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Conserved domains on  [gi|193206531|ref|NP_001122794|]
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Ankyrin repeat and KH domain-containing protein mask-1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-346 1.78e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.54  E-value: 1.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   56 DIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAAIEAQSDRTKDTALSLACSGGRKDVVELLLAHGANK 135
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  136 EHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRtgSKLGISPLMLASMNGHREATRVLLEKGSDINAQiETNRNTAL 215
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  216 TLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLIAAGADTNAspVQQTKDTALTISAEKGHEKFV 295
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIV 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193206531  296 RMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALLEKGADPDMFDNRKI 346
Cdd:COG0666   236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
617-684 3.88e-23

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: 93.85  E-value: 3.88e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193206531  617 WKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQEsnKQAERTVLAKGTPEMVRYAMNIINYMI 684
Cdd:cd22462     1 IEILIPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDS--ATGERIVLISGTPDQARHAQNLIEAFI 66
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-346 1.78e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.54  E-value: 1.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   56 DIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAAIEAQSDRTKDTALSLACSGGRKDVVELLLAHGANK 135
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  136 EHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRtgSKLGISPLMLASMNGHREATRVLLEKGSDINAQiETNRNTAL 215
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  216 TLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLIAAGADTNAspVQQTKDTALTISAEKGHEKFV 295
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIV 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193206531  296 RMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALLEKGADPDMFDNRKI 346
Cdd:COG0666   236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
617-684 3.88e-23

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: 93.85  E-value: 3.88e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193206531  617 WKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQEsnKQAERTVLAKGTPEMVRYAMNIINYMI 684
Cdd:cd22462     1 IEILIPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDS--ATGERIVLISGTPDQARHAQNLIEAFI 66
PHA03095 PHA03095
ankyrin-like protein; Provisional
123-352 8.26e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.40  E-value: 8.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  123 DVVELLLAHGANKEHRNVSDYTPLSL---ASSGGYIEIVNMLLTAGSEINSRtgSKLGISPLMLASMNGHREAT-RVLLE 198
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAP--ERCGFTPLHLYLYNATTLDViKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  199 KGSDINAQIEtNRNTALT--LASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVG--NLLIAAGADTNAsp 274
Cdd:PHA03095  106 AGADVNAKDK-VGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYA-- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  275 VQQTKDTALTISAE--KGHEKFVRMLLNGDAAVDVRNKKGCTALWLACNGGYL--STAQALLEKGADPDMFDNRKISPMM 350
Cdd:PHA03095  183 VDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLH 262

                  ..
gi 193206531  351 AA 352
Cdd:PHA03095  263 YA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
48-139 1.04e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531    48 IACANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLkNHAAIEAQSDrtKDTALSLACSGGRKDVVEL 127
Cdd:pfam12796    3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN--GRTALHYAARSGHLEIVKL 79
                           90
                   ....*....|..
gi 193206531   128 LLAHGANKEHRN 139
Cdd:pfam12796   80 LLEKGADINVKD 91
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
616-681 7.51e-12

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: 61.91  E-value: 7.51e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531   616 SWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEInkIQESNKQAERTVLAKGTPEMVRYAMNIIN 681
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQI--PPSESEGNERIVTITGTPEAVEAAKALIE 64
KH smart00322
K homology RNA-binding domain;
618-684 2.51e-10

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 57.69  E-value: 2.51e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206531    618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESnkqaERTVLAKGTPEMVRYAMNIINYMI 684
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSE----ERVVEITGPPENVEKAAELILEIL 68
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
48-162 2.05e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   48 IACANGHKDIVELLLKEGANIE---------HRDKK-----GFSPLIIAATAGHSSVVEVLLKNHAAIEAQsDRTKDTAL 113
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLGNTVL 173
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193206531  114 ---------SLACsggrkDVVELLLAHGANK-----EH-RNVSDYTPLSLASSGGYIEIVNMLL 162
Cdd:cd22192   174 hilvlqpnkTFAC-----QMYDLILSYDKEDdlqplDLvPNNQGLTPFKLAAKEGNIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
177-205 8.59e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 8.59e-04
                            10        20
                    ....*....|....*....|....*....
gi 193206531    177 GISPLMLASMNGHREATRVLLEKGSDINA 205
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
74-205 4.59e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531    74 KGFSPliiAATAGHSSVVEVLLKNHAAIEAQS-DRTKDTALSLACSGGR-KDVVELLLAHGankehRNVSDYTPLSLASS 151
Cdd:TIGR00870   19 KAFLP---AAERGDLASVYRDLEEPKKLNINCpDRLGRSALFVAAIENEnLELTELLLNLS-----CRGAVGDTLLHAIS 90
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531   152 GGYIEIVNMLLT----------AGSEINSRTGSKL--GISPLMLASMNGHREATRVLLEKGSDINA 205
Cdd:TIGR00870   91 LEYVDAVEAILLhllaafrksgPLELANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPA 156
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-346 1.78e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.54  E-value: 1.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   56 DIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAAIEAQSDRTKDTALSLACSGGRKDVVELLLAHGANK 135
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  136 EHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRtgSKLGISPLMLASMNGHREATRVLLEKGSDINAQiETNRNTAL 215
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  216 TLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLIAAGADTNAspVQQTKDTALTISAEKGHEKFV 295
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA--KDNDGKTALDLAAENGNLEIV 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193206531  296 RMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALLEKGADPDMFDNRKI 346
Cdd:COG0666   236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-316 5.38e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.38  E-value: 5.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   32 NAIDKATETTLETPLTIACANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAAIEAQSDRTKDT 111
Cdd:COG0666    10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  112 ALSLACSGGRKDVVELLLAHGANKEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRTgsKLGISPLMLASMNGHRE 191
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD--NDGNTPLHLAAANGNLE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  192 ATRVLLEKGSDINAQIEtNRNTALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLIAAGADTN 271
Cdd:COG0666   168 IVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 193206531  272 AspVQQTKDTALTISAEKGHEKFVRMLLNGDAAVDVRNKKGCTAL 316
Cdd:COG0666   247 A--KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-380 1.22e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 1.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   94 LLKNHAAIEAQSDRTKDTALSLACSGGRKDVVELLLAHGANKEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRTg 173
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  174 sKLGISPLMLASMNGHREATRVLLEKGSDINAQIEtNRNTALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECAS 253
Cdd:COG0666    85 -DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  254 GGYVDVGNLLIAAGADTNAspVQQTKDTALTISAEKGHEKFVRMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALLE 333
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNA--RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 193206531  334 KGADPDMFDNRKISPMMAAFRKGHVEIVKYMVNSAKQFPNEQDLIRA 380
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-406 4.53e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 4.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  181 LMLASMNGHREATRVLLEKGSDINAQIETNRNTALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVG 260
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  261 NLLIAAGADTNAspVQQTKDTALTISAEKGHEKFVRMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALLEKGADPDM 340
Cdd:COG0666   104 KLLLEAGADVNA--RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206531  341 FDNRKISPMMAAFRKGHVEIVKYMVNS-AKqfPNEQDliRAQQTAETDDIKKKCGECIDIIRSAKKA 406
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAgAD--VNAKD--NDGKTALDLAAENGNLEIVKLLLEAGAD 244
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
617-684 3.88e-23

