187 LSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHTAAVKLLLDMgsdINAQIETNRNTALTLACFQGRTE 1266
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*
gi 38683807   1267 VVSLLLDRKANVEHR 1281
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1096-1280 2.94e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 2.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1096 EELVQTLLERGASIEHRDKKGFTPLILAATAGHV-----GVVEILLDNGADIEAQSERTkDTPLSLACSGGRQ--EVVEL 1168
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG-ITPLLYAISKKSNsySIVEY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1169 LLARGANKEHRNVSDYTPLSLAASGGYV--NIIKILLNAGAEINSRT--------GSKL------GISPLMLAAMNGHTA 1232
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNrvnyllsyGVPInikdvyGFTPLHYAVYNNNPE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 38683807  1233 AVKLLLDMGSDINAqIETNRNTALTLACFQGRTEVVSLLLDRKANVEH 1280
Cdd:PHA03100  207 FVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
504-593 6.52e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 6.52e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    504 LMEAAREGHEEMVALLLGQGANINAQTEETQeTALTLACCGGFLEVADFLI-KAGADIELGCSTPLMEAAQEGHLELVKY 582
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLLeHADVNLKDNGRTALHYAARSGHLEIVKL 79
                           90
                   ....*....|.
gi 38683807    583 LLAAGANVHAT 593
Cdd:pfam12796   80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
601-693 7.47e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 7.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    601 LTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKgANVNRTtaNNDHTVLSLACAGGHLAVV 680
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK--DNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 38683807    681 ELLLAHGADPTHR 693
Cdd:pfam12796   78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1154-1247 1.76e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1154 LSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNaGAEINSRTGsklGISPLMLAAMNGHTAA 1233
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN---GRTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 38683807   1234 VKLLLDMGSDINAQ 1247
Cdd:pfam12796   77 VKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1097-1250 1.83e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.96  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1097 ELVQTLLERGASIEHRDKKGFTPLILAATA--GHVGVVEILLDNGADIEAQSERTKdTPLSLACSGGRQ--EVVELLLAR 1172
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKIdlKILKLLIDK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1173 GA--NKEHR--------------NVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTgsKLGISPLMLAAMNGHTAAVKL 1236
Cdd:PHA03100  166 GVdiNAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN--KYGDTPLHIAILNNNKEIFKL 243
                         170
                  ....*....|....
gi 38683807  1237 LLDMGSDINAQIET 1250
Cdd:PHA03100  244 LLNNGPSIKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
312-634 2.01e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.87  E-value: 2.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   312 GHVKIVKLLLAHKAD-VNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENG 390
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   391 agINThsnefkeSALTLACYKGhlEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 470
Cdd:PHA02874   92 --VDT-------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   471 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQteetqetaltlaCCGGFleva 550
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK------------CKNGF---- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   551 dflikagadielgcsTPLMEAAQegHLELVKYLLAAGANVHATTATGDTALTYA----CEnghTDVADVLLQAGADLEHE 626
Cdd:PHA02874  225 ---------------TPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADISIK 284

                  ....*...
gi 38683807   627 SEGGRTPL 634
Cdd:PHA02874  285 DNKGENPI 292
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1087-1180 2.14e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 2.14e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1087 LTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNgADIEAQSErtKDTPLSLACSGGRQEVV 1166
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 38683807   1167 ELLLARGANKEHRN 1180
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
346-652 2.31e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   346 YVDVVKVLLESGASIEDHNENGHTPL---MEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLE 422
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   423 AGADQEHKTDEMHTALmEACMDG---HVEVARLLLDSGAQVNmpaDSFESPLTLAAC-----GGHVELAALLIERGASLE 494
Cdd:PHA03095  106 AGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVN---ALDLYGMTPLAVllksrNANVELLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   495 EVNDEGYTPLmeaaregheemvalllgqgaNINAQTEETQETaltlaccggfleVADFLIKAGAD---IELGCSTPLMEA 571
Cdd:PHA03095  182 AVDDRFRSLL--------------------HHHLQSFKPRAR------------IVRELIRAGCDpaaTDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   572 AQEGHLE--LVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFL 649
Cdd:PHA03095  230 ATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309

                  ...
gi 38683807   650 ISK 652
Cdd:PHA03095  310 LAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
471-562 5.66e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 5.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    471 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLgQGANINAQTEetQETALTLACCGGFLEVA 550
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN--GRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 38683807    551 DFLIKAGADIEL 562
Cdd:pfam12796   78 KLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1324-1407 1.09e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 1.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1324 LTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQaGADVDAADNRKiTPLMAAFRKGHVKVVR 1403
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVK 78

                   ....
gi 38683807   1404 YLVK 1407
Cdd:pfam12796   79 LLLE 82
PHA02876 PHA02876
ankyrin repeat protein; Provisional
349-719 1.17e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 93.20  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   349 VVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEfKESALTLACYKGHLEMVRFLLeagaDQE 428
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAII----DNR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   429 HKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-ELAALLIERGASLEEVNDEGYTPLMEA 507
Cdd:PHA02876  235 SNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLM 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   508 AREGHE-EMVALLLGQGANINAqteetqetaltlaccggflevADFLIkagadielgcSTPLMEAAQ-EGHLELVKYLLA 585
Cdd:PHA02876  315 AKNGYDtENIRTLIMLGADVNA---------------------ADRLY----------ITPLHQASTlDRNKDIVITLLE 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   586 AGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGH-VCTVQFLISKGANVNrtTANND 664
Cdd:PHA02876  364 LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVN--SKNKD 441
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807   665 -HTVLSLACAGG-HLAVVELLLAHGADPTH-RLKDGSTMLIEAakgGHTSVVCYLLDY 719
Cdd:PHA02876  442 lSTPLHYACKKNcKLDVIEMLLDNGADVNAiNIQNQYPLLIAL---EYHGIVNILLHY 496
PHA03100 PHA03100
ankyrin repeat protein; Provisional
250-463 1.52e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   250 VRKLLIEGRSVNEHTEEGESLLCLACSAGYY-----ELAQVLLAMHANVeDRGIKGDITPLMAAANG--GHVKIVKLLLA 322
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV-NAPDNNGITPLLYAISKksNSYSIVEYLLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   323 HKADVNAQSSTGNTALTYACAGGYVDV------------------VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PHA03100  130 NGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   385 LLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH--------KTDEMHTALMEAcMDGHVEVARLLLDS 456
Cdd:PHA03100  210 YLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKDLNTITKIK-MLKKSIMYMFLLDP 287

                  ....*..
gi 38683807   457 GAQVNMP 463
Cdd:PHA03100  288 GFYKNRK 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1289-1383 2.32e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 2.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1289 LMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLIgrgAHIDVRNK-KGNTPLWLAANGGHLD 1367
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANL--QDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKdNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 38683807   1368 VVQLLVQAGADVDAAD 1383
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
1073-1316 5.80e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.70  E-value: 5.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1073 IDIDAqTESNHDTAL-TLACAGGHEELVQTLLERGASIEHRDKKGFTPL--ILAATAGHVGVVEILLDNGADIEAQSERT 1149
Cdd:PHA03095   74 ADVNA-PERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1150 KdTPLS--------------LACSGG-----------------------RQEVVELLLARGANKEHRNVSDYTPLSLAAS 1192
Cdd:PHA03095  153 M-TPLAvllksrnanvellrLLIDAGadvyavddrfrsllhhhlqsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMAT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1193 GGYVNIIKI--LLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrNTALTLACFQGRTEVVSL 1270
Cdd:PHA03095  232 GSSCKRSLVlpLLIAGISINAR--NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG-NTPLSLMVRNNNGRAVRA 308
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 38683807  1271 LLDRKANVEHRAKTgLTPLMEAASGGYAEVGR-----VLLDKGADVNAPPV 1316
Cdd:PHA03095  309 ALAKNPSAETVAAT-LNTASVAGGDIPSDATRlcvakVVLRGAFSLLPEPI 358
PHA02874 PHA02874
ankyrin repeat protein; Provisional
1126-1455 1.96e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 87.71  E-value: 1.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1126 AGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNA 1205
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1206 GAEinsrtgsklgISPLMLAAMNGHTaaVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTG 1285
Cdd:PHA02874   91 GVD----------TSILPIPCIEKDM--IKTILDCGIDVNIK-DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1286 LTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLA----- 1360
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVK--DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiihnr 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1361 ----------------ANGG-----------HLDVVQLLVQAGADVDAADNRKITPLMAAFRK-GHVKVVR------YLV 1406
Cdd:PHA02874  236 saiellinnasindqdIDGStplhhainppcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKdiianaVLI 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 38683807  1407 KEVNQFPsDSECMRYIATITDKEMLKKCHLCMESIVQAKdRQAAEANKN 1455
Cdd:PHA02874  316 KEADKLK-DSDFLEHIEIKDNKEFSDFIKECNEEIEDMK-KTKCGCDKN 362
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1085-1277 2.25e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.35  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1085 TALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQE 1164
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1165 VVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGskLGISPLMLAAMNGHTAAVKLLLDMGSDI 1244
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC--CGCTPLIIAMAKGDIAICKMLLDSGANI 194
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 38683807  1245 NAqieTNRNTALTLACF---QGRTEVVSLLLDRKAN 1277
Cdd:PHA02875  195 DY---FGKNGCVAALCYaieNNKIDIVRLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
514-727 2.25e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.77  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   514 EMVALLLGQGANINaQTEETQETALT--LAC-CGGFLEVADFLIKAGADIEL----GCsTPL---MEAAQEghLELVKYL 583
Cdd:PHA03095   28 EEVRRLLAAGADVN-FRGEYGKTPLHlyLHYsSEKVKDIVRLLLEAGADVNApercGF-TPLhlyLYNATT--LDVIKLL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   584 LAAGANVHATTATGDTAL-TYAC-ENGHTDVADVLLQAGADLEHESEGGRTPL---MKAARAgHVCTVQFLISKGANVnR 658
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhVYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDAGADV-Y 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   659 TTANNDHTVLSLacaggHL-------AVVELLLAHGADPTHRLKDGSTMLIEAAKGG--HTSVVCYLL------DYPNNL 723
Cdd:PHA03095  182 AVDDRFRSLLHH-----HLqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLiagisiNARNRY 256

                  ....
gi 38683807   724 LSAP 727
Cdd:PHA03095  257 GQTP 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
238-330 2.40e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 2.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGikgdITPLMAAANGGHVKI 316
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNG----RTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 38683807    317 VKLLLAHKADVNAQ 330
Cdd:pfam12796   77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1256-1350 3.12e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 3.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1256 LTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKgADVNappVPSSRDTALTIAADKGHYKF 1335
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN---LKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 38683807   1336 CELLIGRGAHIDVRN 1350
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1727-1791 5.11e-17

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


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 77.32  E-value: 5.11e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807   1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1791
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
1266-1407 7.73e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 7.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1266 EVVSLLLDRKANVEHR---AKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALtiaadkgHYKFC------ 1336
Cdd:PHA03095   28 EEVRRLLAAGADVNFRgeyGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAP--ERCGFTPL-------HLYLYnattld 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807  1337 --ELLIGRGAHIDVRNKKGNTPL--WLAANGGHLDVVQLLVQAGADVDAADNRKITPLmAAFRKGH---VKVVRYLVK 1407
Cdd:PHA03095   99 viKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPL-AVLLKSRnanVELLRLLID 175
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
1728-1790 8.40e-16

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


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 73.87  E-value: 8.40e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807 1728 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLIN 1790
Cdd:cd00105    1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGERVVTITGTPEAVEKAKELIE 63
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
305-473 1.24e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 83.38  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   305 LMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   385 LLLENGAGINTHSNefkESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVN-MP 463
Cdd:PLN03192  609 ILYHFASISDPHAA---GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkAN 685
                         170
                  ....*....|
gi 38683807   464 ADSFESPLTL 473
Cdd:PLN03192  686 TDDDFSPTEL 695
PHA02875 PHA02875
ankyrin repeat protein; Provisional
337-559 4.67e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 4.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   337 ALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFkESALTLACYKGHLEM 416
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   417 VRFLLEAG--ADQEHKTDEMhTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLE 494
Cdd:PHA02875   84 VEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807   495 EVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTLACCGGFLEVADFLIKAGAD 559
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
634-719 5.23e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 5.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    634 LMKAARAGHVCTVQFLISKGANVNRTTANNdHTVLSLACAGGHLAVVELLLAHgADPTHRLkDGSTMLIEAAKGGHTSVV 713
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNG-RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*.
gi 38683807    714 CYLLDY 719
Cdd:pfam12796   78 KLLLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
246-442 8.64e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.26  E-value: 8.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   246 DVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKA 325
Cdd:PHA02875   47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   326 DVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKESAL 405
Cdd:PHA02875  127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 38683807   406 TLACYKGHLEMVRFLLEAGADQEHKT---DEMHTALMEAC 442
Cdd:PHA02875  207 CYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDMIC 246
PHA02875 PHA02875
ankyrin repeat protein; Provisional
437-689 1.17e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.88  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   437 ALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAsLEEVNDEGY-TPLMEAAREGHEEM 515
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   516 VALLLGQGANINaqteetqetaltlaccggflevaDFLIKAGadielgcSTPLMEAAQEGHLELVKYLLAAGANVHATTA 595
Cdd:PHA02875   84 VEELLDLGKFAD-----------------------DVFYKDG-------MTPLHLATILKKLDIMKLLIARGADPDIPNT 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   596 TGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGG 675
Cdd:PHA02875  134 DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENN 213
                         250
                  ....*....|....
gi 38683807   676 HLAVVELLLAHGAD 689
Cdd:PHA02875  214 KIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
478-742 1.84e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   478 GHVELAALLIE-RGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTlACCGGFLEVADFLIKA 556
Cdd:PHA02874   12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLT-AIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   557 GADIELgCSTPLMEAaqeghlELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMK 636
Cdd:PHA02874   91 GVDTSI-LPIPCIEK------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   637 AARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLiEAAKGGHTSVVCYL 716
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL-HNAIIHNRSAIELL 241
                         250       260
                  ....*....|....*....|....*.
gi 38683807   717 LdypnNLLSAPPPDVTQLTPPSHDLN 742
Cdd:PHA02874  242 I----NNASINDQDIDGSTPLHHAIN 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1097-1396 2.13e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.38  E-value: 2.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1097 ELVQTLLERGASIEHRDKKGFTPL-ILAATAGHVGVVEILLDNGADIEAQSERTkdtpLSLACSGGRQEVVELLLARGAN 1175
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPDHRDLTPLhIICKEPNKLGMKEMIRSINKCSVFYTLVA----IKDAFNNRNVEIFKIILTNRYK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1176 KEHrnVSDYTPLSLAASGGYVN--IIKILLNAGAEINSRTGSKLGiSPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrN 1253
Cdd:PHA02878  127 NIQ--TIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTN-N 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1254 TALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMeaASGGYA---EVGRVLLDKGADVNAppvpssRDTALTIAAdk 1330
Cdd:PHA02878  203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH--ISVGYCkdyDILKLLLEHGVDVNA------KSYILGLTA-- 272
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807  1331 ghykfcelligrgAHIDVRNKkgntplwlaangghlDVVQLLVQAGADVDAADNRKITPLMAAFRK 1396
Cdd:PHA02878  273 -------------LHSSIKSE---------------RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1152-1344 4.29e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.95  E-value: 4.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1152 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSrTGSKLGISPLMLAAMNGHT 1231
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADD-VFYKDGMTPLHLATILKKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1232 AAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADV 1311
Cdd:PHA02875  116 DIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 38683807  1312 N----APPVpssrdTALTIAADKGHYKFCELLIGRGA 1344
Cdd:PHA02875  195 DyfgkNGCV-----AALCYAIENNKIDIVRLFIKRGA 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1157-1378 6.23e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 6.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1157 ACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGsklGI-SPLMLAAMNGHTAAVK 1235
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIeSELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1236 LLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPP 1315
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683807  1316 VPSSrdTALTIAADKGHYKFCELLIGRGAHIDVRNKKGN-TPLWLAANGGHLDVVQLLVQAGAD 1378
Cdd:PHA02875  166 CCGC--TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
1727-1792 6.98e-14

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


Pssm-ID: 411867 [Multi-domain]  Cd Length: 68  Bit Score: 68.41  E-value: 6.98e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINAL 1792
Cdd:cd22439    3 TQEITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEDGSTERSVTITGTPEAVSLAQYLINAR 68
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
1729-1793 2.73e-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: 66.89  E-value: 2.73e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807 1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22462    2 EILIPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDSATGERIVLISGTPDQARHAQNLIEAFI 66
PHA02875 PHA02875
ankyrin repeat protein; Provisional
271-491 2.94e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.64  E-value: 2.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   271 LCLACSAGYYELAQVLLAMHANvEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVV 350
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGIN-PNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   351 KVLLESGASIED-HNENGHTPLMEAGSAGHVEVARLLLENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEH 429
Cdd:PHA02875   85 EELLDLGKFADDvFYKDGMTPLHLATILKKLDIMKLLIARGADPDI-PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807   430 KTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAdsfESPLTLAACGG----HVELAALLIERGA 491
Cdd:PHA02875  164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFG---KNGCVAALCYAiennKIDIVRLFIKRGA 226
KH smart00322
K homology RNA-binding domain;
1729-1793 3.37e-13