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: 93.85  E-value: 3.88e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193206531  617 WKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQEsnKQAERTVLAKGTPEMVRYAMNIINYMI 684
Cdd:cd22462     1 IEILIPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDS--ATGERIVLISGTPDQARHAQNLIEAFI 66
PHA03095 PHA03095
ankyrin-like protein; Provisional
123-352 8.26e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.40  E-value: 8.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  123 DVVELLLAHGANKEHRNVSDYTPLSL---ASSGGYIEIVNMLLTAGSEINSRtgSKLGISPLMLASMNGHREAT-RVLLE 198
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAP--ERCGFTPLHLYLYNATTLDViKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  199 KGSDINAQIEtNRNTALT--LASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVG--NLLIAAGADTNAsp 274
Cdd:PHA03095  106 AGADVNAKDK-VGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYA-- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  275 VQQTKDTALTISAE--KGHEKFVRMLLNGDAAVDVRNKKGCTALWLACNGGYL--STAQALLEKGADPDMFDNRKISPMM 350
Cdd:PHA03095  183 VDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLH 262

                  ..
gi 193206531  351 AA 352
Cdd:PHA03095  263 YA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
48-139 1.04e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531    48 IACANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLkNHAAIEAQSDrtKDTALSLACSGGRKDVVEL 127
Cdd:pfam12796    3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN--GRTALHYAARSGHLEIVKL 79
                           90
                   ....*....|..
gi 193206531   128 LLAHGANKEHRN 139
Cdd:pfam12796   80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
146-240 7.53e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 7.53e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   146 LSLASSGGYIEIVNMLLTAGSEINSRTgsKLGISPLMLASMNGHREATRVLLEKgsdINAQIETNRNTALTLASFQGRTE 225
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD--KNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*
gi 193206531   226 VVKLLLAYNANVEHR 240
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
55-404 8.42e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 8.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   55 KDIVELLLKEGANIEHRDKKGFSPLIIAATAGHssvveVLLKNhaaieaqsdrtkdtalslacsggrKDVVELLLAHGAN 134
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKY-----NLTDV------------------------KEIVKLLLEYGAN 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  135 KEHRNVSDYTPLSLASSG--GYIEIVNMLLTAGSEINSRTgsKLGISPLMLASMNGHR--EATRVLLEKGSDINAqieTN 210
Cdd:PHA03100   99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKN--SDGENLLHLYLESNKIdlKILKLLIDKGVDINA---KN 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  211 RntaltlasfqgrtevVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLIAAGADTNAspVQQTKDTALTISAEKG 290
Cdd:PHA03100  174 R---------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL--VNKYGDTPLHIAILNN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  291 HEKFVRMLLNGDAAVDVRNkkgctalwlacnggylstAQALLEKGADpdmFDNRKISPMMaafrkghVEIVKYMVNSAKQ 370
Cdd:PHA03100  237 NKEIFKLLLNNGPSIKTII------------------ETLLYFKDKD---LNTITKIKML-------KKSIMYMFLLDPG 288
                         330       340       350
                  ....*....|....*....|....*....|....
gi 193206531  371 FPNEQDLIraQQTAETDDIKKKCGECIDIIRSAK 404
Cdd:PHA03100  289 FYKNRKLI--ENSKSLKDVINECEKEIERMKEIK 320
PHA03095 PHA03095
ankyrin-like protein; Provisional
55-248 1.10e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.85  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   55 KDIVELLLKEGANIEHRDKKGFSPLIIAATAGHS-SVVEVLLKNHAAIEAqSDRTKDTALSLACSGG--RKDVVELLLAH 131
Cdd:PHA03095   63 KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNA-KDKVGRTPLHVYLSGFniNPKVIRLLLRK 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  132 GANKEHRNVSDYTPLS--LASSGGYIEIVNMLLTAGSEI---------------------------------NSRTGSKL 176
Cdd:PHA03095  142 GADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVyavddrfrsllhhhlqsfkprarivreliragcDPAATDML 221
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531  177 GISPLMLASMNGHREATRV--LLEKGSDINAqieTNRN--TALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPL 248
Cdd:PHA03095  222 GNTPLHSMATGSSCKRSLVlpLLIAGISINA---RNRYgqTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
115-379 1.38e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.11  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  115 LACSGGRKDVVELLLAHGANKEHRNVSDYTPLSLASSGGYI-----EIVNMLLTAGSEINSrtGSKLGISPLMLASMNgh 189
Cdd:PHA03100   41 LAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNA--PDNNGITPLLYAISK-- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  190 reatrvllEKGSdinaqietnrntaltlasfqgrTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVD--VGNLLIAAG 267
Cdd:PHA03100  117 --------KSNS----------------------YSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  268 ADTNAspvqqtKDTaltisaekghekfVRMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALLEKGADPDMFDNRKIS 347
Cdd:PHA03100  167 VDINA------KNR-------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 193206531  348 PMMAAFRKGHVEIVKYMVNSAkqfPNEQDLIR 379
Cdd:PHA03100  228 PLHIAILNNNKEIFKLLLNNG---PSIKTIIE 256
PHA03095 PHA03095
ankyrin-like protein; Provisional
56-328 1.58e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.47  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   56 DIVELLLKEGANIEHRDKKGFSPLiiaATAGHSS------VVEVLLKNHAAIEAQsDRTKDTAL-SLACSGGRKDVVELL 128
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPL---HLYLHYSsekvkdIVRLLLEAGADVNAP-ERCGFTPLhLYLYNATTLDVIKLL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  129 LAHGANKEHRNVSDYTPLSLASSGGYI--EIVNMLLTAGSEINSRtgSKLGISPL--MLASMNGHREATRVLLEKGSDIN 204
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNAL--DLYGMTPLavLLKSRNANVELLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  205 AqIETNRNTALT--LASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNL--LIAAGADTNAspVQQTKD 280
Cdd:PHA03095  182 A-VDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA--RNRYGQ 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193206531  281 TALTISAEKGHEKFVRMLLNGDAAVDVRNKKGCTALWLA---CNGGYLSTA 328
Cdd:PHA03095  259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMvrnNNGRAVRAA 309
KH-I_MASK cd22404
type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family ...
616-686 1.30e-17

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: 78.41  E-value: 1.30e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193206531  616 SWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKiqESNKQAERTVLAKGTPEMVRYAMNIINYMIYD 686
Cdd:cd22404     2 SKKVTVPNSAISRVIGRGGCNINAIREVSGAHIEIDK--QKGEQGDRRITIKGSADATRQAAQLINALIKD 70
Ank_2 pfam12796
Ankyrin repeats (3 copies);
113-206 1.08e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 1.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   113 LSLACSGGRKDVVELLLAHGANKEHRNVSDYTPLSLASSGGYIEIVNMLLtagSEINSRTGSKlGISPLMLASMNGHREA 192
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKDN-GRTALHYAARSGHLEI 76
                           90
                   ....*....|....
gi 193206531   193 TRVLLEKGSDINAQ 206
Cdd:pfam12796   77 VKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
49-248 9.09e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 9.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   49 ACANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAaieaqsdrtkDTALsLACSGGRKDVVELL 128
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGV----------DTSI-LPIPCIEKDMIKTI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  129 LAHGANKEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRTGSklGISPLMLASMNGHREATRVLLEKGSDINAQiE 208
Cdd:PHA02874  111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN--GCYPIHIAIKHNFFDIIKLLLEKGAYANVK-D 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 193206531  209 TNRNTALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPL 248
Cdd:PHA02874  188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
283-376 9.98e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 9.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   283 LTISAEKGHEKFVRMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALLEKgADPDMFDNRKiSPMMAAFRKGHVEIVK 362
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
                           90
                   ....*....|....
gi 193206531   363 YMVNSAKQfPNEQD 376
Cdd:pfam12796   79 LLLEKGAD-INVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
49-353 2.70e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 2.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   49 ACANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAAIEAQSdrtkdtaLSLACSGGRKDVVELL 128
Cdd:PHA02876  185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND-------LSLLKAIRNEDLETSL 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  129 LAHGANKEHRNVSDY--TPLSLASSGGYI-EIVNMLLTAGSEINSRTGSklGISPLMLASMNGH-REATRVLLEKGSDIN 204
Cdd:PHA02876  258 LLYDAGFSVNSIDDCknTPLHHASQAPSLsRLVPKLLERGADVNAKNIK--GETPLYLMAKNGYdTENIRTLIMLGADVN 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  205 AQiETNRNTALTLASFQGR-TEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLIAAGADTNAspVQQTKDTAL 283
Cdd:PHA02876  336 AA-DRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA--LSQKIGTAL 412
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206531  284 TIsAEKGHEKF--VRMLLNGDAAVDVRNKKGCTALWLAC-NGGYLSTAQALLEKGADPDMFDNRKISPMMAAF 353
Cdd:PHA02876  413 HF-ALCGTNPYmsVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL 484
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-376 2.91e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.99  E-value: 2.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  225 EVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLIAAGADTNASPvqQTKDTALTISAEKGHEKFVRMLLNGDAA 304
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALAD--ALGALLLLAAALAGDLLVALLLLAAGAD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206531  305 VDVRNKKGCTALWLACNGGYLSTAQALLEKGADPDMFDNRKISPMMAAFRKGHVEIVKYMVNS-AKqfPNEQD 376
Cdd:COG0666    80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgAD--VNAQD 150
PHA03095 PHA03095
ankyrin-like protein; Provisional
52-243 1.07e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.45  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   52 NGHKDIVELLLKEGANIEHRDKKGFSPLiiaataghssvvEVLLKNHAA--------IEAQSD-RTKD----TAL-SLAC 117
Cdd:PHA03095  129 NINPKVIRLLLRKGADVNALDLYGMTPL------------AVLLKSRNAnvellrllIDAGADvYAVDdrfrSLLhHHLQ 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  118 S-GGRKDVVELLLAHGANKEHRNVSDYTPL-SLA--SSGGYIEIVNmLLTAGSEINSRtgSKLGISPLMLASMNGHREAT 193
Cdd:PHA03095  197 SfKPRARIVRELIRAGCDPAATDMLGNTPLhSMAtgSSCKRSLVLP-LLIAGISINAR--NRYGQTPLHYAAVFNNPRAC 273
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 193206531  194 RVLLEKGSDINAQIETNrNTALTLASFQGRTEVVKLLLAYNANVEHRAKT 243
Cdd:PHA03095  274 RRLIALGADINAVSSDG-NTPLSLMVRNNNGRAVRAALAKNPSAETVAAT 322
Ank_2 pfam12796
Ankyrin repeats (3 copies);
215-309 4.37e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 4.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   215 LTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLIaAGADTNaspVQQTKDTALTISAEKGHEKF 294
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVN---LKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 193206531   295 VRMLLNGDAAVDVRN 309
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
56-355 4.75e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.38  E-value: 4.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   56 DIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLknhAAIEAQSDRTKDTALSLACSGGRKDVVELLLAHGANK 135
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKN 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  136 EHrnVSDYTPLSLASSGGYIE--IVNMLLTAGSEINSRTGSKLGiSPLMLASMNGHREATRVLLEKGSDINAQIETNrNT 213
Cdd:PHA02878  128 IQ--TIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTN-NS 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  214 ALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMecASGGYV---DVGNLLIAAGADTNAspvqqtKDTALtisaekg 290
Cdd:PHA02878  204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH--ISVGYCkdyDILKLLLEHGVDVNA------KSYIL------- 268
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206531  291 hekfvrmllngdaavdvrnkkGCTALWLACNGGylSTAQALLEKGADPDMFDNRKISPMMAAFRK 355
Cdd:PHA02878  269 ---------------------GLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
616-686 1.05e-12