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 66.55  E-value: 3.37e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807    1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIP--GPGSEERVVEITGPPENVEKAAELILEIL 68
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1190-1407 4.02e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1190 AASGGYVNIIKILLNAGaeINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRnTALTLACFQGRTEVVS 1269
Cdd:PHA02875    9 AILFGELDIARRLLDIG--INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1270 LLLDRKANVEHRA-KTGLTPLMEAASGGYAEVGRVLLDKGADvnaPPVPSS-RDTALTIAADKGHYKFCELLIGRGAHID 1347
Cdd:PHA02875   86 ELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGAD---PDIPNTdKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683807  1348 VRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRK-ITPLMAAFRKGHVKVVRYLVK 1407
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA02875 PHA02875
ankyrin repeat protein; Provisional
312-540 5.33e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.87  E-value: 5.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   312 GHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGAsIEDHNENG-HTPLMEAGSAGHVEVARLLLENG 390
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   391 AGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 470
Cdd:PHA02875   92 KFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683807   471 LTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHE-EMVALLLGQGANINAQTEETQETALTL 540
Cdd:PHA02875  172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNIMFMIEGEECTIL 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1069-1145 6.01e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 6.01e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807   1069 IYPAIDIDAQTEsNHDTALTLACAGGHEELVQTLLERgASIEHRDkKGFTPLILAATAGHVGVVEILLDNGADIEAQ 1145
Cdd:pfam12796   17 LENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
449-684 2.61e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   449 VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGAN--I 526
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   527 NAQTEETQETALTLACCGGFLEVADFLIKagadielgcsTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACE 606
Cdd:PHA02874   97 LPIPCIEKDMIKTILDCGIDVNIKDAELK----------TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807   607 NGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHlAVVELLL 684
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM-NKCKNGFTPLHNAIIHNR-SAIELLI 242
PHA02876 PHA02876
ankyrin repeat protein; Provisional
1165-1406 2.66e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 2.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1165 VVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDI 1244
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD--DLSVLECAVDSKNIDTIKAIIDNRSNI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1245 NAQ----IETNRNTALtlacfqgrtEVVSLLLDRKANVEHRAKTGLTPLMEAASG-GYAEVGRVLLDKGADVNAPPVPSs 1319
Cdd:PHA02876  238 NKNdlslLKAIRNEDL---------ETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKG- 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1320 rDTALTIAADKGH-YKFCELLIGRGAHIDVRNKKGNTPLWLAAN-GGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKG 1397
Cdd:PHA02876  308 -ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                  ....*....
gi 38683807  1398 HVKVVRYLV 1406
Cdd:PHA02876  387 NVVIINTLL 395
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1131-1305 2.78e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1131 VVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 1210
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1211 SRtgSKLGISPLMLAAMNGHTAAV-KLLLDMGSDINAQIETNRNTALTLACFQGRteVVSLLLDRKANVEHRAKTGLTPL 1289
Cdd:PHA02878  229 AR--DKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPL 304
                         170
                  ....*....|....*..
gi 38683807  1290 MEAASGGYA-EVGRVLL 1305
Cdd:PHA02878  305 SSAVKQYLCiNIGRILI 321
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
482-749 3.22e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.59  E-value: 3.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   482 LAALLIERGASLEE---VNDEGYTPLMEAAREGHEEMVALLLGQ--GANINAQTEETQET-ALTLACCG--GFLEVadfL 553
Cdd:PLN03192  468 LSQLLRLKTSTLIEamqTRQEDNVVILKNFLQHHKELHDLNVGDllGDNGGEHDDPNMASnLLTVASTGnaALLEE---L 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   554 IKAGADIELGCS---TPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAgADLEHESEGG 630
Cdd:PLN03192  545 LKAKLDPDIGDSkgrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAG 623
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   631 RTpLMKAARAGHVCTVQFLISKGANVNrttaNNDH---TVLSLACAGGHLAVVELLLAHGADPTHRLKD---GSTMLIEA 704
Cdd:PLN03192  624 DL-LCTAAKRNDLTAMKELLKQGLNVD----SEDHqgaTALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELREL 698
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 38683807   705 AK----GGHTSVVCYLLDYPNNLLSAPPPDVTQLTPPSHDLNRAPRVPV 749
Cdd:PLN03192  699 LQkrelGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSI 747
PHA02878 PHA02878
ankyrin repeat protein; Provisional
236-426 3.31e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   236 RSLAEACSEGDVNAVRKLLIegrsvNEHTEEGESLLCLACSAGY-----YELAQVLLAMHANVEDRGIKGDITPLMAAAN 310
Cdd:PHA02878  103 VAIKDAFNNRNVEIFKIILT-----NRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   311 GGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL-MEAGSAGHVEVARLLLEN 389
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 38683807   390 GAGINTHSNEFKESALTLACYKGhlEMVRFLLEAGAD 426
Cdd:PHA02878  258 GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGAD 292
PHA02876 PHA02876
ankyrin repeat protein; Provisional
1039-1311 5.04e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.63  E-value: 5.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1039 NTPTHSIAasisqpQTPtpspiiSPSAMLP--IYPAIDIDAQTESNhDTALTLACAGGHE-ELVQTLLERGASIEHRDKK 1115
Cdd:PHA02876  274 NTPLHHAS------QAP------SLSRLVPklLERGADVNAKNIKG-ETPLYLMAKNGYDtENIRTLIMLGADVNAADRL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1116 GFTPLILAATaghvgvveilLDngadieaqseRTKDTPLSlacsggrqevvelLLARGANKEHRNVSDYTPLSLAASGGY 1195
Cdd:PHA02876  341 YITPLHQAST----------LD----------RNKDIVIT-------------LLELGANVNARDYCDKTPIHYAAVRNN 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1196 VNIIKILLNAGAEINSRTgSKLGIS-PLMLAAMNGHTaAVKLLLDMGSDINAQiETNRNTALTLACFQG-RTEVVSLLLD 1273
Cdd:PHA02876  388 VVIINTLLDYGADIEALS-QKIGTAlHFALCGTNPYM-SVKTLIDRGANVNSK-NKDLSTPLHYACKKNcKLDVIEMLLD 464
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 38683807  1274 RKANVEHRAKTGLTPLMEAAsgGYAEVGRVLLDKGADV 1311
Cdd:PHA02876  465 NGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
447-627 5.78e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.44  E-value: 5.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   447 VEVARLLLDSGAQVNMPADSFeSPLTLAACGGHVELAALLieRGASLEEVND-EGYTPLMEAAREGHEEMVALLLGQGAN 525
Cdd:PLN03192  507 LNVGDLLGDNGGEHDDPNMAS-NLLTVASTGNAALLEELL--KAKLDPDIGDsKGRTPLHIAASKGYEDCVLVLLKHACN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   526 INAQtEETQETALTLACCGGFLEVADFLIK--------AGADIelgcstpLMEAAQEGHLELVKYLLAAGANVHATTATG 597
Cdd:PLN03192  584 VHIR-DANGNTALWNAISAKHHKIFRILYHfasisdphAAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655
                         170       180       190
                  ....*....|....*....|....*....|
gi 38683807   598 DTALTYACENGHTDVADVLLQAGADLEHES 627
Cdd:PLN03192  656 ATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
303-354 5.94e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.68  E-value: 5.94e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683807    303 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLL 354
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1357-1411 1.00e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 1.00e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38683807   1357 LWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVKEVNQ 1411
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV 55
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1251-1407 1.15e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1251 NRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGA--DVNAPPVPSSrdtaLTIAA 1328
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIESE----LHDAV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1329 DKGHYKFCELLIGRGAHI-DVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVK 1407
Cdd:PHA02875   77 EEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
Ank_4 pfam13637
Ankyrin repeats (many copies);
564-617 1.18e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 1.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683807    564 CSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLL 617
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
1727-1796 1.57e-11

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: 61.95  E-value: 1.57e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDP 1796
Cdd:cd22434    3 TTQVTIPKDLAGSIIGKGGQRIRQIRHESGASIKIDEPLPGSEDRIITITGTQDQIQNAQYLLQNSVKQY 72
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
565-743 1.83e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 69.66  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  565 STPLMEAAQEGHLELVKYLL-AAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHE---SE--GGRTPLMKAA 638
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDlyQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  639 RAGHVCTVQFLISKGANVN--RTTAN------------NDHtVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEA 704
Cdd:cd22192   98 VNQNLNLVRELIARGADVVspRATGTffrpgpknliyyGEH-PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 38683807  705 AKGGHTSVVCYLLDYpnnLLSAPPPDvtQLTPPSHDLNR 743
Cdd:cd22192  177 VLQPNKTFACQMYDL---ILSYDKED--DLQPLDLVPNN 210
PHA02878 PHA02878
ankyrin repeat protein; Provisional
347-639 2.93e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 2.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   347 VDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLengAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGAD 426
Cdd:PHA02878   50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   427 QEHKTDEMHtaLMEACMDGHVE--VARLLLDSGAQVNM-PADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTP 503
Cdd:PHA02878  127 NIQTIDLVY--IDKKSKDDIIEaeITKLLLSYGADINMkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   504 LMEAAREGHEEMVALLLGQGANINAQTEetqetaltlacCGgflevadflikagadielgcSTPL-MEAAQEGHLELVKY 582
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENGASTDARDK-----------CG--------------------NTPLhISVGYCKDYDILKL 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807   583 LLAAGANVHA-TTATGDTALTYACENghTDVADVLLQAGADLEHESEGGRTPLMKAAR 639
Cdd:PHA02878  254 LLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02878 PHA02878
ankyrin repeat protein; Provisional
304-560 6.40e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 6.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   304 PLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESgaSIEDHNENGHTPLMEAGSAGHVEVA 383
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   384 RLLLengagINTHSNEfKESALTLACYKGH-----LEMVRFLLEAGADQEHKT-DEMHTALMEACMDGHVEVARLLLDSG 457
Cdd:PHA02878  118 KIIL-----TNRYKNI-QTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   458 AQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPL-MEAAREGHEEMVALLLGQGANINAQTEETQET 536
Cdd:PHA02878  192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLT 271
                         250       260
                  ....*....|....*....|....
gi 38683807   537 ALTLACCGGflEVADFLIKAGADI 560
Cdd:PHA02878  272 ALHSSIKSE--RKLKLLLEYGADI 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
369-584 1.05e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 67.35  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  369 TPLMEAGSAGHVE-VARLLLENGAGINTHSnEFKESALTLACYKGHLEMVRFLLEAGAD--QEHKTDEMH---TALMEAC 442
Cdd:cd22192   19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRG-ALGETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  443 MDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPL---- 504
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilv 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  505 MEAAREGHEEMVALLLGQGANINAQTEETQETALTLaccggflevadflikagadielgcsTPLMEAAQEGHLELVKYLL 584
Cdd:cd22192  178 LQPNKTFACQMYDLILSYDKEDDLQPLDLVPNNQGL-------------------------TPFKLAAKEGNIVMFQHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
1353-1406 1.87e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.87e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683807   1353 GNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLV 1406
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1220-1383 2.16e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.43  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1220 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRnTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAE 1299
Cdd:PLN03192  527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1300 VGRVLLDKGADVNappvPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADV 1379
Cdd:PLN03192  606 IFRILYHFASISD----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681

                  ....
gi 38683807  1380 DAAD 1383
Cdd:PLN03192  682 DKAN 685
KH-I_NOVA_rpt3 cd09031
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
1728-1789 3.66e-10

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


Pssm-ID: 411807 [Multi-domain]  Cd Length: 71  Bit Score: 57.97  E-value: 3.66e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807 1728 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1789
Cdd:cd09031    3 IELEVPENLVGAILGKGGKTLVEIQELTGARIQISKKGEfvpGTRNRKVTITGTPAAVQAAQYLI 67
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
229-407 4.04e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   229 NAGQSDNRSLAE----ACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDiTP 304
Cdd:PLN03192  516 NGGEHDDPNMASnlltVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN-TA 594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   305 LMAAANGGHVKIVKLLLAHKADVNAQssTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVAR 384
Cdd:PLN03192  595 LWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
                         170       180
                  ....*....|....*....|....
gi 38683807   385 LLLENGAGInTHSNEFKE-SALTL 407
Cdd:PLN03192  673 LLIMNGADV-DKANTDDDfSPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
1083-1136 4.74e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 4.74e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683807   1083 HDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL 1136
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
303-429 6.50e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 6.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   303 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESgASIEDHNENGHTpLMEAGSAGHVEV 382
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDLTA 637
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 38683807   383 ARLLLENGAGINTHSNEFKeSALTLACYKGHLEMVRFLLEAGADQEH 429
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA03100 PHA03100
ankyrin repeat protein; Provisional
245-366 6.96e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 6.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   245 GDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR-------GIKGDI------TPLMA 307
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsyGVPINIkdvygfTPLHY 198
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807   308 AANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNEN 366
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1176-1390 7.48e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 7.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1176 KEHR----NVSDYTPLSLAASGGYVNIIKILLNAGAEINsRTGSKlGISPLMLAAMNGHTAAVKLLLdmgSDINAQIETN 1251
Cdd:PHA02878   26 TENYstsaSLIPFIPLHQAVEARNLDVVKSLLTRGHNVN-QPDHR-DLTPLHIICKEPNKLGMKEMI---RSINKCSVFY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1252 RNTALTLACFQGRTEVV-SLLLDRKANVEhraKTGLTPLMEAASGGY--AEVGRVLLDKGADVNAPPvPSSRDTALTIAA 1328
Cdd:PHA02878  101 TLVAIKDAFNNRNVEIFkIILTNRYKNIQ---TIDLVYIDKKSKDDIieAEITKLLLSYGADINMKD-RHKGNTALHYAT 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807  1329 DKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1390
Cdd:PHA02878  177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1737-1791 9.40e-10

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


Pssm-ID: 411829 [Multi-domain]  Cd Length: 72  Bit Score: 56.85  E-value: 9.40e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807 1737 ISRVIGRGGCNINAIREFTGAHIDIDKQKDKT---GDRIITIRGGTESTRQATQLINA 1791
Cdd:cd22401   11 CGRLIGKDGRNIKKIMEDTNTKITISSLQDLTsynPERTITIKGSLEAMSEAESLISE 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
1320-1373 1.44e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.44e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683807   1320 RDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLV 1373
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_PCBP4_rpt3 cd22523
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
1727-1791 1.53e-09

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


Pssm-ID: 411951  Cd Length: 68  Bit Score: 56.06  E-value: 1.53e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1791
Cdd:cd22523    3 SQEFLIPNDLIGCVIGRQGSKISEIRQMSGAHIKIGNQTEGTSERHVTITGSPVSITLAQYLITT 67
Ank_2 pfam12796
Ankyrin repeats (3 copies);
668-721 1.65e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 1.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683807    668 LSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPN 721
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
1728-1793 1.84e-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: 56.19  E-value: 1.84e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807 1728 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKT--GDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22428    7 IEMKVPREAVGLIIGRQGATIKQIQKETGARIDFKDEGSGGelPERVLLIQGNPVQAQRAEEAIHQII 74
PHA02874 PHA02874
ankyrin repeat protein; Provisional
238-398 1.93e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLL----------------AMHANVEDRGIKGD 301
Cdd:PHA02874   39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekDMIKTILDCGIDVN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   302 I------TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAG 375
Cdd:PHA02874  119 IkdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
                         170       180
                  ....*....|....*....|...
gi 38683807   376 SAGHVEVARLLLENGAGINTHSN 398
Cdd:PHA02874  199 EYGDYACIKLLIDHGNHIMNKCK 221
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
1728-1789 2.02e-09

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


Pssm-ID: 411885 [Multi-domain]  Cd Length: 64  Bit Score: 55.54  E-value: 2.02e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807 1728 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQK-DKTGDRIITIRGGTESTRQATQLI 1789
Cdd:cd22457    1 QNISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAKAPhDETGERMFTITGTPEANDRALRLL 63
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1092-1170 2.18e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 2.18e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807  1092 AGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAqSERTKDTPLSLACSGGRQEVVELLL 1170
Cdd:PTZ00322   91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
334-387 2.24e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 2.24e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683807    334 GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLL 387
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
367-421 2.31e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 2.31e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38683807    367 GHTPLMEAGSAGHVEVARLLLENGAGINtHSNEFKESALTLACYKGHLEMVRFLL 421
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1145-1374 2.35e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1145 QSERTKDTPLSLACSGGRQEVVELLL--------ARGANKEhrnvsdyTPLSLAASGGYVNIIKILLNAGAE-INSRTGS 1215
Cdd:cd22192   12 QQKRISESPLLLAAKENDVQAIKKLLkcpscdlfQRGALGE-------TALHVAALYDNLEAAVVLMEAAPElVNEPMTS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1216 KL--GISPLMLAAMNGHTAAVKLLLDMGSDINaqieTNRNTALtlaCFqgrtevvsllLDRKANV----EHraktgltPL 1289
Cdd:cd22192   85 DLyqGETALHIAVVNQNLNLVRELIARGADVV----SPRATGT---FF----------RPGPKNLiyygEH-------PL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1290 MEAASGGYAEVGRVLLDKGADVNAppvpssRD----TALTIAADKGHYKF-CE---LLIGRGAHID------VRNKKGNT 1355
Cdd:cd22192  141 SFAACVGNEEIVRLLIEHGADIRA------QDslgnTVLHILVLQPNKTFaCQmydLILSYDKEDDlqpldlVPNNQGLT 214
                        250
                 ....*....|....*....
gi 38683807 1356 PLWLAANGGHLDVVQLLVQ 1374
Cdd:cd22192  215 PFKLAAKEGNIVMFQHLVQ 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
597-650 2.47e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.47e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683807    597 GDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLI 650
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
666-717 2.47e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.47e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683807    666 TVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLL 717
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
238-510 2.73e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSA----GYYELAQVLLAMHANVEDRGIKgditplmAAANGGH 313
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIK-------DAFNNRN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   314 VKIVKLLLAHKADVNAQSStgntaLTYACAGGYVD-----VVKVLLESGASIEDHNEN-GHTPLMEAGSAGHVEVARLLL 387
Cdd:PHA02878  114 VEIFKIILTNRYKNIQTID-----LVYIDKKSKDDiieaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   388 ENGAGINThSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEA---CMDghVEVARLLLDSGAQVNmpA 464
Cdd:PHA02878  189 SYGANVNI-PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVN--A 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 38683807   465 DSFESPLTLAACGGHVE-LAALLIERGASLEEVNDEGYTPLMEAARE 510
Cdd:PHA02878  264 KSYILGLTALHSSIKSErKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
KH-I_TDRKH_rpt2 cd22429
second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
1727-1789 4.25e-09