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: 64.39  E-value: 1.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193206531  616 SWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKiqESNKQAERTVLAKGTPEMVRYAMNIINYMIYD 686
Cdd:cd22502     2 SKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDK--QKDKTGDRIITIRGGTESTRQATQLINALIKD 70
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
56-239 1.57e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.21  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   56 DIVELLLKEGAniEHRDKKGFSPLIIAATAGHSSVVEVLLKnhAAIEAQ-SDRTKDTALSLACSGGRKDVVELLLAHGAN 134
Cdd:PLN03192  508 NVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLK--AKLDPDiGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  135 KEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRTGSKLgispLMLASMNGHREATRVLLEKGSDINAQiETNRNTA 214
Cdd:PLN03192  584 VHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSE-DHQGATA 658
                         170       180
                  ....*....|....*....|....*
gi 193206531  215 LTLASFQGRTEVVKLLLAYNANVEH 239
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02875 PHA02875
ankyrin repeat protein; Provisional
112-404 2.80e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.41  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  112 ALSLACSGGRKDVVELLLAHGANKEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRTGsklGI-SPLMLASMNGHR 190
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIeSELHDAVEEGDV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  191 EATRVLLEKGSDINAQIETNRNTALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLIAAGADT 270
Cdd:PHA02875   82 KAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  271 NaspvqqTKD----TALTISAEKGHEKFVRMLLNGDAAVDVRNKKGC-TALWLACNGGYLSTAQALLEKGADP------- 338
Cdd:PHA02875  162 D------IEDccgcTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCnimfmie 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206531  339 -------DMFDNRKISPMMAAFRKGHVEIV----KYMVNSAKQFPNEQDLIraQQTAETDDIKKKCGECIDIIRSAK 404
Cdd:PHA02875  236 geectilDMICNMCTNLESEAIDALIADIAirihKKTIRRDEGFKNNMSTI--EDKEEFKDVFEKCIIELRRIKSEK 310
KH-I_ANKHD1 cd22503
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ...
616-695 4.06e-12

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: 63.23  E-value: 4.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  616 SWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKiqESNKQAERTVLAKGTPEMVRYAMNIINYMIYDADVLVTDAI 695
Cdd:cd22503     2 SKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDK--QKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLI 79
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
616-681 7.51e-12

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: 61.91  E-value: 7.51e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531   616 SWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEInkIQESNKQAERTVLAKGTPEMVRYAMNIIN 681
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQI--PPSESEGNERIVTITGTPEAVEAAKALIE 64
PHA02876 PHA02876
ankyrin repeat protein; Provisional
57-275 4.48e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.40  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   57 IVELLLKEGANIEHRDKKGFSPLIIAATAGHSSV-VEVLLKNHAAIEAqSDRTKDTALSLACSGGR-KDVVELLLAHGAN 134
Cdd:PHA02876  289 LVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNA-ADRLYITPLHQASTLDRnKDIVITLLELGAN 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  135 KEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINS---RTGSKL-----GISPLMlasmnghreATRVLLEKGSDINAQ 206
Cdd:PHA02876  368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAlsqKIGTALhfalcGTNPYM---------SVKTLIDRGANVNSK 438
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  207 iETNRNTALTLASFQG-RTEVVKLLLAYNANVEHRAKTGLTPLMecASGGYVDVGNLLIAAGADTNASPV 275
Cdd:PHA02876  439 -NKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLL--IALEYHGIVNILLHYGAELRDSRV 505
KH smart00322
K homology RNA-binding domain;
618-684 2.51e-10

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 57.69  E-value: 2.51e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206531    618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESnkqaERTVLAKGTPEMVRYAMNIINYMI 684
Cdd:smart00322    6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSE----ERVVEITGPPENVEKAAELILEIL 68
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
618-681 2.97e-10

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: 57.31  E-value: 2.97e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKiqESNKQAERTVLAKGTPEMVRYAMNIIN 681
Cdd:cd00105     2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPK--EGEGSGERVVTITGTPEAVEKAKELIE 63
PHA03095 PHA03095
ankyrin-like protein; Provisional
225-366 5.51e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 5.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  225 EVVKLLLAYNANVEHR---AKTGLTPLMECASGGYVDVGNLLIAAGADTNAspVQQTKDTALTISAEKGH-EKFVRMLLN 300
Cdd:PHA03095   28 EEVRRLLAAGADVNFRgeyGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNA--PERCGFTPLHLYLYNATtLDVIKLLIK 105
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531  301 GDAAVDVRNKKGCTALWLacnggYLS-------TAQALLEKGADPDMFDNRKISPmMAAFRKGH---VEIVKYMVN 366
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHV-----YLSgfninpkVIRLLLRKGADVNALDLYGMTP-LAVLLKSRnanVELLRLLID 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
49-218 1.55e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   49 ACANGHKDIVELLLKEGANIEHRDKKGFSPLiiaataghssvvevllknHAAIeaqsdrtkdtalslacSGGRKDVVELL 128
Cdd:PHA02878  175 ATENKDQRLTELLLSYGANVNIPDKTNNSPL------------------HHAV----------------KHYNKPIVHIL 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  129 LAHGANKEHRNVSDYTPLSLASsgGY---IEIVNMLLTAGSEINSRTgSKLGISPLMLASMNghREATRVLLEKGSDINA 205
Cdd:PHA02878  221 LENGASTDARDKCGNTPLHISV--GYckdYDILKLLLEHGVDVNAKS-YILGLTALHSSIKS--ERKLKLLLEYGADINS 295
                         170
                  ....*....|...
gi 193206531  206 qIETNRNTALTLA 218
Cdd:PHA02878  296 -LNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
58-232 2.49e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   58 VELLLKEGANIEhrD---KKGFSPLIIAATAGHSSVVEVLLKNHAAIEAQS-DRTkdTALSLACSGGRKDVVELLLAHGA 133
Cdd:PHA02875   84 VEELLDLGKFAD--DvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNtDKF--SPLHLAVMMGDIKGIELLIDHKA 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  134 NKEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEIN--SRTGSklgISPLMLASMNGHREATRVLLEKGSDIN--AQIET 209
Cdd:PHA02875  160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyfGKNGC---VAALCYAIENNKIDIVRLFIKRGADCNimFMIEG 236
                         170       180
                  ....*....|....*....|....*.
gi 193206531  210 NRNTALTLAS---FQGRTEVVKLLLA 232
Cdd:PHA02875  237 EECTILDMICnmcTNLESEAIDALIA 262
KH-I_NOVA_rpt1 cd22435
first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
618-685 1.54e-08