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


Pssm-ID: 411857 [Multi-domain]  Cd Length: 82  Bit Score: 55.42  E-value: 4.25e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGD--RIITIRGGTESTRQATQLI 1789
Cdd:cd22429    3 TEELHVPQRAVGRIIGRGGETIRSICRTSGAKVKCDRESDDTLDlvRLITITGTKKEVDAAKSLI 67
PHA02798 PHA02798
ankyrin-like protein; Provisional
314-531 5.13e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 61.39  E-value: 5.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   314 VKIVKLLLAHKADVNAQSSTGNTALT--------YACAggyVDVVKVLLESGASIEDHNENGHTP---LMEAGSAGHVEV 382
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCtilsnikdYKHM---LDIVKILIENGADINKKNSDGETPlycLLSNGYINNLEI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   383 ARLLLENGAGINTHSNeFKESALTLACYKGH---LEMVRFLLEAGAD-----QEHKTDEMHTALME--ACMDghVEVARL 452
Cdd:PHA02798  128 LLFMIENGADTTLLDK-DGFTMLQVYLQSNHhidIEIIKLLLEKGVDinthnNKEKYDTLHCYFKYniDRID--ADILKL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   453 LLDSGAQVNMPADSFESPL-----TLAACGGHVELAAL-LIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANI 526
Cdd:PHA02798  205 FVDNGFIINKENKSHKKKFmeylnSLLYDNKRFKKNILdFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDI 284

                  ....*
gi 38683807   527 NAQTE 531
Cdd:PHA02798  285 NIITE 289
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
1726-1796 6.08e-09

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


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 54.40  E-value: 6.08e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807 1726 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDP 1796
Cdd:cd02393    4 RITTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIED------DGTVTIFATDkESAEAAKAMIEDIVAEP 69
Ank_4 pfam13637
Ankyrin repeats (many copies);
469-520 1.07e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 1.07e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683807    469 SPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLL 520
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_NOVA_rpt2 cd22436
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
1729-1789 1.11e-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: 53.78  E-value: 1.11e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807 1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDK--TGDRIITIRGGTESTRQATQLI 1789
Cdd:cd22436    4 KILVPNSTAGMIIGKGGATIKAIMEQSGARVQISQKPESinLQERVVTVTGEPEANRKAVSLI 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
434-487 1.12e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.12e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683807    434 MHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLI 487
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1085-1204 1.23e-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: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1085 TALTLACAGGHEELVQTLLERGASIE---------HRDKK-----GFTPLILAATAGHVGVVEILLDNGADIEAQsERTK 1150
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLG 169
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807 1151 DTPL---------SLACsggrqEVVELLLARGANK-----EH-RNVSDYTPLSLAASGGYVNIIKILLN 1204
Cdd:cd22192  170 NTVLhilvlqpnkTFAC-----QMYDLILSYDKEDdlqplDLvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1241-1406 1.37e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1241 GSDINAQIETNRNTALTLacfqGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSsr 1320
Cdd:PLN03192  518 GEHDDPNMASNLLTVAST----GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG-- 591
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1321 DTALTIAADKGHYKFCELLIgRGAHIDVRNKKGNTpLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVK 1400
Cdd:PLN03192  592 NTALWNAISAKHHKIFRILY-HFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669

                  ....*.
gi 38683807  1401 VVRYLV 1406
Cdd:PLN03192  670 MVRLLI 675
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1730-1791 1.66e-08

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


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 53.09  E-value: 1.66e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807 1730 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqKDKTGDrIITIRGGTESTRQATQLINA 1791
Cdd:cd22452    6 IKVSPRYFGRIIGPGGSNINQIREKSGCFINVPK-KNKESD-VITLRGTKEGVEKAEEMIKK 65
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
2082-2337 1.91e-08

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.17  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2082 PPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMT-------VPPLATSSAPVAVPSTAP 2154
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTpqssqsqVPPGPSPAAPGQSQQRIH 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2155 VTYPMPQTPMGCP---QPTPK--METPAIRPPPHGTTAPHKNSASvqnssvavlsvnHIKRPH-SVPSSVQLPSTLSTQS 2228
Cdd:pfam03154  327 TPPSQSQLQSQQPpreQPLPPapLSMPHIKPPPTTPIPQLPNPQS------------HKHPPHlSGPSPFQMNSNLPPPP 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2229 ACQN----------SVHPANKPIAPNfSAPLPFGPFS----TLFENSPTSAhafwggsvvsSQSTPESMLSGKSSYLPNs 2294
Cdd:pfam03154  395 ALKPlsslsthhppSAHPPPLQLMPQ-SQQLPPPPAQppvlTQSQSLPPPA----------ASHPPTSGLHQVPSQSPF- 462
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 38683807   2295 dPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDSPyGSVTPSST 2337
Cdd:pfam03154  463 -PQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPP-SSASVSSS 503
PHA02878 PHA02878
ankyrin repeat protein; Provisional
346-731 2.86e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   346 YVDVVKVLLESGASIeDHNENGHT--------PLMEAGSAGHVEVARLLLENGAGINTHSNEFKeSALTLACYK----GH 413
Cdd:PHA02878    9 YTDNYETILKYIEYI-DHTENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDL-TPLHIICKEpnklGM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   414 LEMVRFLLEAGADQEHKtdemhtALMEACMDGHVEVARLLLdsgaqvnmpADSFESpltlaacgghvelaalliERGASL 493
Cdd:PHA02878   87 KEMIRSINKCSVFYTLV------AIKDAFNNRNVEIFKIIL---------TNRYKN------------------IQTIDL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   494 EEVNDEGYTPLMEAaregheEMVALLLGQGANINAQTEETQetaltlaccggflevadflikagadielgcSTPLMEAAQ 573
Cdd:PHA02878  134 VYIDKKSKDDIIEA------EITKLLLSYGADINMKDRHKG------------------------------NTALHYATE 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   574 EGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPL-MKAARAGHVCTVQFLISK 652
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807   653 GANVNRTTANNDHTVLSLACAGGHlaVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPNNLLSAPPPDV 731
Cdd:PHA02878  258 GVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334
Ank_4 pfam13637
Ankyrin repeats (many copies);
500-554 3.73e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 3.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38683807    500 GYTPLMEAAREGHEEMVALLLGQGANINAQTEEtQETALTLACCGGFLEVADFLI 554
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
630-684 5.35e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 5.35e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38683807    630 GRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDhTVLSLACAGGHLAVVELLL 684
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1189-1291 5.97e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 5.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1189 LAASGGYVNIiKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDINAqIETNRNTALTLACFQGRTEVV 1268
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCRDYD--GRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVV 164
                          90       100       110
                  ....*....|....*....|....*....|
gi 38683807  1269 SLLL-------DRKANVEHRAKTGLTPLME 1291
Cdd:PTZ00322  165 QLLSrhsqchfELGANAKPDSFTGKPPSLE 194
KH-I_PCBP1_2_rpt3 cd22521
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
1727-1791 6.01e-08

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


Pssm-ID: 411949  Cd Length: 76  Bit Score: 51.98  E-value: 6.01e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1791
Cdd:cd22521    6 SHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINA 70
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1725-1795 7.16e-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: 7.16e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807 1725 RRSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRI--------ITIRGGTESTRQATQLINALIKD 1795
Cdd:cd22446    6 KVTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGNYDEddddetveISIEGDAEGVELAKKEIEAIVKE 84
Ank_4 pfam13637
Ankyrin repeats (many copies);
403-454 8.00e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 8.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683807    403 SALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLL 454
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
314-618 8.46e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 57.44  E-value: 8.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   314 VKIVKLLLAHKADVNAQS--STGNTAL---TYACAGGYVDVVKVLLESGASIEDHNENGHTPLM---EAGSAGHVEVARL 385
Cdd:PHA02989   50 IKIVKLLIDNGADVNYKGyiETPLCAVlrnREITSNKIKKIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRF 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   386 LLENGAGINTHSNE--FKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVArllldsgaqvnmp 463
Cdd:PHA02989  130 LLSKGINVNDVKNSrgYNLLHMYLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMNIYLRNDIDVI------------- 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   464 adsfespltlaacggHVELAALLIERGASLEEvNDEGYTPLMEAAREGHEEMValllgqganinaqteeTQEtaltlacc 543
Cdd:PHA02989  197 ---------------SIKVIKYLIKKGVNIET-NNNGSESVLESFLDNNKILS----------------KKE-------- 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807   544 ggfLEVADFL---IKAGADIELGCsTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQ 618
Cdd:PHA02989  237 ---FKVLNFIlkyIKINKKDKKGF-NPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1730-1794 1.24e-07

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


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 51.26  E-value: 1.24e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807 1730 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRI--------ITIRGGTESTRQATQLINALIK 1794
Cdd:cd22447    8 VPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPADedddtmveVTITGDEFNVQHAKQRIEEIIS 80
KH-I_IGF2BP_rpt1 cd22400
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1732-1789 1.53e-07

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


Pssm-ID: 411828 [Multi-domain]  Cd Length: 68  Bit Score: 50.35  E-value: 1.53e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807 1732 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTG-DRIITIRGGTESTRQATQLI 1789
Cdd:cd22400    6 VPSEFVGAIIGKGGATIRQITQQTGARIDIHRKENAGAaEKAITIYGTPEGCSSACKQI 64
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1352-1384 1.59e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 49.21  E-value: 1.59e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 38683807   1352 KGNTPLWLAA-NGGHLDVVQLLVQAGADVDAADN 1384
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1729-1794 1.79e-07

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


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 50.35  E-value: 1.79e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807 1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqkDKTGDRIITIRGGTESTRQATQLINALIK 1794
Cdd:cd22449    7 KFDVPAKYVPHIIGKKGANINKLREEYGVKIDFE---DKTGEGNVEIKGSKKNVEEAKKRILSQID 69
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1074-1262 1.84e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1074 DIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSeRTKDTP 1153
Cdd:PHA02878  159 DINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD-KCGNTP 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1154 LSLACSggrqevvelllargankehrNVSDYtplslaasggyvNIIKILLNAGAEINSRTgSKLGISPLMLAAMNghTAA 1233
Cdd:PHA02878  238 LHISVG--------------------YCKDY------------DILKLLLEHGVDVNAKS-YILGLTALHSSIKS--ERK 282
                         170       180
                  ....*....|....*....|....*....
gi 38683807  1234 VKLLLDMGSDINAqIETNRNTALTLACFQ 1262
Cdd:PHA02878  283 LKLLLEYGADINS-LNSYKLTPLSSAVKQ 310
PHA02989 PHA02989
ankyrin repeat protein; Provisional
1164-1402 1.85e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 56.29  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1164 EVVELLLARGANKEHRNVSDyTPL------SLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAV--- 1234
Cdd:PHA02989   51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFN--GVSPIVCFIYNSNINNCdml 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1235 KLLLDMGSDINAQIETNRNTAL--TLACFQGRTEVVSLLLDRKANV-EHRAKTGLTP----LMEAASGGYAEVGRVLLDK 1307
Cdd:PHA02989  128 RFLLSKGINVNDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKK 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1308 GADVNAPPVPSSRDTALTIAADKGHYKFC-ELL--IGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADN 1384
Cdd:PHA02989  208 GVNIETNNNGSESVLESFLDNNKILSKKEfKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSK 287
                         250
                  ....*....|....*...
gi 38683807  1385 RKITPLMAAFRKGHVKVV 1402
Cdd:PHA02989  288 DGDTVLTYAIKHGNIDML 305
Ank_5 pfam13857
Ankyrin repeats (many copies);
1102-1157 1.92e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.92e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807   1102 LLERG-ASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKdTPLSLA 1157
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
308-387 2.01e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   308 AANGGHVKIvKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLL 387
Cdd:PTZ00322   90 AASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
794-893 2.02e-07

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 52.19  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    794 DVQgYITNQSPEsiVEEAQGKLTELEQRIKEAIE-KNAQLQSL--ELahadQLTKEKIEELNKTREEQIQKKQKILEELQ 870
Cdd:pfam03938    6 DMQ-KILEESPE--GKAAQAQLEKKFKKRQAELEaKQKELQKLyeEL----QKDGALLEEEREEKEQELQKKEQELQQLQ 78
                           90       100
                   ....*....|....*....|....
gi 38683807    871 -KVERELQLKTQQQLKKQYLEVKA 893
Cdd:pfam03938   79 qKAQQELQKKQQELLQPIQDKINK 102
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1732-1793 2.06e-07

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


Pssm-ID: 411824 [Multi-domain]  Cd Length: 68  Bit Score: 49.95  E-value: 2.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807 1732 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22396    7 VPDKMVGLIIGRGGEQINRLQAESGAKIQIAPDSGGLPERPCTLTGTPDAIETAKRLIDQIV 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
1220-1272 2.42e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 2.42e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 38683807   1220 SPLMLAAMNGHTAAVKLLLDMGSDINAQIEtNRNTALTLACFQGRTEVVSLLL 1272
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1727-1790 2.56e-07

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


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 49.51  E-value: 2.56e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLIN 1790
Cdd:cd22411    1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDL--PEENSDSDVITITGKKEDVEKARERIL 62
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
794-893 2.60e-07

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 52.92  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  794 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEKI---EELNKTREEQIQKKQKILEEL 869
Cdd:COG2825   30 DVQ-RILQESPE--GKAAQKKLeKEFKKRQAELQKLEKELQALQ----EKLQKEAAtlsEEERQKKERELQKKQQELQRK 102
                         90       100
                 ....*....|....*....|....*
gi 38683807  870 -QKVERELQLKTQQQLKKQYLEVKA 893
Cdd:COG2825  103 qQEAQQDLQKRQQELLQPILEKIQK 127
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
238-421 2.77e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.17  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  238 LAEACSEGDVNAVRKLLiEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDI----TPLMAAANG 311
Cdd:cd22192   21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLyqgeTALHIAVVN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  312 GHVKIVKLLLAHKADVNAQSST--------------GNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL----ME 373
Cdd:cd22192  100 QNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvLQ 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 38683807  374 AGSAGHVEVARLLLENGAGINTHS-----NEFKESALTLACYKGHLEMVRFLL 421
Cdd:cd22192  180 PNKTFACQMYDLILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
KH-I_BTR1_rpt3 cd22514
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ...
1727-1789 3.91e-07

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


Pssm-ID: 411942 [Multi-domain]  Cd Length: 71  Bit Score: 49.34  E-value: 3.91e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1789
Cdd:cd22514    2 SVTIGVPDEHIGAILGRGGRTINEIQQHSGARIKISDRGDfvsGTRNRKVTITGPQDAVQMAQYLL 67
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1220-1407 4.31e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.40  E-value: 4.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1220 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKT-----GLTPLMEAAS 1294
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1295 GGYAEVGRVLLDKGADVNAPPV------PSSR------DTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLwlaan 1362
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPRAtgtffrPGPKnliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL----- 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807 1363 ggHLDVVQ------------LLVQAGADVDAA-----DNRKITPLMAAFRKGHVKVVRYLVK 1407
Cdd:cd22192  174 --HILVLQpnktfacqmydlILSYDKEDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1795-2222 5.29e-07

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.54  E-value: 5.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1795 DPdKEIDElipKNRLKSSSANSKIGSSAPTTTAANTSLMGIKMTTVALSSTSQTATALTVPAISSASTH-KTIKNPVNNV 1873
Cdd:pfam03154  133 DP-KDIDQ---DNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAgPTPSAPSVPP 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1874 RPGFPVSLPLAYPPPQFAHALLAAQTfQQIRPPRLPMTHfggtfPPAQSTwgpfpvrPLSPARATNSPKPHMVPRHSNQN 1953
Cdd:pfam03154  209 QGSPATSQPPNQTQSTAAPHTLIQQT-PTLHPQRLPSPH-----PPLQPM-------TQPPPPSQVSPQPLPQPSLHGQM 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1954 SSGSQVNSAGSLTSSPTTTTSSSASTVPGTSTNGSPS-SPSVRRQLFVTVVKTSNATTTTVTTTASNNNTAPtnATYPMP 2032
Cdd:pfam03154  276 PPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGpSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPP--APLSMP 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2033 TAKehypvsSPSSPSPPAQPGGVSRNSPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPP 2112
Cdd:pfam03154  354 HIK------PPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPP 427
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2113 GS----VSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPvtypmPQTPMGCPQPTPKMETPAIRPPphgTTAP 2188
Cdd:pfam03154  428 PAqppvLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPP-----PITPPSGPPTSTSSAMPGIQPP---SSAS 499
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 38683807   2189 HKNSASVQNSSVAVLSVNHIK--------RPHSVPSSVQLPS 2222
Cdd:pfam03154  500 VSSSGPVPAAVSCPLPPVQIKeealdeaeEPESPPPPPRSPS 541
KH-I_PCBP3_rpt3 cd22522
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
1727-1791 5.77e-07

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


Pssm-ID: 411950 [Multi-domain]  Cd Length: 75  Bit Score: 49.34  E-value: 5.77e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINA 1791
Cdd:cd22522   10 THELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGSPANISLAQYLINA 74
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1079-1258 6.16e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 6.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1079 TESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQsERTKDTPLSLAC 1158
Cdd:PLN03192  521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR-DANGNTALWNAI 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1159 SGGRQEVVELLLARGANKEHRNVSDYtpLSLAASGGYVNIIKILLNAGAEINSRtgSKLGISPLMLAAMNGHTAAVKLLL 1238
Cdd:PLN03192  600 SAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSE--DHQGATALQVAMAEDHVDMVRLLI 675
                         170       180
                  ....*....|....*....|
gi 38683807  1239 DMGSDINAQIETNRNTALTL 1258
Cdd:PLN03192  676 MNGADVDKANTDDDFSPTEL 695
PHA03095 PHA03095
ankyrin-like protein; Provisional
1272-1407 7.87e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 7.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1272 LDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCE---LLIGRGAHIDV 1348
Cdd:PHA03095    1 DEEDESVDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNF--RGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807  1349 RNKKGNTPLWL-AANGGHLDVVQLLVQAGADVDAADNRKITPL---MAAFRKgHVKVVRYLVK 1407
Cdd:PHA03095   79 PERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvyLSGFNI-NPKVIRLLLR 140
KH-I_FUBP_rpt4 cd22399
fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1731-1790 9.81e-07