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: 52.54  E-value: 1.54e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKiqesNKQ-----AERTVLAKGTPEMVRYAMNIINYMIY 685
Cdd:cd22435     5 KLLVPNYAAGSIIGKGGQTIAQLQKETGARIKLSK----NNDfypgtTERVCLIQGEVEAVNAVLDFILEKIR 73
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
48-191 2.18e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   48 IACANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLlknHAAIEAQSDRTKDTALSLACSGGRKDVVEL 127
Cdd:PLN03192  564 IAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL---YHFASISDPHAAGDLLCTAAKRNDLTAMKE 640
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193206531  128 LLAHGANKEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINsRTGSKLGISPLMLASMNGHRE 191
Cdd:PLN03192  641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD-KANTDDDFSPTELRELLQKRE 703
KH-I_NOVA_rpt2 cd22436
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
618-684 3.24e-08

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


Pssm-ID: 411864 [Multi-domain]  Cd Length: 70  Bit Score: 51.85  E-value: 3.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKQAERTVLAKGTPEMVRYAMNIINYMI 684
Cdd:cd22436     4 KILVPNSTAGMIIGKGGATIKAIMEQSGARVQISQKPESINLQERVVTVTGEPEANRKAVSLILQKI 70
PHA02876 PHA02876
ankyrin repeat protein; Provisional
124-372 3.70e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.15  E-value: 3.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  124 VVELLLAHGANKEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRTGSKLGI------------------------- 178
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVlecavdsknidtikaiidnrsnink 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  179 --SPLMLASMNGHREATRVLLEKGSDINAqIETNRNTALTLAS-FQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGG 255
Cdd:PHA02876  240 ndLSLLKAIRNEDLETSLLLYDAGFSVNS-IDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  256 YvDVGNL--LIAAGADTNA------SPVQQT------KDTALT-------ISAEKGHEK-------------FVRMLLNG 301
Cdd:PHA02876  319 Y-DTENIrtLIMLGADVNAadrlyiTPLHQAstldrnKDIVITllelganVNARDYCDKtpihyaavrnnvvIINTLLDY 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  302 DAAVDVRNKKGCTALWLA-CNGGYLSTAQALLEKGADPDMFDNRKISPMMAAFRKG-HVEIVKYM---------VNSAKQ 370
Cdd:PHA02876  398 GADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLldngadvnaINIQNQ 477

                  ..
gi 193206531  371 FP 372
Cdd:PHA02876  478 YP 479
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
615-681 3.82e-08

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: 51.46  E-value: 3.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206531  615 SSWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNkqAERTVLAKGTPEMVRYAMNIIN 681
Cdd:cd22439     2 TTQEITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEDGS--TERSVTITGTPEAVSLAQYLIN 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
49-95 4.35e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 4.35e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 193206531    49 ACANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLL 95
Cdd:pfam13637    8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
194-374 7.41e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.51  E-value: 7.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  194 RVLLEKGSDINAQIETNrNTALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLIAAGADTNAS 273
Cdd:PHA02874   19 KIIKNKGNCINISVDET-TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  274 PVQQ-TKDTALTI--------------------SAEKGHEKFVRMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALL 332
Cdd:PHA02874   98 PIPCiEKDMIKTIldcgidvnikdaelktflhyAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 193206531  333 EKGADPDMFDNRKISPMMAAFRKGHVEIVKYMVNSAKQFPNE 374
Cdd:PHA02874  178 EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK 219
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
148-250 8.51e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 8.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  148 LASSGGYIEIvNMLLTAGSEINSRTGSklGISPLMLASMNGHREATRVLLEKGSDINAqIETNRNTALTLASFQGRTEVV 227
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCRDYD--GRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVV 164
                          90       100       110
                  ....*....|....*....|....*....|
gi 193206531  228 KLLLAY---NANVEHRAK----TGLTPLME 250
Cdd:PTZ00322  165 QLLSRHsqcHFELGANAKpdsfTGKPPSLE 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
314-365 2.26e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.26e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 193206531   314 TALWLACNGGYLSTAQALLEKGADPDMFDNRKISPMMAAFRKGHVEIVKYMV 365
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
51-131 2.76e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   51 ANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAAIEAqSDRTKDTALSLACSGGRKDVVELLLA 130
Cdd:PTZ00322   91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLSR 169

                  .
gi 193206531  131 H 131
Cdd:PTZ00322  170 H 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
179-231 3.41e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 3.41e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 193206531   179 SPLMLASMNGHREATRVLLEKGSDINAQIEtNRNTALTLASFQGRTEVVKLLL 231
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
54-203 4.38e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.68  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   54 HKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAAIEAQSDRTkDTALSLACSGGRKDV-VELLLAHG 132
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKI-GTALHFALCGTNPYMsVKTLIDRG 432
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206531  133 ANKEHRNVSDYTPLSLASSGG-YIEIVNMLLTAGSEINSrtgskLGIS---PLMLASmnGHREATRVLLEKGSDI 203
Cdd:PHA02876  433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA-----INIQnqyPLLIAL--EYHGIVNILLHYGAEL 500
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
621-684 4.99e-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: 48.40  E-value: 4.99e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193206531  621 IPAYAASRVIGKGGSNVNAVREATGAIIEINkiQESNKQAERTVLAKGTPEMVRYAMNIINYMI 684
Cdd:cd22396     7 VPDKMVGLIIGRGGEQINRLQAESGAKIQIA--PDSGGLPERPCTLTGTPDAIETAKRLIDQIV 68
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
265-362 9.42e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 9.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  265 AAGADTNASP---VQQTKDTALTIS----AEKGHEKFVRMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALLEKGAD 337
Cdd:PTZ00322   61 DATPDHNLTTeevIDPVVAHMLTVElcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140
                          90       100
                  ....*....|....*....|....*
gi 193206531  338 PDMFDNRKISPMMAAFRKGHVEIVK 362
Cdd:PTZ00322  141 PTLLDKDGKTPLELAEENGFREVVQ 165
PHA02989 PHA02989
ankyrin repeat protein; Provisional
123-248 1.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 53.21  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  123 DVVELLLAHGANKEHRNVSDyTPL------SLASSGGYIEIVNMLLTAGSEINSRTGSklGISPLMLASMNGH---REAT 193
Cdd:PHA02989   51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFN--GVSPIVCFIYNSNinnCDML 127
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 193206531  194 RVLLEKGSDINAQIETNRNTAL--TLASFQGRTEVVKLLLAYNANV-EHRAKTGLTPL 248
Cdd:PHA02989  128 RFLLSKGINVNDVKNSRGYNLLhmYLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPM 185
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-162 1.19e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 193206531   111 TALSLACSGGRKDVVELLLAHGANKEHRNVSDYTPLSLASSGGYIEIVNMLL 162
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
60-116 2.27e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 2.27e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 193206531    60 LLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAAIEAQSDRTKdTALSLA 116
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
628-680 2.36e-06

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


Pssm-ID: 411829 [Multi-domain]  Cd Length: 72  Bit Score: 46.45  E-value: 2.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 193206531  628 RVIGKGGSNVNAVREATGAIIEINKIQE-SNKQAERTVLAKGTPEMVRYAMNII 680
Cdd:cd22401    13 RLIGKDGRNIKKIMEDTNTKITISSLQDlTSYNPERTITIKGSLEAMSEAESLI 66
KH-I_IGF2BP_rpt4 cd22403
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
619-669 2.90e-06

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: 46.08  E-value: 2.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193206531  619 LTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKQAERTVLAKGT 669
Cdd:cd22403     4 IRVPSSMVGRIIGKGGQNVRELQRLTGAIIKLPRDQTPDEGDEVPVEIIGN 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
48-134 5.18e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 5.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   48 IACANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAAIEAQSDRTKDTALSLACSGGRKDVVEL 127
Cdd:PHA02875  141 LAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRL 220

                  ....*..
gi 193206531  128 LLAHGAN 134
Cdd:PHA02875  221 FIKRGAD 227
KH-I_PCBP3_rpt3 cd22522
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
602-681 1.71e-05

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


Pssm-ID: 411950 [Multi-domain]  Cd Length: 75  Bit Score: 44.33  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  602 DQTPPyeidtrnESSWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNkqAERTVLAKGTPEMVRYAMNIIN 681
Cdd:cd22522     3 DASPP-------ASTHELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGS--SERQITITGSPANISLAQYLIN 73
KH-I_MER1_like cd22458
type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic ...
617-680 1.94e-05

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: 43.59  E-value: 1.94e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193206531  617 WKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESnkqAERTVLAKGTPEMVRYAMNII 680
Cdd:cd22458     3 WEIKLPQALCGRLIGAKGKNIKALSEKSGASIRLIPISNS---SQQTIHLSGTDKQIALAISSI 63
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
48-162 2.05e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   48 IACANGHKDIVELLLKEGANIE---------HRDKK-----GFSPLIIAATAGHSSVVEVLLKNHAAIEAQsDRTKDTAL 113
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLGNTVL 173
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193206531  114 ---------SLACsggrkDVVELLLAHGANK-----EH-RNVSDYTPLSLASSGGYIEIVNMLL 162
Cdd:cd22192   174 hilvlqpnkTFAC-----QMYDLILSYDKEDdlqplDLvPNNQGLTPFKLAAKEGNIVMFQHLV 232
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
627-681 3.42e-05

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: 43.08  E-value: 3.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193206531  627 SRVIGKGGSNVNAVREATGAIIEINKiqeSNKQAERTVLaKGTPEMVRYAMNIIN 681
Cdd:cd22452    14 GRIIGPGGSNINQIREKSGCFINVPK---KNKESDVITL-RGTKEGVEKAEEMIK 64
Ank_4 pfam13637
Ankyrin repeats (many copies);
211-264 3.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 3.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 193206531   211 RNTALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLI 264
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_PCBP4_rpt2 cd22520
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
618-673 4.20e-05

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: 43.09  E-value: 4.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNkQAERTVLAKGTPEMV 673
Cdd:cd22520     5 RLVIPASQCGSLIGKAGSKIKEIRESTGAQVQVAGDLLPN-STERAVTVSGVPDAI 59
KH-I_FUBP_rpt4 cd22399
fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
620-681 4.34e-05

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: 42.60  E-value: 4.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193206531  620 TIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKQaERTVLAKGTPEMVRYAMNIIN 681
Cdd:cd22399     5 LVPANKCGLVIGKGGETIRQINQQSGAHVELDRNPPPNPN-EKLFIIRGNPQQIEHAKQLIR 65
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
618-680 4.79e-05

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: 42.99  E-value: 4.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEI---NKIQESNKQAERTVLAKGTPEMVRYAMNII 680
Cdd:cd22460     3 RLLVASSQAGSLIGKGGAIIKQIREESGASVRIlpeEELPPCASPDDRVVQISGEAQAVKKALELV 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-129 4.94e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 4.94e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 193206531    77 SPLIIAATAGHSSVVEVLLKNHAAIEAQsDRTKDTALSLACSGGRKDVVELLL 129
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
77-248 5.24e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.70  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   77 SPLIIAATAGHSSVVEVLLKNHAAIEAQSDRTKDTALSLACSGGRKDVVELLLAhgANKEHRNV---SDY----TPLSLA 149
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtSDLyqgeTALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  150 SSGGYIEIVNMLLTAGSEINS--------RTGSK----LGISPLMLASMNGHREATRVLLEKGSDINAQiETNRNTALTL 217
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSpratgtffRPGPKnliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLGNTVLHI 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 193206531  218 ASFQGRTEVVK----LLLAYNAN-----VEH-RAKTGLTPL 248
Cdd:cd22192   176 LVLQPNKTFACqmydLILSYDKEddlqpLDLvPNNQGLTPF 216
KH-I_TDRKH_rpt2 cd22429
second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
619-680 6.93e-05