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


Pssm-ID: 411827 [Multi-domain]  Cd Length: 67  Bit Score: 47.99  E-value: 9.81e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683807 1731 SVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD-KTGDRIITIRGGTESTRQATQLIN 1790
Cdd:cd22399    5 LVPANKCGLVIGKGGETIRQINQQSGAHVELDRNPPpNPNEKLFIIRGNPQQIEHAKQLIR 65
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1069-1305 1.08e-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: 54.32  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1069 IYPAIDIDaqtESNHDTALTLACAGGHEELVQTLLERGAS--IEHRDKKGFTPLILAATAG-HVGVVEILLDNGADIEaq 1145
Cdd:TIGR00870    6 IVPAEESP---LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1146 serTKDTPLsLACSGGRQEVVELLLA-------RGANKEHRNVS-------DYTPLSLAASGGYVNIIKILLNAGAEINS 1211
Cdd:TIGR00870   81 ---VGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1212 R------------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIE---------------TNRNTALTLACFQgr 1264
Cdd:TIGR00870  157 RacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSlgntllhllvmenefKAEYEELSCQMYN-- 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 38683807   1265 tEVVSLL--LDRKANVEH-RAKTGLTPLMEAASGGYAEVGRVLL 1305
Cdd:TIGR00870  235 -FALSLLdkLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1732-1775 1.38e-06

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


Pssm-ID: 411887 [Multi-domain]  Cd Length: 69  Bit Score: 47.99  E-value: 1.38e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 38683807 1732 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITI 1775
Cdd:cd22459    8 CPVSKAGSVIGKGGEIIKQLRQETGARIKVEDGVPGTEERVITI 51
Ank_4 pfam13637
Ankyrin repeats (many copies);
1184-1238 1.46e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.46e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38683807   1184 YTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLAAMNGHTAAVKLLL 1238
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGN--GETALHFAASNGNVEVLKLLL 54
KH-I_FUBP2_rpt4 cd22488
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1731-1789 1.48e-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: 47.79  E-value: 1.48e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807 1731 SVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGD---RIITIRGGTESTRQATQLI 1789
Cdd:cd22488    5 SIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQPPPNGDpnfKLFIIRGSPQQIDHAKQLI 66
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
634-738 2.12e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   634 LMKAARAGHVCTVQFLISKGANVNrTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVV 713
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90       100
                  ....*....|....*....|....*...
gi 38683807   714 CYLLDYPNNLLSA---PPPDVTQLTPPS 738
Cdd:PTZ00322  165 QLLSRHSQCHFELganAKPDSFTGKPPS 192
PHA03247 PHA03247
large tegument protein UL36; Provisional
2025-2457 2.26e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2025 TNATYPMPTAKEHYPVSSPSSPSPPAQPGGVSRNSPLDcGSASPNKVASSSeqeaGSPPVVETTNTRPPNSSSSSGSSSA 2104
Cdd:PHA03247 2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRL----GRAAQASSPPQRPRRRAARPTVGSL 2695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2105 HSNQQQPPGSVSQEPRPPLQQSQVPPPEV----RMTVPPLATSSAPVAVPST-----APVTYPMPQTPMGCPQPTPKMET 2175
Cdd:PHA03247 2696 TSLADPPPPPPTPEPAPHALVSATPLPPGpaaaRQASPALPAAPAPPAVPAGpatpgGPARPARPPTTAGPPAPAPPAAP 2775
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2176 PAirPPPHGTTAPHKNSASVQNSSVAVLSvnhikRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIAPNfSAPLPFGPFS 2255
Cdd:PHA03247 2776 AA--GPPRRLTRPAVASLSESRESLPSPW-----DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT-APPPPPGPPP 2847
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2256 TlfensPTSAhafwGGSVVssqstPESMLSGKSsylpnsdPLHQSDTSKAPGFRPP---LQRPAPSPSGIVNMDSPYGSV 2332
Cdd:PHA03247 2848 P-----SLPL----GGSVA-----PGGDVRRRP-------PSRSPAAKPAAPARPPvrrLARPAVSRSTESFALPPDQPE 2906
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2333 TPssthlgnfasnisggqmygpgaplggapaaanfnRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSP-APSSVPLGS 2411
Cdd:PHA03247 2907 RP----------------------------------PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPlAPTTDPAGA 2952
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 38683807  2412 EKPSNVSQDRKVPVPIGTERSARIRQTGTSAPSVIGSNLSTSVGHS 2457
Cdd:PHA03247 2953 GEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTG 2998
PHA02989 PHA02989
ankyrin repeat protein; Provisional
1233-1434 2.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.82  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1233 AVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRA--KTGLTPLM---EAASGGYAEVGRVLLDK 1307
Cdd:PHA02989   18 ALEFLLRTGFDVNEEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGyiETPLCAVLrnrEITSNKIKKIVKLLLKF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1308 GADVNAPPVPSSRDTALTIAadKGHYKFCE---LLIGRGAHI-DVRNKKGNTPL--WLAANGGHLDVVQLLVQAGADV-D 1380
Cdd:PHA02989   98 GADINLKTFNGVSPIVCFIY--NSNINNCDmlrFLLSKGINVnDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfE 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807  1381 AADNRKITPLMAAFRKG----HVKVVRYLVK-----EVNQFPSDSECMRYIAtiTDKEMLKKC 1434
Cdd:PHA02989  176 KTSLYGLTPMNIYLRNDidviSIKVIKYLIKkgvniETNNNGSESVLESFLD--NNKILSKKE 236
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
809-887 3.00e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  809 EEAQGKLTELEQRIKEAIEK----NAQLQSLElAHADQLTKEkIEELNKTREEQIQKKQKILEELQKVERELQLKTQQ-- 882
Cdd:COG4372   76 EQLEEELEELNEQLQAAQAElaqaQEELESLQ-EEAEELQEE-LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEElk 153

                 ....*
gi 38683807  883 QLKKQ 887
Cdd:COG4372  154 ELEEQ 158
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1730-1793 3.39e-06

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


Pssm-ID: 411826 [Multi-domain]  Cd Length: 67  Bit Score: 46.48  E-value: 3.39e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683807 1730 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22398    4 VPVPRFAVGVVIGKGGEMIKKIQNETGARVQFKPDDGNSPDRICVITGPPDQVQHAARMIQELI 67
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
1732-1789 3.65e-06

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


Pssm-ID: 411823 [Multi-domain]  Cd Length: 68  Bit Score: 46.75  E-value: 3.65e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807 1732 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLI 1789
Cdd:cd22395    6 VPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYTQNFQICSIEGTQQQIDKALKLI 63
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
436-652 4.92e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  436 TALMEACMDGHVE-VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIErgASLEEVND-------EGYTPLMEA 507
Cdd:cd22192   19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  508 AREGHEEMVALLLGQGANInaqteetqetaLTLACCGGFlevadFLIKAGADIELGcSTPLMEAAQEGHLELVKYLLAAG 587
Cdd:cd22192   97 VVNQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNLIYYG-EHPLSFAACVGNEEIVRLLIEHG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  588 ANVHATTATGDTAL---------TYACEnghtdVADVLL-----QAGADLEHESEG-GRTPLMKAARAGHVCTVQFLISK 652
Cdd:cd22192  160 ADIRAQDSLGNTVLhilvlqpnkTFACQ-----MYDLILsydkeDDLQPLDLVPNNqGLTPFKLAAKEGNIVMFQHLVQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1131-1313 4.94e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 4.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1131 VVEILLDNGadiEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEIN 1210
Cdd:PLN03192  509 VGDLLGDNG---GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1211 SRTGSklGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNrntALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLM 1290
Cdd:PLN03192  586 IRDAN--GNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
                         170       180
                  ....*....|....*....|...
gi 38683807  1291 EAASGGYAEVGRVLLDKGADVNA 1313
Cdd:PLN03192  661 VAMAEDHVDMVRLLIMNGADVDK 683
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
1732-1793 4.96e-06

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


Pssm-ID: 411806 [Multi-domain]  Cd Length: 72  Bit Score: 46.49  E-value: 4.96e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807 1732 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQK-DKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd02396    8 VPASQCGSLIGKGGSKIKEIRESTGASVQVASEMlPNSTERAVTISGSPEAITKCVEQICCVM 70
KH-I_PCBP_rpt1 cd22438
first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
1737-1789 5.82e-06

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


Pssm-ID: 411866 [Multi-domain]  Cd Length: 67  Bit Score: 46.10  E-value: 5.82e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 38683807 1737 ISRVIGRGGCNINAIREFTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLI 1789
Cdd:cd22438   10 VGSIIGKKGETIKKFREESGARINI--SDGSCPERIVTVTGTTDAVFKAFELI 60
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
499-531 5.98e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.97  E-value: 5.98e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 38683807    499 EGYTPLMEAA-REGHEEMVALLLGQGANINAQTE 531
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
1732-1789 6.13e-06

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


Pssm-ID: 411865 [Multi-domain]  Cd Length: 69  Bit Score: 46.06  E-value: 6.13e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683807 1732 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDK---TGDRIITIRGGTESTRQATQLI 1789
Cdd:cd22437    5 VPNSSCGLIIGKGGSTIKELREDSNANIKISPKDQLlpgSSERIVTITGSFDQVVKAVALI 65
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2024-2444 6.23e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 6.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2024 PTNATYPMPTAkehypvsspsspsppaqpggvsrNSPLdcgsASPNKVASSSEQEAGSPPVVET----TNTRPPNSSSSS 2099
Cdd:PHA03307   22 PRPPATPGDAA-----------------------DDLL----SGSQGQLVSDSAELAAVTVVAGaaacDRFEPPTGPPPG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2100 GSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAV---PSTAPVTYPMPQTPmGCPQPTPKMETP 2176
Cdd:PHA03307   75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPAsppPSPAPDLSEMLRPV-GSPGPPPAASPP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2177 AIRPPPHGTTAPHKNSASvqnSSVAVLSVNHIKRPhsvPSSVQLPSTLSTQS-ACQNSVHPANKPIAPNFSAPLPFGPFS 2255
Cdd:PHA03307  154 AAGASPAAVASDAASSRQ---AALPLSSPEETARA---PSSPPAEPPPSTPPaAASPRPPRRSSPISASASSPAPAPGRS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2256 TLFENSPTSahafwggsvvSSQSTPESMLSGKSSYLPNSDPLHQSDTSK----------APGFRPPLQRPAPSPSGivnm 2325
Cdd:PHA03307  228 AADDAGASS----------SDSSSSESSGCGWGPENECPLPRPAPITLPtriweasgwnGPSSRPGPASSSSSPRE---- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2326 dsPYGSVTPSSTHLGNFASNISggqmygpgaplggapAAANFNRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSPA-P 2404
Cdd:PHA03307  294 --RSPSPSPSSPGSGPAPSSPR---------------ASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSrP 356
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 38683807  2405 SSVPLGSEKPSNVSQDRKVPVPIGTERSARIRQTGTSAPS 2444
Cdd:PHA03307  357 PPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAG 396
Ank_4 pfam13637
Ankyrin repeats (many copies);
1152-1203 7.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 7.35e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683807   1152 TPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILL 1203
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1728-1794 7.57e-06

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


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 45.64  E-value: 7.57e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807 1728 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDriITIRGGTESTRQATQLINALIK 1794
Cdd:cd02394    4 TTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDE--IRIEGSPEGVKKAKAEILELVD 68
KH-I_FUBP3_rpt4 cd22489
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1731-1790 8.26e-06

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


Pssm-ID: 411917 [Multi-domain]  Cd Length: 69  Bit Score: 45.69  E-value: 8.26e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807 1731 SVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGD---RIITIRGGTESTRQATQLIN 1790
Cdd:cd22489    5 TIPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNTDpnvRIFTIRGVPQQIEHARQLID 67
Ank_4 pfam13637
Ankyrin repeats (many copies);
1118-1170 8.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 8.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 38683807   1118 TPLILAATAGHVGVVEILLDNGADIEAQSERtKDTPLSLACSGGRQEVVELLL 1170
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
774-887 9.00e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.17  E-value: 9.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    774 IRNKAASKQKSSSHLPANSQDVQGYITNQSPE--SIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTK-EKIEE 850
Cdd:TIGR04523  326 IQNQISQNNKIISQLNEQISQLKKELTNSESEnsEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiQNQEK 405
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 38683807    851 LNKTREEQIQKKQKILEELQK-VERELQLKTQQQ-----LKKQ 887
Cdd:TIGR04523  406 LNQQKDEQIKKLQQEKELLEKeIERLKETIIKNNseikdLTNQ 448
Ank_5 pfam13857
Ankyrin repeats (many copies);
386-438 9.06e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 9.06e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 38683807    386 LLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTAL 438
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1732-1793 9.12e-06

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


Pssm-ID: 411888 [Multi-domain]  Cd Length: 73  Bit Score: 45.69  E-value: 9.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807 1732 VPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDK-----TGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22460    6 VASSQAGSLIGKGGAIIKQIREESGASVRILPEEELppcasPDDRVVQISGEAQAVKKALELVSSRL 72
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
1218-1374 9.13e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 51.03  E-value: 9.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1218 GISPLMLAAMN---GHTAAVKLLLDMGSD-------INAQIETNR---NTALTLACFQGRTEVVSLLLDRKANVEHRA-- 1282
Cdd:cd21882   26 GKTCLHKAALNlndGVNEAIMLLLEAAPDsgnpkelVNAPCTDEFyqgQTALHIAIENRNLNLVRLLVENGADVSARAtg 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1283 ----KTGLT-------PLMEAASGGYAEVGRVLLDKGADvnaPPVPSSRDT-------ALTIAADK--GHYKFC----EL 1338
Cdd:cd21882  106 rffrKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQ---PAALEAQDSlgntvlhALVLQADNtpENSAFVcqmyNL 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 38683807 1339 LIGRGAHID-------VRNKKGNTPLWLAANGGHLDVVQLLVQ 1374
Cdd:cd21882  183 LLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
2108-2317 9.33e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 51.31  E-value: 9.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2108 QQQPPgsVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPVTYPMPQTPMGCPQP-TPKMETPAIRPP----P 2182
Cdd:pfam03154  168 QTQPP--VLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPhTLIQQTPTLHPQrlpsP 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2183 HGTTAPhknsasvqnssvavlsvnhikRPHSVPssvqlPSTLSTQSACQNSVHPANKPIA-------PNFSAPLPFGPFS 2255
Cdd:pfam03154  246 HPPLQP---------------------MTQPPP-----PSQVSPQPLPQPSLHGQMPPMPhslqtgpSHMQHPVPPQPFP 299
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807   2256 TLFENS----PTSAHAFWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSkAPGFRPPLQRPAP 2317
Cdd:pfam03154  300 LTPQSSqsqvPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLS-MPHIKPPPTTPIP 364
Ank_5 pfam13857
Ankyrin repeats (many copies);
320-371 9.60e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 9.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 38683807    320 LLAHK-ADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPL 371
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1289-1372 9.63e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 9.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1289 LMEAASGGYAEVGRVLLDKGADvnappvPSSRD----TALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGG 1364
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGAD------PNCRDydgrTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159

                  ....*...
gi 38683807  1365 HLDVVQLL 1372
Cdd:PTZ00322  160 FREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
1285-1340 9.97e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 9.97e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807   1285 GLTPLMEAASGGYAEVGRVLLDKGADVNAppVPSSRDTALTIAADKGHYKFCELLI 1340
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
568-719 1.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   568 LMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQ 647
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807   648 FLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDY 719
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
303-341 1.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.13e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 38683807    303 TPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYA 341
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
371-475 1.19e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   371 LMEAGSAGHVEVARLLLENGAgiNTHSNEFKESA-LTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEV 449
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGA--DPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 38683807   450 ARLLL-----DSGAQVNMPADSF--------ESPLTLAA 475
Cdd:PTZ00322  164 VQLLSrhsqcHFELGANAKPDSFtgkppsleDSPISSHH 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1352-1381 1.21e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 1.21e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 38683807    1352 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1381
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
499-528 1.26e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 1.26e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 38683807     499 EGYTPLMEAAREGHEEMVALLLGQGANINA 528
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
423-521 1.32e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   423 AGADQEHKTDE------MHTALMEAC---MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASL 493
Cdd:PTZ00322   62 ATPDHNLTTEEvidpvvAHMLTVELCqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
                          90       100
                  ....*....|....*....|....*...
gi 38683807   494 EEVNDEGYTPLMEAAREGHEEMVALLLG 521
Cdd:PTZ00322  142 TLLDKDGKTPLELAEENGFREVVQLLSR 169
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
1734-1795 1.34e-05

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


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 44.97  E-value: 1.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807 1734 STVISRVIGRGGCNINAIREFTGAHIDIDKQKDktgDRIITIRGGTESTRQATQLINALIKD 1795
Cdd:cd22430    8 SSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQ---EAEVKIFGSDEAQQKAKELIDELVGR 66
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1729-1798 1.41e-05

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


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 44.89  E-value: 1.41e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIdKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDK 1798
Cdd:cd22417    4 TVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQF-PDKGDENDDEITITGYEKNAEAAKDAILKIVQELES 72
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
780-887 1.73e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    780 SKQKSSSHLPANSQDVQGYITN--QSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSLElAHADQLTKEKIEELNKTREE 857
Cdd:TIGR04523  236 KKQQEINEKTTEISNTQTQLNQlkDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK-SEISDLNNQKEQDWNKELKS 314
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 38683807    858 QIQKKQKILEELQKverEL--------QLKTQ-QQLKKQ 887
Cdd:TIGR04523  315 ELKNQEKKLEEIQN---QIsqnnkiisQLNEQiSQLKKE 350
PRK11633 PRK11633
cell division protein DedD; Provisional
2110-2219 1.73e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 48.46  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2110 QPPGSVSQEPR------PPLQQSQVPPPEVRMTVPPlatssAPVAVPSTAPVTYPMPQT---PMGCPQPTPKmetPAIRP 2180
Cdd:PRK11633   66 QPPEGAAEAVRagdaaaPSLDPATVAPPNTPVEPEP-----APVEPPKPKPVEKPKPKPkpqQKVEAPPAPK---PEPKP 137
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 38683807  2181 PPHGTTAPH-----------KNSASVqNSSVAVLSVNHIkRPHSVPSS-VQ 2219
Cdd:PRK11633  138 VVEEKAAPTgkayvvqlgalKNADKV-NEIVAKLRLSGY-RVYTVPSTpVQ 186
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1122-1226 1.97e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1122 LAATAGHVGVvEILLDNGADIEAQsERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKI 1201
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 38683807  1202 LL---------NAGAEINSRTG--SKLGISPLMLAA 1226
Cdd:PTZ00322  167 LSrhsqchfelGANAKPDSFTGkpPSLEDSPISSHH 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1338-1405 2.10e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 2.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807  1338 LLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYL 1405
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1226-1315 2.37e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1226 AMNGHTAAVKLLLDMGSDINAQiETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1305
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
                          90
                  ....*....|....*
gi 38683807  1306 -----DKGADVNAPP 1315
Cdd:PTZ00322  169 rhsqcHFELGANAKP 183
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
303-330 2.43e-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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 2.43e-05
                           10        20
                   ....*....|....*....|....*....
gi 38683807    303 TPLMAAA-NGGHVKIVKLLLAHKADVNAQ 330
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
804-886 2.44e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.83  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   804 PESIVEEAQGKLTELEQRIKEAIEKNAQLQ-SLE--LAHADQLtkekIEELNKTREEQIQKKQKILEELQKVERELQLKT 880
Cdd:PRK00409  500 PENIIEEAKKLIGEDKEKLNELIASLEELErELEqkAEEAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA 575