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: 42.71  E-value: 6.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193206531  619 LTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKQAERTVLAKGTPEMVRYAMNII 680
Cdd:cd22429     6 LHVPQRAVGRIIGRGGETIRSICRTSGAKVKCDRESDDTLDLVRLITITGTKKEVDAAKSLI 67
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
618-673 7.23e-05

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: 42.26  E-value: 7.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEI--NKIQESnkqAERTVLAKGTPEMV 673
Cdd:cd02396     5 RLLVPASQCGSLIGKGGSKIKEIRESTGASVQVasEMLPNS---TERAVTISGSPEAI 59
PHA02875 PHA02875
ankyrin repeat protein; Provisional
210-366 1.15e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  210 NRNTALTLASFQGRTEVVKLLL--AYNANVEhrAKTGLTPLMECASGGYVDVGNLLIAAGA--DTNASPVQqtkdTALTI 285
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLdiGINPNFE--IYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE----SELHD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  286 SAEKGHEKFVRMLLN-GDAAVDVRNKKGCTALWLACNGGYLSTAQALLEKGADPDMFDNRKISPMMAAFRKGHVEIVKYM 364
Cdd:PHA02875   75 AVEEGDVKAVEELLDlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                  ..
gi 193206531  365 VN 366
Cdd:PHA02875  155 ID 156
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
619-660 1.32e-04

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: 41.63  E-value: 1.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 193206531  619 LTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKQA 660
Cdd:cd22447     8 VPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPA 49
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
618-684 1.33e-04

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: 41.49  E-value: 1.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINkiqesNKQAERTVLAKGTPEMVRYAMNIINYMI 684
Cdd:cd22449     7 KFDVPAKYVPHIIGKKGANINKLREEYGVKIDFE-----DKTGEGNVEIKGSKKNVEEAKKRILSQI 68
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
144-371 1.43e-04

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: 46.16  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  144 TPLSLASSGGYIEIVNMLLTAGSEINSRTGSkLGISPLMLASMNGHREATRVLLEKGSD-INAQIETNR---NTALTLAS 219
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGA-LGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDLyqgETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  220 FQGRTEVVKLLLAYNANVEHRAKTG----LTPLMECASGGYVdvgnlliaagadtnaspvqqtkdtaLTISAEKGHEKFV 295
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGtffrPGPKNLIYYGEHP-------------------------LSFAACVGNEEIV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  296 RMLLNGDAAVDVRNKKGCTALW---------LACNGGYLSTAQALLEKGADPDMFDNRK-ISPMMAAFRKGHVEIVKYMV 365
Cdd:cd22192   153 RLLIEHGADIRAQDSLGNTVLHilvlqpnktFACQMYDLILSYDKEDDLQPLDLVPNNQgLTPFKLAAKEGNIVMFQHLV 232

                  ....*.
gi 193206531  366 NSAKQF 371
Cdd:cd22192   233 QKRRHI 238
KH-I_IGF2BP_rpt3 cd22402
third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
619-671 1.44e-04

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: 41.08  E-value: 1.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 193206531  619 LTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIqESNKQAERTVLAKGTPE 671
Cdd:cd22402     5 LYIPNKAVGAIIGTKGSHIRYIKRFSGASIKIAPA-DSPDAPERKVTITGPPE 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
49-103 1.50e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 1.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193206531   49 ACANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAAIEA 103
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
179-339 1.53e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  179 SPLMLASMNGHREATRVLLEKGSDINAQIETNRnTALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVD 258
Cdd:PLN03192  527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  259 VGNLLIAAGADTNAspvqQTKDTALTISAEKGHEKFVRMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALLEKGADP 338
Cdd:PLN03192  606 IFRILYHFASISDP----HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681

                  .
gi 193206531  339 D 339
Cdd:PLN03192  682 D 682
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
621-684 1.57e-04

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: 41.55  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193206531  621 IPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKQAERTVLAKGTPEMVRYAMNIINYMI 684
Cdd:cd22428    11 VPREAVGLIIGRQGATIKQIQKETGARIDFKDEGSGGELPERVLLIQGNPVQAQRAEEAIHQII 74
KH-I_PCBP3_rpt2 cd22519
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
618-673 1.57e-04

second 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 second one.


Pssm-ID: 411947 [Multi-domain]  Cd Length: 79  Bit Score: 41.70  E-value: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNkQAERTVLAKGTPEMV 673
Cdd:cd22519     9 RLVVPASQCGSLIGKGGSKIKEIRESTGAQVQVAGDMLPN-STERAVTISGTPDAI 63
KH-I_FUBP2_rpt4 cd22488
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
619-680 1.59e-04

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: 41.24  E-value: 1.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206531  619 LTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKQAE-RTVLAKGTPEMVRYAMNII 680
Cdd:cd22488     4 FSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQPPPNGDPNfKLFIIRGSPQQIDHAKQLI 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
244-299 1.69e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.69e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531   244 GLTPLMECASGGYVDVGNLLIAAGADTNASPVQQtkDTALTISAEKGHEKFVRMLL 299
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNG--ETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
281-332 1.84e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 193206531   281 TALTISAEKGHEKFVRMLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALL 332
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
620-676 1.87e-04

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: 41.15  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 193206531  620 TIPAYAASRVIGKGGSNVNAVREATGAIIeinKIQESNK-QAERTVLAKGTPEMVRYA 676
Cdd:cd22434     7 TIPKDLAGSIIGKGGQRIRQIRHESGASI---KIDEPLPgSEDRIITITGTQDQIQNA 61
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
618-685 2.14e-04