                  ....*.
gi 38683807   881 QQQLKK 886
Cdd:PRK00409  576 QQAIKE 581
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
236-489 3.13e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 49.69  E-value: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    236 RSLAEACSEGDVNAVRKLLIEGRSVNEHTEE--GESLLCLACSAG-YYELAQVLLamhaNVEDRGIKGDiTPLMAAANGg 312
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLL----NLSCRGAVGD-TLLHAISLE- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    313 HVKIVKLLLAHKADvnAQSSTGNTALTYACAGG--YVDvvkvllesgasiedhnengHTPLMEAGSAGHVEVARLLLENG 390
Cdd:TIGR00870   93 YVDAVEAILLHLLA--AFRKSGPLELANDQYTSefTPG-------------------ITALHLAAHRQNYEIVKLLLERG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    391 AGINT--HSNEFKESALT---------LACYK--GHLEMVRFLLEAGADQEhKTDEM-----HTALMEA----------- 441
Cdd:TIGR00870  152 ASVPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelsc 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 38683807    442 -CMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 489
Cdd:TIGR00870  231 qMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
PHA03247 PHA03247
large tegument protein UL36; Provisional
1886-2339 3.15e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1886 PPPQFAHALLAAQTFQQIRPPRL------PMTHFGGTFP--PAQSTWGPFPVRPLSPARAT---NSPKPHMVPRHSNQNS 1954
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRPaprpsePAVTSRARRPdaPPQSARPRAPVDDRGDPRGPappSPLPPDTHAPDPPPPS 2630
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1955 SGSQVNSAGSLTSSPTTttsssastvPGTSTNGSPSSPSVRRQLFVTVVKTSNATTTTVTTTASNNNTAP----TNATYP 2030
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVP---------PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgslTSLADP 2701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2031 MPTAKEHYPVSSPSSPSPPAQPGgvsrnsPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSSAHsnqqq 2110
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPG------PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA----- 2770
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2111 PPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPV-TYPMPQTPMGcPQPTPKMETPAIRPPPHGTTAPh 2189
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAaALPPAASPAG-PLPPPTSAQPTAPPPPPGPPPP- 2848
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2190 knSASVQNSSVAVLSVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIA--PNFSAPLPFGPFSTLFENSPTSAHA 2267
Cdd:PHA03247 2849 --SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAlpPDQPERPPQPQAPPPPQPQPQPPPP 2926
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2268 FWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDT---------------SKAPGFRPPLQRPAPSPSGIVNMDSPYGSV 2332
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgalvpgrvavprFRVPQPAPSREAPASSTPPLTGHSLSRVSS 3006

                  ....*..
gi 38683807  2333 TPSSTHL 2339
Cdd:PHA03247 3007 WASSLAL 3013
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
417-486 3.22e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 3.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   417 VRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALL 486
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
805-881 3.44e-05

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 44.45  E-value: 3.44e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807    805 ESIVEEAQgklTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEElnkTREEQIQKKQKILEELQKVERELQLKTQ 881
Cdd:TIGR02926   12 EELIEEAE---EERKQRIAEAREEARELLEEAEEEASKLGEEIIKE---AEEEIEKEAEKIREEGEKEIEAMKSKAK 82
Ank_5 pfam13857
Ankyrin repeats (many copies);
559-604 3.65e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 3.65e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 38683807    559 DIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYA 604
Cdd:pfam13857   11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
KH-I_NOVA_rpt1 cd22435
first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
1729-1789 4.00e-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: 43.68  E-value: 4.00e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683807 1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD---KTGDRIITIRGGTESTRQATQLI 1789
Cdd:cd22435    5 KLLVPNYAAGSIIGKGGQTIAQLQKETGARIKLSKNNDfypGTTERVCLIQGEVEAVNAVLDFI 68
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1218-1246 5.07e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 5.07e-05
                           10        20
                   ....*....|....*....|....*....
gi 38683807   1218 GISPLMLAAMNGHTAAVKLLLDMGSDINA 1246
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
341-494 5.43e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 5.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    341 ACAGGYVDVVKVLLESGAS--IEDHNENGHTPLMEAGSAG-HVEVARLLLENGAGINThsnefKESALTLAC--YKGHLE 415
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV-----GDTLLHAISleYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    416 MVRFLLEAGADQ--------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ESP 470
Cdd:TIGR00870   99 AILLHLLAAFRKsgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgESP 178
                          170       180
                   ....*....|....*....|....
gi 38683807    471 LTLAACGGHVELAALLIERGASLE 494
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADIL 202
Ank_4 pfam13637
Ankyrin repeats (many copies);
1252-1305 5.61e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 5.61e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 38683807   1252 RNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLL 1305
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1115-1145 5.66e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.28  E-value: 5.66e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 38683807   1115 KGFTPLILAAT-AGHVGVVEILLDNGADIEAQ 1145
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
326-520 5.84e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 48.34  E-value: 5.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  326 DVNAQSSTGNTALTYAC---AGGYVDVVKVLLESG-----------ASIEDHNENGHTPLMEAGSAGHVEVARLLLENGA 391
Cdd:cd21882   18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAApdsgnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  392 GINTHSN------------EFKESALTLACYKGHLEMVRFLLEAGAD--QEHKTDEMHTALMEACmdghVEVARLLLDSG 457
Cdd:cd21882   98 DVSARATgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQpaALEAQDSLGNTVLHAL----VLQADNTPENS 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683807  458 AQVnmpADSFESPLTLAACGGHVElaalliergaSLEEV-NDEGYTPLMEAAREGHEEMVALLL 520
Cdd:cd21882  174 AFV---CQMYNLLLSYGAHLDPTQ----------QLEEIpNHQGLTPLKLAAVEGKIVMFQHIL 224
PHA02859 PHA02859
ankyrin repeat protein; Provisional
314-428 5.89e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.74  E-value: 5.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   314 VKIVKLLLAHKADVNAQSSTGNTAL--TYACAGGYV--DVVKVLLESGASIEDHNENGHTPL---MEAGSAgHVEVARLL 386
Cdd:PHA02859   66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV-RINVIKLL 144
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 38683807   387 LENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQE 428
Cdd:PHA02859  145 IDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDIN 186
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
1729-1793 6.17e-05

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


Pssm-ID: 411882 [Multi-domain]  Cd Length: 71  Bit Score: 43.07  E-value: 6.17e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807 1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22454    7 EVVIPNADVGKVIGKGGETIKRIEALTDTVITFERVNGGSPNREVQITGSPDNVAAAKRLIEDTI 71
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
630-660 6.49e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 6.49e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 38683807    630 GRTPLMKAA-RAGHVCTVQFLISKGANVNRTT 660
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
566-594 6.49e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 6.49e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683807    566 TPLMEAA-QEGHLELVKYLLAAGANVHATT 594
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
565-651 6.68e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 6.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   565 STPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVC 644
Cdd:PTZ00322   83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                  ....*..
gi 38683807   645 TVQFLIS 651
Cdd:PTZ00322  163 VVQLLSR 169
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1727-1795 7.34e-05

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


Pssm-ID: 411837 [Multi-domain]  Cd Length: 70  Bit Score: 42.95  E-value: 7.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIR-EFTGAHIDIDKQKDKtgdriITIRGGTESTRQATQLINALIKD 1795
Cdd:cd22409    3 VAEVSAPSWLHRFIIGKKGANIKKITqDLPKVHIEFTEGEDK-----IELEGPPEEVEVVREQLEAIVKE 67
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1741-1789 7.40e-05

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


Pssm-ID: 411841 [Multi-domain]  Cd Length: 66  Bit Score: 42.63  E-value: 7.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 38683807 1741 IGRGGCNINAIREFTGAHIDIDKQKDKTGDrIITIRGGTESTRQATQLI 1789
Cdd:cd22413   18 IGRGGANIRKIRDNTGARIIFPTARDEDQE-LITIIGTKEAVEKAKEEL 65
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
794-886 7.99e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.88  E-value: 7.99e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807     794 DVQgYITNQSPEsiVEEAQGKL-TELEQRIKEAIEKNAQLQSLElahaDQLTKEK---IEELNKTREEQIQKKQKILEEL 869
Cdd:smart00935    5 DVQ-KILQESPA--GKAAQKQLeKEFKKRQAELEKLEKELQKLK----EKLQKDAatlSEAAREKKEKELQKKVQEFQRK 77
                            90
                    ....*....|....*...
gi 38683807     870 QKV-ERELQLKTQQQLKK 886
Cdd:smart00935   78 QQKlQQDLQKRQQEELQK 95
PTZ00121 PTZ00121
MAEBL; Provisional
809-892 8.08e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 8.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   809 EEAQGKLTEL--EQRIKEAIEKNAQLQSLELAHADQLTKEkiEELNKTREEQIQKK----QKILEELQKVERElQLKTQQ 882
Cdd:PTZ00121 1616 EEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKaeedKKKAEEAKKAEED-EKKAAE 1692
                          90
                  ....*....|
gi 38683807   883 QLKKQYLEVK 892
Cdd:PTZ00121 1693 ALKKEAEEAK 1702
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1218-1246 8.10e-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: 41.80  E-value: 8.10e-05
                            10        20
                    ....*....|....*....|....*....
gi 38683807    1218 GISPLMLAAMNGHTAAVKLLLDMGSDINA 1246
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
808-893 8.42e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 8.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  808 VEEAQGKL----TELEQRIKEAIEKNAQLQSL--ELAHADQLTKEKIEELNKTREEQIQKKQKIlEELQKvERELQLKTQ 881
Cdd:COG4372   54 LEQAREELeqleEELEQARSELEQLEEELEELneQLQAAQAELAQAQEELESLQEEAEELQEEL-EELQK-ERQDLEQQR 131
                         90
                 ....*....|..
gi 38683807  882 QQLKKQYLEVKA 893
Cdd:COG4372  132 KQLEAQIAELQS 143
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
499-528 1.17e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 1.17e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683807    499 EGYTPLMEAAREGHEEMVALLLGQGANINA 528
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_FUBP2_rpt1 cd22479
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1727-1793 1.22e-04

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


Pssm-ID: 411907 [Multi-domain]  Cd Length: 71  Bit Score: 42.24  E-value: 1.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22479    2 TEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGSPEAVQKAKMMLDDIV 68
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
366-394 1.33e-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: 1.33e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683807    366 NGHTPLMEA-GSAGHVEVARLLLENGAGIN 394
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVN 30
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
2142-2340 1.34e-04

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


Pssm-ID: 430088 [Multi-domain]  Cd Length: 684  Bit Score: 47.52  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2142 TSSAPVAVPSTaPVTYPMPQTPMGCPQPTPKMETPAIRPPPHGTTAPHKNSASVQNSsvavLSVNHIKRPHSVPSSvqlP 2221
Cdd:pfam08580  491 PSKIPRASPNH-SGFLSTPSNTATSETPTPALRPPSRPQPPPPGNRPRWNASTNTND----LDVGHNFKPLTLTTP---S 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2222 STLSTQSACQNSVHPANKPIAPNFSAPLPFGPFSTLFENSPTSAHAfwggSVVSSQSTPESMLsgkssylpNSDPLHQSD 2301
Cdd:pfam08580  563 PTPSRSSRSSSTLPPVSPLSRDKSRSPAPTCRSVSRASRRRASRKP----TRIGSPNSRTSLL--------DEPPYPKLT 630
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 38683807   2302 TSKAPGfRPPLQRP---APSPSGIVNMDSPYGSVTPSSTHLG 2340
Cdd:pfam08580  631 LSKGLP-RTPRNRQsyaGTSPSRSVSVSSGLGPQTRPGTSLG 671
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1115-1144 1.45e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 1.45e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 38683807    1115 KGFTPLILAATAGHVGVVEILLDNGADIEA 1144
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
774-892 1.46e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    774 IRNKAASKQKSSSHLPANSQDVQGYI-----TNQSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSL--ELAHADQLTKE 846
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQINDLESKIqnqekLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEikDLTNQDSVKEL 454
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 38683807    847 KIEELNKTREEQIQKKQKILEELQKVERELQlKTQQQLKKQYLEVK 892
Cdd:TIGR04523  455 IIKNLDNTRESLETQLKVLSRSINKIKQNLE-QKQKELKSKEKELK 499
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
566-592 1.50e-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: 1.50e-04
                            10        20
                    ....*....|....*....|....*..
gi 38683807     566 TPLMEAAQEGHLELVKYLLAAGANVHA 592
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
1131-1261 1.59e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1131 VVEILLDNGADIEAQsERTKDTPLSLACSGGRQ-----EVVELLLARGANKEHRNVSDYTPLSLAASGGYVN---IIKIL 1202
Cdd:PHA02798   53 IVKLFINLGANVNGL-DNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINnleILLFM 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807  1203 LNAGAEINSRtgSKLGISPLMLAAMNGHTA---AVKLLLDMGSDINaqIETNRNTALTLACF 1261
Cdd:PHA02798  132 IENGADTTLL--DKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDIN--THNNKEKYDTLHCY 189
KH-I_MER1_like cd22458
type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic ...
1728-1789 1.67e-04

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


Pssm-ID: 411886 [Multi-domain]  Cd Length: 65  Bit Score: 41.67  E-value: 1.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807 1728 KKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTgDRIITIRGGTESTRQATQLI 1789
Cdd:cd22458    3 WEIKLPQALCGRLIGAKGKNIKALSEKSGASIRLIPISNSS-QQTIHLSGTDKQIALAISSI 63
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
630-657 1.69e-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: 1.69e-04
                            10        20
                    ....*....|....*....|....*...
gi 38683807     630 GRTPLMKAARAGHVCTVQFLISKGANVN 657
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
348-522 1.86e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.06  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  348 DVVKVLLEsgASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGIN----------THSNE---FKESALTLACYKGHL 414
Cdd:cd22194  124 GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEgfyFGETPLALAACTNQP 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  415 EMVRFLLEAGADQEHKTDEMHTALMEACmdghVEVARlllDSGAQVNMPADSFESPLTlaACGGHvelaalliergaSLE 494
Cdd:cd22194  202 EIVQLLMEKESTDITSQDSRGNTVLHAL----VTVAE---DSKTQNDFVKRMYDMILL--KSENK------------NLE 260
                        170       180
                 ....*....|....*....|....*....
gi 38683807  495 EV-NDEGYTPLMEAAREGHEEMVALLLGQ 522
Cdd:cd22194  261 TIrNNEGLTPLQLAAKMGKAEILKYILSR 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
486-541 1.98e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 1.98e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807    486 LIERG-ASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETqETALTLA 541
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
597-624 2.00e-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: 2.00e-04
                            10        20
                    ....*....|....*....|....*...
gi 38683807     597 GDTALTYACENGHTDVADVLLQAGADLE 624
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
334-362 2.02e-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: 2.02e-04
                            10        20
                    ....*....|....*....|....*....
gi 38683807     334 GNTALTYACAGGYVDVVKVLLESGASIED 362
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 ...
1730-1793 2.08e-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: 41.65  E-value: 2.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807 1730 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKD--KTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22463    6 FQIPEAVVGLIIGKSGNTIKQISERSGAFVAIVQDRYplEETQKILRISGTEEQLKRAQSLVEGLI 71
KH-I_IGF2BP_rpt4 cd22403
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1730-1785 2.32e-04

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


Pssm-ID: 411831 [Multi-domain]  Cd Length: 66  Bit Score: 41.46  E-value: 2.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807 1730 VSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTGDRIITIRGGTESTRQA 1785
Cdd:cd22403    4 IRVPSSMVGRIIGKGGQNVRELQRLTGAIIKLprDQTPDEGDEVPVEIIGNFYATQSA 61
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1075-1204 2.59e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 46.29  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1075 IDAQ-TESNHD--TALTLACAGGHEELVQTLLERGASIEHRDKKGF--------------TPLILAATAGHVGVVEILLD 1137
Cdd:cd22194  130 INAEyTEEAYEgqTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLME 209
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807 1138 NGADIEAQSERTKDTPL---------SLACSGGRQEVVELLLARGANKE---HRNVSDYTPLSLAASGGYVNIIKILLN 1204
Cdd:cd22194  210 KESTDITSQDSRGNTVLhalvtvaedSKTQNDFVKRMYDMILLKSENKNletIRNNEGLTPLQLAAKMGKAEILKYILS 288
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1218-1247 2.59e-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: 40.35  E-value: 2.59e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 38683807   1218 GISPLMLAA-MNGHTAAVKLLLDMGSDINAQ 1247
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1299-1452 2.70e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1299 EVGRVLLDKGADVNAPPVPSSrdtALTIAAdKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGAD 1378
Cdd:PLN03192  508 NVGDLLGDNGGEHDDPNMASN---LLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1379 VDAADNRKITPLMAAFRKGHVKVVRYLvkevNQFPSDS------ECMRYIATITDKEMLKKChLCMESIVQAKDRQAAEA 1452
Cdd:PLN03192  584 VHIRDANGNTALWNAISAKHHKIFRIL----YHFASISdphaagDLLCTAAKRNDLTAMKEL-LKQGLNVDSEDHQGATA 658
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
234-454 2.71e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    234 DNRSLAEACSEGDVNAVRKLLIEgrsVNEHTEEGESLLcLACSAGYY----ELAQVLLAMH--------ANVEDRG-IKG 300
Cdd:TIGR00870   52 GRSALFVAAIENENLELTELLLN---LSCRGAVGDTLL-HAISLEYVdaveAILLHLLAAFrksgplelANDQYTSeFTP 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    301 DITPLMAAANGGHVKIVKLLLAHKADVNA-------QSSTGNTAL--------TYACAGGYvDVVKVLLESGASIEDHNE 365
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFyhgesplnAAACLGSP-SIVALLSEDPADILTADS 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    366 NGHTplmeagsaghveVARLLLENgaginthsNEFKESALTLACykghlEMVRFLLEAGaDQEHKTDEMH--------TA 437
Cdd:TIGR00870  207 LGNT------------LLHLLVME--------NEFKAEYEELSC-----QMYNFALSLL-DKLRDSKELEvilnhqglTP 260
                          250
                   ....*....|....*..
gi 38683807    438 LMEACMDGHVEVARLLL 454
Cdd:TIGR00870  261 LKLAAKEGRIVLFRLKL 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
303-329 2.85e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 2.85e-04
                            10        20
                    ....*....|....*....|....*..
gi 38683807     303 TPLMAAANGGHVKIVKLLLAHKADVNA 329
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
271-364 2.85e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   271 LCLACSAGYYELAQVLLAMHANVEDRGIKGDiTPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVV 350
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90
                  ....*....|....
gi 38683807   351 KVLleSGASIEDHN 364
Cdd:PTZ00322  165 QLL--SRHSQCHFE 176
Ank_5 pfam13857
Ankyrin repeats (many copies);
1135-1190 3.27e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 3.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807   1135 LLDNG-ADIEAQsERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLA 1190
Cdd:pfam13857    1 LLEHGpIDLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
808-893 3.35e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.53  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  808 VEEAQGKLTELEQRIKEAIE----KNAQLQSLELAHADQltKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQQ 883
Cdd:COG1579   98 IESLKRRISDLEDEILELMErieeLEEELAELEAELAEL--EAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
                         90
                 ....*....|
gi 38683807  884 LKKQYLEVKA 893
Cdd:COG1579  176 LLALYERIRK 185
HAUS4 pfam14735
HAUS augmin-like complex subunit 4; This family includes HAUS augmin-like complex subunit 4. ...
757-892 3.41e-04

HAUS augmin-like complex subunit 4; This family includes HAUS augmin-like complex subunit 4. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.


Pssm-ID: 464287  Cd Length: 235  Bit Score: 44.56  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    757 PPQEPDKP------PANVATTLPIRNKAASKQKS-----SSHLPANSQDVQGYITNQSPESIVEEAQGKLTELEQRIKEA 825
Cdd:pfam14735    5 PTVGGDQPrllgltPADLLQLMPDKQDVQQMQQRlprelEARLKKKCFALLSYYQPESEGDSEGLKAAKLSRLPELLESE 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    826 IEknaQLQSLELAHADQLTKekieeLNKTREEQIQKKQKILEELQKVERELQLKTQQQL---KKQYLEVK 892
Cdd:pfam14735   85 KR---RLESEKEKLRENLVL-----LQRQFAEYYQVLLQCLQLLQRLVLDHRLKHQSDLdrkKKEYLEAK 146
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
1726-1802 3.42e-04

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 46.15  E-value: 3.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807 1726 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDkqkDktgDRIITIrGGT--ESTRQATQLINALIKDPdkEIDE 1802
Cdd:COG1185  549 RIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIE---D---DGTVKI-AATdgEAAEKAIERIEGITAEP--EVGE 618
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1073-1144 3.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 3.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807  1073 IDIDAQTEsNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEA 1144
Cdd:PHA03100  183 VPINIKDV-YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
570-669 3.80e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   570 EAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFL 649
Cdd:PHA02876  151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI 230
                          90       100
                  ....*....|....*....|
gi 38683807   650 ISKGANVNRttanNDHTVLS 669
Cdd:PHA02876  231 IDNRSNINK----NDLSLLK 246
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
822-887 4.02e-04

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 40.71  E-value: 4.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807  822 IKEaiEKNAQLQSLElahaDQLTKEKIEElNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQ 887
Cdd:cd22249    7 IRE--EYEAQLKKLE----EERRKEREEE-EKASEELIRKLQEEEERQRKREREEQLKQDEELAKQ 65
Ank_5 pfam13857
Ankyrin repeats (many copies);
1202-1259 4.10e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 4.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807   1202 LLNAGAeINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQiETNRNTALTLA 1259
Cdd:pfam13857    1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK-DEEGLTALDLA 56
PRK12704 PRK12704
phosphodiesterase; Provisional
809-884 4.46e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   809 EEAQGKLTELEQRIKEaieKNAQLQSLE---LAHADQLtKEKIEELNK------TREEQIQKKQKILEELQKVERELQLK 879
Cdd:PRK12704   64 EEIHKLRNEFEKELRE---RRNELQKLEkrlLQKEENL-DRKLELLEKreeeleKKEKELEQKQQELEKKEEELEELIEE 139

                  ....*
gi 38683807   880 TQQQL 884
Cdd:PRK12704  140 QLQEL 144
Ank_5 pfam13857
Ankyrin repeats (many copies);
1346-1390 4.52e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 4.52e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 38683807   1346 IDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPL 1390
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
1726-1802 4.56e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.81  E-value: 4.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807  1726 RSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKqkdktgDRIITIRGGT-ESTRQATQLINALIKDPdkEIDE 1802
Cdd:PRK11824  554 RIETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIED------DGTVKIAATDgEAAEAAKERIEGITAEP--EVGE 623
PHA02946 PHA02946
ankyin-like protein; Provisional
1093-1289 4.58e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1093 GGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKdTPLSLaCSGGRQEVVE---LL 1169
Cdd:PHA02946   49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHK-TPLYY-LSGTDDEVIErinLL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1170 LARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEinSRTGSKLGISPL--MLAAMNGHTAAVKLLLDMGSDiNAQ 1247
Cdd:PHA02946  127 VQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFE--ARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGIS-PSK 203
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 38683807  1248 IETNRNTALTLACFQ--GRTEVVSLLLDrKANVEHRAKTGLTPL 1289
Cdd:PHA02946  204 PDHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPL 246
PHA02884 PHA02884
ankyrin repeat protein; Provisional
346-443 5.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.59  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   346 YVDVVKVLLESGASIE---DHNENGHT-PLMEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLL 421
Cdd:PHA02884   45 YTDIIDAILKLGADPEapfPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
                          90       100
                  ....*....|....*....|..
gi 38683807   422 EAGADQEHKTDEMHTALMEACM 443
Cdd:PHA02884  125 SYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
630-657 5.24e-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: 5.24e-04
                           10        20
                   ....*....|....*....|....*...
gi 38683807    630 GRTPLMKAARAGHVCTVQFLISKGANVN 657
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
536-584 5.60e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 5.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683807    536 TALTLACCGGFLEVADFLIKAGADI---ELGCSTPLMEAAQEGHLELVKYLL 584
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADInavDGNGETALHFAASNGNVEVLKLLL 54
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
805-1008 5.89e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  805 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTR-----EEQIQKKQKILEELQKVERELQLK 879
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEA 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  880 TQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLLTPVGVGEQLSEGDYARLQQVDPVLLKDEPQQtAAQMGFAPIQPLAMP 959
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLE 508
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 38683807  960 QALPLAAGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQ 1008
Cdd:COG1196  509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
801-893 6.04e-04

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 43.60  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    801 NQSPESIVEEAQGKLTELEQRIKE---AIEKNAQLQSlelahadQLTKE--KIEELNKTREEQIQKKQKILEELQKVERE 875
Cdd:pfam14988   28 VQECEEIERRRQELASRYTQQTAElqtQLLQKEKEQA-------SLKKElqALRPFAKLKESQEREIQDLEEEKEKVRAE 100
                           90
                   ....*....|....*...
gi 38683807    876 LQLKTQQqLKKQYLEVKA 893
Cdd:pfam14988  101 TAEKDRE-AHLQFLKEKA 117
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
808-893 6.07e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 6.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    808 VEEAQGKLTELEQRIKEaIEKNAQLQSLELAHADQltkeKIEELNKTREEQIQKKQKILEELQKVEREL-QLKTQQQLKK 886
Cdd:TIGR02168  283 IEELQKELYALANEISR-LEQQKQILRERLANLER----QLEELEAQLEELESKLDELAEELAELEEKLeELKEELESLE 357

                   ....*..
gi 38683807    887 QYLEVKA 893
Cdd:TIGR02168  358 AELEELE 364
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
808-893 6.12e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   808 VEEAQGKLTELEQRIKEAIEKNAQLQSLELahadqlTKEKIEELNKTREEQIQKKQKILEELQKVERElqLKTQQQLKKQ 887
Cdd:PRK03918  223 LEKLEKEVKELEELKEEIEELEKELESLEG------SKRKLEEKIRELEERIEELKKEIEELEEKVKE--LKELKEKAEE 294

                  ....*.
gi 38683807   888 YLEVKA 893
Cdd:PRK03918  295 YIKLSE 300
PHA03100 PHA03100
ankyrin repeat protein; Provisional
611-723 6.24e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 6.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   611 DVADVLLQAGADLEHESEGGRTPLMKAARAGHVCT-----VQFLISKGANVNRTTANNDHTVLSLACAG-GHLAVVELLL 684
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLL 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 38683807   685 AHGADPTHRLKDGSTMLIEAAKGGH--TSVVCYLLDYPNNL 723
Cdd:PHA03100  129 DNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDI 169
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
815-883 6.35e-04

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 40.73  E-value: 6.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807  815 LTELEQRIKEAIEKNAQLQslelahadqLTKEKIEELNKTREEQIQKKQKILEELQKVERelQLKTQQQ 883
Cdd:COG3074    6 LEELEAKVQQAVDTIELLQ---------MEVEELKEKNEELEQENEELQSENEELQSENE--QLKTENA 63
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
775-890 6.58e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 44.42  E-value: 6.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    775 RNKAASKQKSSShlpANSQDVQGYItnQSPESIVEEAQGKLTELEQRI----KEAIEKNAQLQSLElahadqltkEKIEE 850
Cdd:pfam15905  165 RNKLEAKMKEVM---AKQEGMEGKL--QVTQKNLEHSKGKVAQLEEKLvsteKEKIEEKSETEKLL---------EYITE 230
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 38683807    851 LNKTREEQIQKKQKI--LEE-LQKVERELQ-LKTQQQLKKQYLE 890
Cdd:pfam15905  231 LSCVSEQVEKYKLDIaqLEElLKEKNDEIEsLKQSLEEKEQELS 274
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1352-1381 6.90e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 6.90e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683807   1352 KGNTPLWLAANGGHLDVVQLLVQAGADVDA 1381
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
515-725 7.66e-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: 7.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  515 MVALLlgqgaNINAQTEETQETALTLACCGGFLEVadfLIKAGADIE-LGCSTPLMEAAQEGHLELVKYLLAAGANVHAt 593
Cdd:cd22194   99 MKALL-----NINENTKEIVRILLAFAEENGILDR---FINAEYTEEaYEGQTALNIAIERRQGDIVKLLIAKGADVNA- 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  594 TATGdtaltyacenghtdvadVLLQAgadlEHESEG---GRTPLMKAAraghvCT-----VQFLISKGANVNRTTANNDH 665
Cdd:cd22194  170 HAKG-----------------VFFNP----KYKHEGfyfGETPLALAA-----CTnqpeiVQLLMEKESTDITSQDSRGN 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807  666 TVL-SLACAG----GHLAVV-----ELLLAHGAD--PTHRLKDGSTMLIEAAKGGHTSVVCYLL-----DYPNNLLS 725
Cdd:cd22194  224 TVLhALVTVAedskTQNDFVkrmydMILLKSENKnlETIRNNEGLTPLQLAAKMGKAEILKYILsreikEKPNRSLS 300
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
435-462 8.46e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 8.46e-04
                            10        20
                    ....*....|....*....|....*...
gi 38683807     435 HTALMEACMDGHVEVARLLLDSGAQVNM 462
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
366-394 9.07e-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: 9.07e-04
                            10        20
                    ....*....|....*....|....*....
gi 38683807     366 NGHTPLMEAGSAGHVEVARLLLENGAGIN 394
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
808-893 9.86e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 9.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  808 VEEAQGKLTELEQRIkEAIEKNAQLQSLELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKV-----ERELQLKTQQ 882
Cdd:COG1196  283 LEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeaeeELEEAEAELA 361
                         90
                 ....*....|.
gi 38683807  883 QLKKQYLEVKA 893
Cdd:COG1196  362 EAEEALLEAEA 372
PRK12704 PRK12704
phosphodiesterase; Provisional
805-890 1.00e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   805 ESIVEEAQ------GKLTELE-----QRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKtREEQIQKKQKILE------ 867
Cdd:PRK12704   41 KRILEEAKkeaeaiKKEALLEakeeiHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR-KLELLEKREEELEkkekel 119
                          90       100
                  ....*....|....*....|....*...
gi 38683807   868 -----ELQKVERELQLKTQQQLKKqyLE 890
Cdd:PRK12704  120 eqkqqELEKKEEELEELIEEQLQE--LE 145
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1075-1113 1.04e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 1.04e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 38683807   1075 IDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRD 1113
Cdd:pfam12796   53 ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
1270-1327 1.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807   1270 LLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPpvPSSRDTALTIA 1327
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK--DEEGLTALDLA 56
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
805-886 1.08e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  805 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSlELAHADQLTKEKIE---ELNKtREEQIQKKQKILEELQKVERELQLKTq 881
Cdd:COG2433  419 EEQVERLEAEVEELEAELEEKDERIERLER-ELSEARSEERREIRkdrEISR-LDREIERLERELEEERERIEELKRKL- 495

                 ....*
gi 38683807  882 QQLKK 886
Cdd:COG2433  496 ERLKE 500
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
2024-2350 1.17e-03

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.52  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2024 PTNATYPMPTAkehypVSSPSSPSPPAQPGGVSRNSPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSS 2103
Cdd:pfam05109  455 PTNLTAPASTG-----PTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTT 529
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2104 AHSNQQQP------PGSVSQEPRP----PLQQSQVPPPEVrmTVPPLATSSAPVAVPSTAP-VTYPM-----PQTPMGCP 2167
Cdd:pfam05109  530 PTPNATSPtlgktsPTSAVTTPTPnatsPTPAVTTPTPNA--TIPTLGKTSPTSAVTTPTPnATSPTvgetsPQANTTNH 607
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2168 QPTPKMETPAI-RPPPHGTTAPHKNSASVQNSSVAVLSVnhikRPHSVPSSVQlPSTLSTQSACQNSVHPANKPIAPNFS 2246
Cdd:pfam05109  608 TLGGTSSTPVVtSPPKNATSAVTTGQHNITSSSTSSMSL----RPSSISETLS-PSTSDNSTSHMPLLTSAHPTGGENIT 682
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   2247 APLPfgpfstlfenSPTSAHafwggSVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFRPPLQRPAP-SPSGivnm 2325
Cdd:pfam05109  683 QVTP----------ASTSTH-----HVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPqAPSG---- 743
                          330       340
                   ....*....|....*....|....*
gi 38683807   2326 dspYGSVTPSSTHLGNFASNISGGQ 2350
Cdd:pfam05109  744 ---QKTAVPTVTSTGGKANSTTGGK 765
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
811-893 1.27e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.91  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    811 AQGKLTELEQRIKEaIEKNAQLQSlelAHADQ--LTKEKIEE-LNKTRE--EQIQKKQKILEELQ-KVERELQLKT---Q 881
Cdd:pfam05622  330 ANQRILELQQQVEE-LQKALQEQG---SKAEDssLLKQKLEEhLEKLHEaqSELQKKKEQIEELEpKQDSNLAQKIdelQ 405
                           90
                   ....*....|..
gi 38683807    882 QQLKKQYLEVKA 893
Cdd:pfam05622  406 EALRKKDEDMKA 417
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1082-1110 1.29e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.29e-03
                            10        20
                    ....*....|....*....|....*....
gi 38683807    1082 NHDTALTLACAGGHEELVQTLLERGASIE 1110
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
1084-1231 1.31e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.23  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1084 DTALTLACAGGHEELVQTLLERGAS-----IEHRDKKGFTPLILAATAGHVGVVEILLDNGADIeaQSERTKDT------ 1152
Cdd:cd22192   52 ETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLVRELIARGADV--VSPRATGTffrpgp 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1153 ---------PLSLACSGGRQEVVELLLARGANKEHRNVSDYTP---LSLAASGGYV-NIIKILLNAGAEINSRTGSKL-- 1217
Cdd:cd22192  130 knliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVlhiLVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVpn 209
                        170
                 ....*....|....*.
gi 38683807 1218 --GISPLMLAAMNGHT 1231
Cdd:cd22192  210 nqGLTPFKLAAKEGNI 225
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
808-890 1.32e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  808 VEEAQGKLTELEQRIKEAIEKNAQLQslelAHADQLtKEKIEELNKTREEQIQKKQKILEELQKVERELQL--KTQQQLK 885
Cdd:COG4372  103 LESLQEEAEELQEELEELQKERQDLE----QQRKQL-EAQIAELQSEIAEREEELKELEEQLESLQEELAAleQELQALS 177

                 ....*
gi 38683807  886 KQYLE 890
Cdd:COG4372  178 EAEAE 182
KH-I_Rnc1_rpt1 cd22455
first type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
1740-1789 1.41e-03

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


Pssm-ID: 411883  Cd Length: 70  Bit Score: 39.20  E-value: 1.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 38683807 1740 VIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLI 1789
Cdd:cd22455   15 IIGKGGENIARLRATTGVKAGVSKVVPGVHDRVLTVSGPLEGVAKAFGLI 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
808-887 1.42e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  808 VEEAQGKLTELEQRIKEAIEKNAQLQS--LELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQQLK 885
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEelAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                 ..
gi 38683807  886 KQ 887
Cdd:COG1196  377 AE 378
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1183-1210 1.47e-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: 1.47e-03
                            10        20
                    ....*....|....*....|....*...
gi 38683807    1183 DYTPLSLAASGGYVNIIKILLNAGAEIN 1210
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
2111-2243 1.49e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.93  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2111 PPGSVSQEPRPPLQQSQVPPPevrmtVPPLATSSAPVAVPSTAPVTYPMPQTPmgcPQPTPKMETPAIRPPPhgttAPHK 2190
Cdd:PRK14951  373 AAPAEKKTPARPEAAAPAAAP-----VAQAAAAPAPAAAPAAAASAPAAPPAA---APPAPVAAPAAAAPAA----APAA 440
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 38683807  2191 NSASVQNSSVAvlSVNHIKRPHSVPSSVQlPSTLSTQSACQNSVHPANKPIAP 2243
Cdd:PRK14951  441 APAAVALAPAP--PAQAAPETVAIPVRVA-PEPAVASAAPAPAAAPAAARLTP 490
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
809-891 1.49e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  809 EEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTK--EKI----EELNKTrEEQIQKKQKILEELQKVERELQlKTQQ 882
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAleRRIaalaRRIRAL-EQELAALEAELAELEKEIAELR-AELE 100

                 ....*....
gi 38683807  883 QLKKQYLEV 891
Cdd:COG4942  101 AQKEELAEL 109
Ank_5 pfam13857
Ankyrin repeats (many copies);
1168-1225 1.50e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807   1168 LLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSklGISPLMLA 1225
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE--GLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1087-1275 1.52e-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: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1087 LTLACAGGHEELVQTLLERGASIEHRDKkgftpLILAATAGHVGVVE----ILLDNGADI--------EAQSERTKD-TP 1153
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDAVEaillHLLAAFRKSgplelandQYTSEFTPGiTA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1154 LSLACSGGRQEVVELLLARGAN------------KEHRNVSDYT--PLSLAASGGYVNIIKILLNAGAEInsRTGSKLGI 1219
Cdd:TIGR00870  132 LHLAAHRQNYEIVKLLLERGASvparacgdffvkSQGVDSFYHGesPLNAAACLGSPSIVALLSEDPADI--LTADSLGN 209
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683807   1220 SPLMLAAMNGHTAAV---------KLLLDMG--SDINAQIE--TNRN--TALTLACFQGRTEVVSLLLDRK 1275
Cdd:TIGR00870  210 TLLHLLVMENEFKAEyeelscqmyNFALSLLdkLRDSKELEviLNHQglTPLKLAAKEGRIVLFRLKLAIK 280
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1082-1114 1.54e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 1.54e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 38683807   1082 NHDTALTLACA-GGHEELVQTLLERGASIEHRDK 1114
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
805-887 1.61e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  805 ESIVEEAQGKLTELEQRIKEAIEKNAQLQS--LELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQ 882
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAEEYELLAelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345

                 ....*
gi 38683807  883 QLKKQ 887
Cdd:COG1196  346 LEEAE 350
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
365-584 1.62e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  365 ENGHTPLMEAgsaghvevarlLLEngagINTHSNEFKESALTLACYKGHLEmvRFLleaGADQEHKTDEMHTALMEACMD 444
Cdd:cd22194   92 DTGKTCLMKA-----------LLN----INENTKEIVRILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIER 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  445 GHVEVARLLLDSGAQVNMPA-----------DSF---ESPLTLAACGGHVELAALLIERGAsleevndegyTPLMEAARE 510
Cdd:cd22194  152 RQGDIVKLLIAKGADVNAHAkgvffnpkykhEGFyfgETPLALAACTNQPEIVQLLMEKES----------TDITSQDSR 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  511 GHEEMVALLlgqganINAQTEETQETALTlaccggflEVADFLIKAGADIELGCS------TPLMEAAQEGHLELVKYLL 584
Cdd:cd22194  222 GNTVLHALV------TVAEDSKTQNDFVK--------RMYDMILLKSENKNLETIrnneglTPLQLAAKMGKAEILKYIL 287
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
808-892 1.72e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   808 VEEAQGKLTE----LEQRIKEAIEKNAQLQslELAHADQLTKEKIEELnKTREEQIQKKQKILEELQKVERELQLKTQQQ 883
Cdd:PRK03918  312 IEKRLSRLEEeingIEERIKELEEKEERLE--ELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTPEK 388

                  ....*....
gi 38683807   884 LKKQYLEVK 892
Cdd:PRK03918  389 LEKELEELE 397
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
809-890 1.80e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  809 EEAQGKLTELEQRIKEAIEKNAQLQSlELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVER-ELQLKTQQQLKKQ 887
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEE-ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEElEEAEEALLERLER 418

                 ...
gi 38683807  888 YLE 890
Cdd:COG1196  419 LEE 421
PRK10263 PRK10263
DNA translocase FtsK; Provisional
2125-2319 1.88e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.92  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2125 QSQVPPPEVRMTVPPLATSSAPVAVPSTAPVTYPMPQTPmgcpqptpkmeTPAIRPPPHGTTaPHKNSASVQNSSVAvls 2204
Cdd:PRK10263  331 QSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTG-----------EPVIAPAPEGYP-QQSQYAQPAVQYNE--- 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2205 vnHIKRPHSVPSSVQLPSTLSTQSACQNSVHPAnKPIAPNFSAPLPFGPfstlfensptSAHAFWGGSVVSSQSTPESML 2284
Cdd:PRK10263  396 --PLQQPVQPQQPYYAPAAEQPAQQPYYAPAPE-QPAQQPYYAPAPEQP----------VAGNAWQAEEQQSTFAPQSTY 462
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 38683807  2285 SGKSSYLpnsDPLHQSDTSKAPGFRPPLQRPAPSP 2319
Cdd:PRK10263  463 QTEQTYQ---QPAAQEPLYQQPQPVEQQPVVEPEP 494
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1085-1136 1.91e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 1.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 38683807  1085 TALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL 1136
Cdd:PTZ00322  117 TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
KH-I_IGF2BP2_rpt4 cd22500
fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
1730-1794 1.92e-03

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: 39.35  E-value: 1.92e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807 1730 VSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTGDRIITIRGGTESTRQATQLINALIK 1794
Cdd:cd22500    6 IKVPSSAAGRVIGKGGKTVNELQNLTSAEVIVprDQTPDENEEVIVKIIGHFFASQTAQRKIREIVQ 72
PHA02798 PHA02798
ankyrin-like protein; Provisional
1097-1210 2.00e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1097 ELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILL---DNGADIEAQSERTKdTPLSLACSGGRQ---EVVELLL 1170
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGF-TMLQVYLQSNHHidiEIIKLLL 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 38683807  1171 ARGAN-KEHRNVSDYTPLSLAASGGY----VNIIKILLNAGAEIN 1210
Cdd:PHA02798  169 EKGVDiNTHNNKEKYDTLHCYFKYNIdridADILKLFVDNGFIIN 213
Ank_5 pfam13857
Ankyrin repeats (many copies);
616-671 2.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807    616 LLQAG-ADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDhTVLSLA 671
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
597-625 2.20e-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: 2.20e-03
                           10        20
                   ....*....|....*....|....*....
gi 38683807    597 GDTALTYACENGHTDVADVLLQAGADLEH 625
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1120-1374 2.22e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1120 LILAATAGHVGVVEILLDNGADIEAQS-ERTKDTPLSLACSGGR-QEVVELLLarganKEHRNVSDYTPLSLAASGGYVN 1197
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEPKKLNINCpDRLGRSALFVAAIENEnLELTELLL-----NLSCRGAVGDTLLHAISLEYVD 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1198 ----IIKILLNAGAE------INSRTGSKL--GISPLMLAAMNGHTAAVKLLLDMGSDINAQietnrntaltlAC---FQ 1262
Cdd:TIGR00870   96 aveaILLHLLAAFRKsgplelANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPAR-----------ACgdfFV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   1263 GRTEVVSLLLDRkanvehraktglTPLMEAASGGYAEVGRVLLDKGADVNAppvpssRDT-------ALTIAAD-KGHYK 1334
Cdd:TIGR00870  165 KSQGVDSFYHGE------------SPLNAAACLGSPSIVALLSEDPADILT------ADSlgntllhLLVMENEfKAEYE 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38683807   1335 F----C-ELLIGRGAHID-------VRNKKGNTPLWLAANGGHLDVVQLLVQ 1374
Cdd:TIGR00870  227 ElscqMyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLA 278
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
814-893 2.29e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.56  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  814 KLTELEQRIKEAIEKN--AQLQSLELAHADQLTKEKIEELNKTREEQIQK-KQKILEELQKVERELQ------LKTQQQL 884
Cdd:cd16269  192 ALTEKEKEIEAERAKAeaAEQERKLLEEQQRELEQKLEDQERSYEEHLRQlKEKMEEERENLLKEQEraleskLKEQEAL 271

                 ....*....
gi 38683807  885 KKQYLEVKA 893
Cdd:cd16269  272 LEEGFKEQA 280
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
805-892 2.30e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    805 ESIVEEAQGKLTELEQR---IKEAIEKNAQLQS--LELahadqltKEKIEELNKTREEQIQKKQKILEELQKVEREL-QL 878
Cdd:TIGR04523  186 QKNIDKIKNKLLKLELLlsnLKKKIQKNKSLESqiSEL-------KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLnQL 258
                           90
                   ....*....|....*....
gi 38683807    879 KTQQ-----QLKKQYLEVK 892
Cdd:TIGR04523  259 KDEQnkikkQLSEKQKELE 277
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
814-892 2.35e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  814 KLTELEQRIKEAIEKNAQLQSL--ELAHADQLTKEKIEELNKTRE-----EQIQKKQKILEELQKVERELQLKTQQ--QL 884
Cdd:COG4717   72 ELKELEEELKEAEEKEEEYAELqeELEELEEELEELEAELEELREeleklEKLLQLLPLYQELEALEAELAELPERleEL 151

                 ....*...
gi 38683807  885 KKQYLEVK 892
Cdd:COG4717  152 EERLEELR 159
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
350-421 2.44e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 2.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38683807   350 VKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKeSALTLACYKGHLEMVRFLL 421
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLS 168
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1142-1370 2.60e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.21  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1142 IEAQSERTKDTPLSL--ACSGGRQEVVELLlargANKEHRN-------VSDYTPLSLAASG-GYVNIIKILLNagaeINS 1211
Cdd:cd22194   36 AELAKEEQRDKKKRLkkVSEAAVEELGELL----KELKDLSrrrrktdVPDFLMHKLTASDtGKTCLMKALLN----INE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1212 RTGSklgISPLMLAAMNGHTAAVKLlldmgsdINAQIeTNRN----TALTLACFQGRTEVVSLLLDRKANVEHRAKT--- 1284
Cdd:cd22194  108 NTKE---IVRILLAFAEENGILDRF-------INAEY-TEEAyegqTALNIAIERRQGDIVKLLIAKGADVNAHAKGvff 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1285 -----------GLTPLMEAASGGYAEVGRVLLDKGADVNappvpSSRDT-------ALTIAAD--KGHYKFCE------L 1338
Cdd:cd22194  177 npkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDI-----TSQDSrgntvlhALVTVAEdsKTQNDFVKrmydmiL 251
                        250       260       270
                 ....*....|....*....|....*....|...
gi 38683807 1339 LIGRGAHID-VRNKKGNTPLWLAANGGHLDVVQ 1370
Cdd:cd22194  252 LKSENKNLEtIRNNEGLTPLQLAAKMGKAEILK 284
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
436-652 2.63e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.25  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  436 TALMEACM---DGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAaLLIERgasleevndegytplmeaaREGH 512
Cdd:cd22193   31 TCLMKALLnlnPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEGQTALH-IAIER-------------------RQGD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  513 eeMVALLLGQGANINAQTeetqetaltlacCGGFLEVADflikAGADIELGcSTPLMEAAQEGHLELVKYLLA---AGAN 589
Cdd:cd22193   91 --IVALLVENGADVHAHA------------KGRFFQPKY----QGEGFYFG-ELPLSLAACTNQPDIVQYLLEnehQPAD 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807  590 VHATTATGDT---ALTYACENGHTDVA------DVLLQAGADLEHESE-------GGRTPLMKAARAGHVCTVQFLISK 652
Cdd:cd22193  152 IEAQDSRGNTvlhALVTVADNTKENTKfvtrmyDMILIRGAKLCPTVEleeirnnDGLTPLQLAAKMGKIEILKYILQR 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
1085-1203 2.85e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1085 TALTLACAGGHEELVQTLLERGASIEHRDKKGF-------------TPLILAATAGHVGVVEILLDNGADIEAQSER--- 1148
Cdd:cd21882   75 TALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGAQPAALEAQdsl 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807 1149 -----------TKDTP--LSLACSggrqeVVELLLARGANKEH-------RNVSDYTPLSLAASGGYVNIIKILL 1203
Cdd:cd21882  155 gntvlhalvlqADNTPenSAFVCQ-----MYNLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGKIVMFQHIL 224
PRK12704 PRK12704
phosphodiesterase; Provisional
811-892 2.87e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   811 AQGKLTELEQR----IKEA------IEKNAQLQSLELAH-----ADQLTKEKIEELNKT------REEQIQKKQKILE-- 867
Cdd:PRK12704   29 AEAKIKEAEEEakriLEEAkkeaeaIKKEALLEAKEEIHklrneFEKELRERRNELQKLekrllqKEENLDRKLELLEkr 108
                          90       100
                  ....*....|....*....|....*..
gi 38683807   868 --ELQKVERELQlKTQQQLKKQYLEVK 892
Cdd:PRK12704  109 eeELEKKEKELE-QKQQELEKKEEELE 134
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
303-329 3.01e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 3.01e-03
                           10        20
                   ....*....|....*....|....*..
gi 38683807    303 TPLMAAANGGHVKIVKLLLAHKADVNA 329
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_IGF2BP_rpt3 cd22402
third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
1732-1789 3.02e-03

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


Pssm-ID: 411830 [Multi-domain]  Cd Length: 66  Bit Score: 38.39  E-value: 3.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807 1732 VPSTVISRVIGRGGCNINAIREFTGAHIDI-DKQKDKTGDRIITIRGGTESTRQATQLI 1789
Cdd:cd22402    7 IPNKAVGAIIGTKGSHIRYIKRFSGASIKIaPADSPDAPERKVTITGPPEAQWKAQLCI 65
PHA02859 PHA02859
ankyrin repeat protein; Provisional
398-527 3.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.34  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   398 NEFKESALtLACY---KGHLEMVRFLLEAGADQEHKTDEMHTALMEACM----DGHVEVARLLLDSGAQVNMPADSFESP 470
Cdd:PHA02859   48 NDLYETPI-FSCLekdKVNVEILKFLIENGADVNFKTRDNNLSALHHYLsfnkNVEPEILKILIDSGSSITEEDEDGKNL 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807   471 L--TLAACGGHVELAALLIERGASLEEVNDEG----YTPLMeaaREGHEEMVALLLGQGANIN 527
Cdd:PHA02859  127 LhmYMCNFNVRINVIKLLIDSGVSFLNKDFDNnnilYSYIL---FHSDKKIFDFLTSLGIDIN 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
403-426 3.52e-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: 3.52e-03
                            10        20
                    ....*....|....*....|....
gi 38683807     403 SALTLACYKGHLEMVRFLLEAGAD 426
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGAD 27
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
805-883 3.71e-03

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 39.44  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  805 ESIVEEAQGKLTELEQRIKEAIEKNAQLQSlELAHADQLTKEKIEELNKTREEQiqkKQKILEELQKV--ERELQLKTQQ 882
Cdd:cd20482    6 QQLLEEARAKIPELRDALKNVEHALSRLQM-QYHKAQNEINETFQFYRSMLEER---KDELLKELESIynAKQLSLNEQQ 81

                 .
gi 38683807  883 Q 883
Cdd:cd20482   82 Q 82
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
800-890 3.87e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 40.38  E-value: 3.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    800 TNQSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSlELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELqlk 879
Cdd:pfam11559   67 EIERLQSKIERLKTQLEDLERELALLQAKERQLEK-KLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREI--- 142
                           90
                   ....*....|.
gi 38683807    880 tqQQLKKQYLE 890
Cdd:pfam11559  143 --EKLKERLAQ 151
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
334-365 3.99e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 3.99e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 38683807    334 GNTALTYACA-GGYVDVVKVLLESGASIEDHNE 365
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
826-886 4.03e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.47  E-value: 4.03e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807    826 IEKNAQLQSLELAHADQLTK-EKIEELNKTREEQIQKKQKILEE-LQKVE---RELQLKTQQQLKK 886
Cdd:pfam13863    2 LEKKREMFLVQLALDAKREEiERLEELLKQREEELEKKEQELKEdLIKFDkflKENDAKRRRALKK 67
KH-I_FUBP3_rpt1 cd22480
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1727-1793 4.49e-03

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


Pssm-ID: 411908 [Multi-domain]  Cd Length: 71  Bit Score: 37.95  E-value: 4.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22480    2 TEEYKVPDKMVGFIIGRGGEQISRIQLESGCKIQIAPDSGGMPERPCVLTGTPESIEQAKRLLGQIV 68
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1285-1313 4.53e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 4.53e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683807   1285 GLTPLMEAA-SGGYAEVGRVLLDKGADVNA 1313
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
805-892 4.56e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.79  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  805 ESIVEEAQGKLTELEQRIKEaiEKNAQLQ--------SLElAHADQLTKEKIEELNKTREEQiqkkQKILEELQKVEREL 876
Cdd:cd16269  199 EIEAERAKAEAAEQERKLLE--EQQRELEqkledqerSYE-EHLRQLKEKMEEERENLLKEQ----ERALESKLKEQEAL 271
                         90       100
                 ....*....|....*....|
gi 38683807  877 Q----LKTQQQLKKQYLEVK 892
Cdd:cd16269  272 LeegfKEQAELLQEEIRSLK 291
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
1725-1759 4.75e-03

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


Pssm-ID: 411849  Cd Length: 70  Bit Score: 37.71  E-value: 4.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 38683807 1725 RRSKKVSVPSTVISRVIGRGGCNINAIREFTGAHI 1759
Cdd:cd22421    2 RVTLKMDVSHTDHSHVIGKGGNNIKKVMEDTGCHI 36
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
808-892 4.81e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   808 VEEAQGKLTELEQRIKEAIEKNAQLQSLElahaDQLtkEKIEELNKTREEQIQKKQKILEELQKVEREL----------- 876
Cdd:PRK03918  517 LEELEKKAEEYEKLKEKLIKLKGEIKSLK----KEL--EKLEELKKKLAELEKKLDELEEELAELLKELeelgfesveel 590
                          90
                  ....*....|....*...
gi 38683807   877 --QLKTQQQLKKQYLEVK 892
Cdd:PRK03918  591 eeRLKELEPFYNEYLELK 608
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1730-1789 4.95e-03

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


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 37.54  E-value: 4.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1730 VSVPSTVISRVIGRGGCNINAIREFTGAHIDIdkQKDKTGDRIITIRGGTESTRQATQLI 1789
Cdd:cd22408    4 VEVPKSQHRFVIGPRGSTIQEILEETGCSVEV--PPNDSDSETITLRGPADKLGAALTLV 61
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1096-1238 5.08e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.05  E-value: 5.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1096 EELVQTLLERG-----------ASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERT-------------KD 1151
Cdd:cd22194  110 KEIVRILLAFAeengildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfGE 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1152 TPLSLACSGGRQEVVELLL-----------ARGANKEHR--NVSDytplslaASGGYVNIIK-----ILLNAGAEINSRT 1213
Cdd:cd22194  190 TPLALAACTNQPEIVQLLMekestditsqdSRGNTVLHAlvTVAE-------DSKTQNDFVKrmydmILLKSENKNLETI 262
                        170       180
                 ....*....|....*....|....*
gi 38683807 1214 GSKLGISPLMLAAMNGHTAAVKLLL 1238
Cdd:cd22194  263 RNNEGLTPLQLAAKMGKAEILKYIL 287
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
2160-2328 5.44e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 41.90  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2160 PQTPMGCPQPTPKMETPAIRPPPHgtTAPHKNSAS--------VQNSSVAVLSVNHIKRPHSVPSSVQLPSTLSTQS--- 2228
Cdd:PRK12727   60 SDTPATAAAPAPAPQAPTKPAAPV--HAPLKLSANanmsqrqrVASAAEDMIAAMALRQPVSVPRQAPAAAPVRAASips 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2229 -ACQNSVHPANKPIAPNFSAPLPFGPfSTLFENSPTSA----HAFWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDts 2303
Cdd:PRK12727  138 pAAQALAHAAAVRTAPRQEHALSAVP-EQLFADFLTTApvprAPVQAPVVAAPAPVPAIAAALAAHAAYAQDDDEQLD-- 214
                         170       180       190
                  ....*....|....*....|....*....|
gi 38683807  2304 kAPGFR-----PPLQRPAPSPSGIVNMDSP 2328
Cdd:PRK12727  215 -DDGFDlddalPQILPPAALPPIVVAPAAP 243
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
1185-1320 5.44e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 5.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1185 TPLSLAASGGYVNIIKILLNAGAEINSR-----------TGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNR- 1252
Cdd:cd21882   75 TALHIAIENRNLNLVRLLVENGADVSARatgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSl 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1253 -NTALTLACFQGR---------TEVVSLLLDRKANVEHRAK-------TGLTPLMEAASGGYAEVGRVLLDKgaDVNAPP 1315
Cdd:cd21882  155 gNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQR--EFSGPY 232

                 ....*
gi 38683807 1316 VPSSR 1320
Cdd:cd21882  233 QPLSR 237
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
1164-1308 5.48e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.05  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1164 EVVELLLA---------RGANKEHRNvSDY---TPLSLAASGGYVNIIKILLNAGAEINSRT------------GSKLGI 1219
Cdd:cd22194  111 EIVRILLAfaeengildRFINAEYTE-EAYegqTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykheGFYFGE 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 1220 SPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNT---ALTLAC--FQGRTEVVSLLLD------RKANVEH-RAKTGLT 1287
Cdd:cd22194  190 TPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTvlhALVTVAedSKTQNDFVKRMYDmillksENKNLETiRNNEGLT 269
                        170       180
                 ....*....|....*....|....*.
gi 38683807 1288 PLMEAASGGYAEV-----GRVLLDKG 1308
Cdd:cd22194  270 PLQLAAKMGKAEIlkyilSREIKEKP 295
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
817-887 5.81e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 5.81e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38683807    817 ELEQRIKEA---IEKNAQLQSLELAHADQLTKEKieELNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQ 887
Cdd:pfam13868   10 ELNSKLLAAkcnKERDAQIAEKKRIKAEEKEEER--RLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ 81
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
566-592 5.82e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 5.82e-03
                           10        20
                   ....*....|....*....|....*..
gi 38683807    566 TPLMEAAQEGHLELVKYLLAAGANVHA 592
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
808-887 5.87e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 5.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  808 VEEAQGKLTELEQRIKEAIEKNAQLQslelahadQLTKEKIEELNKtREEQIQKKQKILEELQKVERELQL-KTQQQLKK 886
Cdd:COG4372  117 LEELQKERQDLEQQRKQLEAQIAELQ--------SEIAEREEELKE-LEEQLESLQEELAALEQELQALSEaEAEQALDE 187

                 .
gi 38683807  887 Q 887
Cdd:COG4372  188 L 188
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
818-893 6.19e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 6.19e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807  818 LEQRIKEAIEKNAQLQSlELAHADQLTKEKIEELNKTrEEQIQKKQKileELQKVERELQlKTQQQLKKQYLEVKA 893
Cdd:COG4372   29 LSEQLRKALFELDKLQE-ELEQLREELEQAREELEQL-EEELEQARS---ELEQLEEELE-ELNEQLQAAQAELAQ 98
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
238-323 6.26e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   238 LAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVE--DRGIKgdiTPLMAAANGGHVK 315
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTllDKDGK---TPLELAEENGFRE 162

                  ....*...
gi 38683807   316 IVKLLLAH 323
Cdd:PTZ00322  163 VVQLLSRH 170
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1115-1144 6.36e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 6.36e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 38683807   1115 KGFTPLILAATAGHVGVVEILLDNGADIEA 1144
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
809-887 6.57e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 6.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38683807  809 EEAQGKLTELEQRIKEAIEKNAQLQSLElahaDQLTKEKiEELNKTREEQIQKKqkilEELQKVERELQLKTQQQLKKQ 887
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAR----EELEQLE-EELEQARSELEQLE----EELEELNEQLQAAQAELAQAQ 100
Ank_5 pfam13857
Ankyrin repeats (many copies);
1304-1360 6.58e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 6.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 38683807   1304 LLDKG-ADVNAPPvpSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLA 1360
Cdd:pfam13857    1 LLEHGpIDLNRLD--GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
805-893 6.65e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 40.27  E-value: 6.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    805 ESIVEEAQGKLTELEQRIKEAIEknaQLQSLELAHADQLtKEKIEELNKT---REEQIQKKQKIL----EELQKVERELQ 877
Cdd:pfam10368   17 EKPFEEQQEPLVELEKKEQELYE---EIIELGMDEFDEI-KKLSDEALENveeREELLEKEKESIeeakEEFKKIKEIIE 92
                           90
                   ....*....|....*.
gi 38683807    878 LKTQQQLKKQYLEVKA 893
Cdd:pfam10368   93 EIEDEELKKEAEELID 108
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
435-461 6.85e-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: 6.85e-03
                           10        20
                   ....*....|....*....|....*...
gi 38683807    435 HTALMEAC-MDGHVEVARLLLDSGAQVN 461
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
809-892 7.04e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   809 EEAQGKLTELE---QRIKEAIEKNAQL----------QSLELA-HADQLT--KEKIEELN------KTREEQIQKKQKIL 866
Cdd:PRK02224  422 DELREREAELEatlRTARERVEEAEALleagkcpecgQPVEGSpHVETIEedRERVEELEaeledlEEEVEEVEERLERA 501
                          90       100
                  ....*....|....*....|....*..
gi 38683807   867 EELQKVERELQ-LKTQQQLKKQYLEVK 892
Cdd:PRK02224  502 EDLVEAEDRIErLEERREDLEELIAER 528
KH-I_PCBP1_2_rpt2 cd22518
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
1729-1789 7.06e-03

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


Pssm-ID: 411946 [Multi-domain]  Cd Length: 78  Bit Score: 37.79  E-value: 7.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807 1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTgDRIITIRGGTESTRQATQLI 1789
Cdd:cd22518   10 RLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVagDMLPNST-ERAITIAGIPQSIIECVKQI 71
PHA02798 PHA02798
ankyrin-like protein; Provisional
380-538 7.07e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   380 VEVARLLLENGAGINTHSNEFKESALTLAC----YKGHLEMVRFLLEAGADQEHKTDEMHTALMeaCMdghvevarllLD 455
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdYKHMLDIVKILIENGADINKKNSDGETPLY--CL----------LS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   456 SGAQVNMpadsfespltlaacgghvELAALLIERGASLEEVNDEGYTPLMEAAREGHE---EMVALLLGQGANINAQTEE 532
Cdd:PHA02798  119 NGYINNL------------------EILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNK 180

                  ....*.
gi 38683807   533 TQETAL 538
Cdd:PHA02798  181 EKYDTL 186
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
809-893 7.10e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.64  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    809 EEAQGKLTELEQRIKEA-IEKNAQLQSLElahadqltkekiEELNKTREEQIQKKQKILEELQKVERELQLKTQQQlkKQ 887
Cdd:pfam05672   39 EEERLRKEELRRRAEEErARREEEARRLE------------EERRREEEERQRKAEEEAEEREQREQEEQERLQKQ--KE 104

                   ....*.
gi 38683807    888 YLEVKA 893
Cdd:pfam05672  105 EAEAKA 110
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
821-892 7.14e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 40.31  E-value: 7.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38683807  821 RIKEAIEKNAQlqslelAHADQLTKEKIEELNKTREEQIQKKQKILEE-LQKVERELQLKTQQQLKKQYLEVK 892
Cdd:COG1390    6 KIIEEILEEAE------AEAEEILEEAEEEAEKILEEAEEEAEEIKEEiLEKAEREAEREKRRIISSAELEAR 72
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
808-893 7.18e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 7.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  808 VEEAQGKLTELEQRIKEAIEK----NAQLQSLeLAHADQLTKE----------KIEELNKTREEQIQKKQKIlEELQKVE 873
Cdd:COG1340  169 LKELRKEAEEIHKKIKELAEEaqelHEEMIEL-YKEADELRKEadelhkeiveAQEKADELHEEIIELQKEL-RELRKEL 246
                         90       100
                 ....*....|....*....|...
gi 38683807  874 REL---QLKTQQQLKKQYLEVKA 893
Cdd:COG1340  247 KKLrkkQRALKREKEKEELEEKA 269
PHA02884 PHA02884
ankyrin repeat protein; Provisional
609-715 7.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.12  E-value: 7.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807   609 HTDVADVLLQAGADLEHE---SEGGRT-PLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLL 684
Cdd:PHA02884   45 YTDIIDAILKLGADPEAPfplSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124
                          90       100       110
                  ....*....|....*....|....*....|.
gi 38683807   685 AHGADPTHRLKDGSTMlIEAAkgghtSVVCY 715
Cdd:PHA02884  125 SYGADINIQTNDMVTP-IELA-----LMICN 149
KH-I_FUBP3_rpt3 cd22486
third type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
1727-1793 7.39e-03

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


Pssm-ID: 411914  Cd Length: 70  Bit Score: 37.24  E-value: 7.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22486    4 SIEVSVPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGISPERVAQVMGPPDRCQHAAHIINELI 70
KH-I_AtC3H36_like cd22464
type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana zinc finger CCCH ...
1729-1793 7.57e-03

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


Pssm-ID: 411892 [Multi-domain]  Cd Length: 66  Bit Score: 37.07  E-value: 7.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38683807 1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22464    2 KISVDASLAGAIIGKGGVNSKQICRETGVKLSIRDHERDPNLKNVELEGSFEQIKEASGMVRELI 66
PHA02798 PHA02798
ankyrin-like protein; Provisional
1302-1411 7.77e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  1302 RVLLDKGADVNAppVPSSRDTAL-TIAADKGHYK----FCELLIGRGAHIDVRNKKGNTPLW-LAANG--GHLDVVQLLV 1373
Cdd:PHA02798   55 KLFINLGANVNG--LDNEYSTPLcTILSNIKDYKhmldIVKILIENGADINKKNSDGETPLYcLLSNGyiNNLEILLFMI 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 38683807  1374 QAGADVDAADNRKITPLMAAFRKGH---VKVVRYLVK---EVNQ 1411
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEkgvDINT 176
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
774-882 7.97e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 7.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  774 IRNKAASKQKSSSHLPANSQDVQGYITNQSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSLE-------------LAHA 840
Cdd:COG4717  107 LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEaelaelqeeleelLEQL 186
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 38683807  841 DQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQ 882
Cdd:COG4717  187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
436-462 7.97e-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: 7.97e-03
                           10        20
                   ....*....|....*....|....*..
gi 38683807    436 TALMEACMDGHVEVARLLLDSGAQVNM 462
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_PCBP4_rpt2 cd22520
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
1729-1793 8.57e-03

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


Pssm-ID: 411948 [Multi-domain]  Cd Length: 72  Bit Score: 37.31  E-value: 8.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807 1729 KVSVPSTVISRVIGRGGCNINAIREFTGAHIDI--DKQKDKTgDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22520    5 RLVIPASQCGSLIGKAGSKIKEIRESTGAQVQVagDLLPNST-ERAVTVSGVPDAIIQCVRQICAVI 70
PHA03291 PHA03291
envelope glycoprotein I; Provisional
2112-2321 8.59e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 41.09  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2112 PGSVSQEPRPPLQQSQVPPPEvrmTVPPLATSSAPVAVPSTAPVTYPMPQTPMGCPQP--TPKMETPAIRPPPHGTTAPh 2189
Cdd:PHA03291  199 PADVFVPATPRPTPRTTASPE---TTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPEAegTPAPPTPGGGEAPPANATP- 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2190 knSASVQNSSVAVLSVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIapnFSAPLPFGP-FSTLFEnsptSAHAF 2268
Cdd:PHA03291  275 --APEASRYELTVTQIIQIAIPASIIACVFLGSCACCLHRRCRRRRRRPARI---YRPPSPVAPsISAVNE----AALAR 345
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 38683807  2269 WGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFrPPLQRPAPSPSG 2321
Cdd:PHA03291  346 LGDELKRHPPESPRRSKRRSSQTMVPSLTAISEESEAPAV-VELSRSPRRPGG 397
Ank_5 pfam13857
Ankyrin repeats (many copies);
420-474 8.67e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 8.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 38683807    420 LLEAG-ADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLA 474
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
KH-I_PEPPER_like_rpt3 cd22461
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
1727-1793 8.71e-03

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


Pssm-ID: 411889  Cd Length: 69  Bit Score: 37.15  E-value: 8.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807 1727 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALI 1793
Cdd:cd22461    3 SQQMQIPLSYADAIIGTAGANISYIRRTSGATITIQETRGAPGEMTVEIHGTQSQVQTAQQLIQNFM 69
Ank_5 pfam13857
Ankyrin repeats (many copies);
353-408 9.20e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 9.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 38683807    353 LLESG-ASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINThSNEFKESALTLA 408
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
2073-2193 9.50e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.30  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807  2073 SSSEQEAGSPPVVETTNTRPPNSSSssgsssahsNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPST 2152
Cdd:PRK14971  372 GRGPKQHIKPVFTQPAAAPQPSAAA---------AASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNPPST 442
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 38683807  2153 APVTYPMPQTPMgcPQPTPKMETPAIRPPphgTTAPHKNSA 2193
Cdd:PRK14971  443 APQAVRPAQFKE--EKKIPVSKVSSLGPS---TLRPIQEKA 478
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
814-890 9.68e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.21  E-value: 9.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    814 KLTELEQRIKEAIEKNAQLQSlELAHADQLTKE---KIEELNKTREEQ-------IQKKQKILEELQKVeRELQlkTQQQ 883
Cdd:pfam05622  305 RLTELQQLLEDANRRKNELET-QNRLANQRILElqqQVEELQKALQEQgskaedsSLLKQKLEEHLEKL-HEAQ--SELQ 380

                   ....*..
gi 38683807    884 LKKQYLE 890
Cdd:pfam05622  381 KKKEQIE 387
SCS2 COG5066
VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and ...
2076-2182 9.89e-03

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


Pssm-ID: 227398 [Multi-domain]  Cd Length: 242  Bit Score: 40.33  E-value: 9.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807 2076 EQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPV 2155
Cdd:COG5066  121 SEEEISKNVHECSEDRGAAVLLVEMPTLLNILYLEVRFFVNQKEVPAEPETQPPVQVKKEEVPPVTQKTVPHENEKQTSV 200
                         90       100
                 ....*....|....*....|....*..
gi 38683807 2156 TYPMPQTPMGCPQPTPKmETPAIRPPP 2182
Cdd:COG5066  201 STPKPQNQIKEAATVPA-ENEPSSMPI 226
NYD-SP28 pfam14772
Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in ...
809-891 9.91e-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: 37.96  E-value: 9.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683807    809 EEAQGKLTELEQRIKEAIE---KNAQLQSLELAH--ADQLTKEKIEELNKTREEQ-------IQKKQKILEELQKverEL 876
Cdd:pfam14772    8 EQRRRKEEELRRFRKEKLEeeaKSSQEKFEKINQrwRSILRKNKPQELREELEEQkqaceriIDRKDKLIKELQQ---EL 84
                           90
                   ....*....|....*...
gi 38683807    877 QLKTQQ---QLKKQYLEV 891
Cdd:pfam14772   85 KEADEQyvkALRKQAEDI 102
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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