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: 40.91  E-value: 2.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKiQESNKQAERTVLAKGTPEMVRYAMniinYMIY 685
Cdd:cd22457     2 NISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAK-APHDETGERMFTITGTPEANDRAL----RLLY 64
Ank_5 pfam13857
Ankyrin repeats (many copies);
128-184 3.46e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 3.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 193206531   128 LLAHG-ANKEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRTGSklGISPLMLA 184
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE--GLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
56-204 3.52e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   56 DIVELLLKEGANIEHRDKKGFSPLIiaataghssvveVLLKNhaaieaqsdrTKDTALSLacsggrkDVVELLLAHGANK 135
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLC------------TILSN----------IKDYKHML-------DIVKILIENGADI 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206531  136 EHRNVSDYTPLSLASSGGYI---EIVNMLLTAGSEINSRtgSKLGISPLMLASMNGHR---EATRVLLEKGSDIN 204
Cdd:PHA02798  103 NKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLL--DKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDIN 175
KH-I_BTR1_rpt1 cd22513
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ...
615-680 4.39e-04

first 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 first one.


Pssm-ID: 411941 [Multi-domain]  Cd Length: 73  Bit Score: 40.11  E-value: 4.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206531  615 SSWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQES-NKQAERTVLAKGTPEMVRYAMNII 680
Cdd:cd22513     2 VVAKLLVSNAAAGSVIGKGGATINDFQAQSGARIQLSRAQEFfPGTTDRVLLVSGSLNEVLTALNLI 68
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
177-205 5.11e-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: 38.78  E-value: 5.11e-04
                           10        20
                   ....*....|....*....|....*....
gi 193206531   177 GISPLMLASMNGHREATRVLLEKGSDINA 205
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
616-680 5.15e-04

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: 39.81  E-value: 5.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206531  616 SWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESnkQAERTVLAKGTPEMVRYAMNII 680
Cdd:cd22395     1 VYEFEVPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYT--QNFQICSIEGTQQQIDKALKLI 63
Ank_5 pfam13857
Ankyrin repeats (many copies);
161-218 5.24e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 5.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 193206531   161 LLTAGSeINSRTGSKLGISPLMLASMNGHREATRVLLEKGSDINAQiETNRNTALTLA 218
Cdd:pfam13857    1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK-DEEGLTALDLA 56
KH-I_FUBP3_rpt4 cd22489
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
620-681 5.32e-04

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: 39.91  E-value: 5.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206531  620 TIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKQAE-RTVLAKGTPEMVRYAMNIIN 681
Cdd:cd22489     5 TIPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNTDPNvRIFTIRGVPQQIEHARQLID 67
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
311-343 6.56e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 6.56e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 193206531   311 KGCTALWLAC-NGGYLSTAQALLEKGADPDMFDN 343
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
KH-I_IGF2BP_rpt1 cd22400
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
618-671 7.43e-04

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: 39.18  E-value: 7.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKiQESNKQAERTVLAKGTPE 671
Cdd:cd22400     3 RILVPSEFVGAIIGKGGATIRQITQQTGARIDIHR-KENAGAAEKAITIYGTPE 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
297-349 7.61e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 7.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 193206531   297 MLLNGDAAVDVRNKKGCTALWLACNGGYLSTAQALLEKGADPDMFDNRKISPM 349
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
612-684 7.72e-04

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: 39.22  E-value: 7.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206531  612 RNESSWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKqaERTVLAKGTPEMVRYAMNIINYMI 684
Cdd:cd22454     1 TGQTTIEVVIPNADVGKVIGKGGETIKRIEALTDTVITFERVNGGSP--NREVQITGSPDNVAAAKRLIEDTI 71
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
177-205 8.59e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 8.59e-04
                            10        20
                    ....*....|....*....|....*....
gi 193206531    177 GISPLMLASMNGHREATRVLLEKGSDINA 205
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
281-365 1.13e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  281 TALTISAEKGHEKFVRMLLNGDAAVDVRNKKGCTALW-------------------------------LACNGGYLSTAQ 329
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWnaisakhhkifrilyhfasisdphaagdllcTAAKRNDLTAMK 639
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 193206531  330 ALLEKGADPDMFDNRKISPMMAAFRKGHVEIVKYMV 365
Cdd:PLN03192  640 ELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
Ank_5 pfam13857
Ankyrin repeats (many copies);
94-149 1.20e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531    94 LLKNHAAIEAQSDRTKDTALSLACSGGRKDVVELLLAHGANKEHRNVSDYTPLSLA 149
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
617-683 1.22e-03

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: 38.74  E-value: 1.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193206531  617 WKLTIPAYAASRVIGKGGSNVNAVREATGAIIEI-NKIQESNKQAERTVLAKGTPE-MVRYAMNIINYM 683
Cdd:cd22437     1 VRLLVPNSSCGLIIGKGGSTIKELREDSNANIKIsPKDQLLPGSSERIVTITGSFDqVVKAVALILEKL 69
PHA02989 PHA02989
ankyrin repeat protein; Provisional
192-365 1.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.81  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  192 ATRVLLEKGSDINAQIETNRNTALTLASFQGRTEVVKLLLAYNANVEHRA--KTGLTPLM---ECASGGYVDVGNLLIAA 266
Cdd:PHA02989   18 ALEFLLRTGFDVNEEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGyiETPLCAVLrnrEITSNKIKKIVKLLLKF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  267 GADTNASPVQQTKDTALTI--SAEKGHEKFVRMLLNGDAAVDVRNKKGCTALWLACNGGYLST--AQALLEKGADPDMFD 342
Cdd:PHA02989   98 GADINLKTFNGVSPIVCFIynSNINNCDMLRFLLSKGINVNDVKNSRGYNLLHMYLESFSVKKdvIKILLSFGVNLFEKT 177
                         170       180
                  ....*....|....*....|....*...
gi 193206531  343 NRK-ISPMMAAFRKG----HVEIVKYMV 365
Cdd:PHA02989  178 SLYgLTPMNIYLRNDidviSIKVIKYLI 205
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
48-96 1.45e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 193206531   48 IACANGHKDIVELLLKEGANIEHRDKKGFSPLIIAATAGHSSVVEVLLK 96
Cdd:PTZ00322  121 IACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
618-652 1.49e-03

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: 38.36  E-value: 1.49e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEINK 652
Cdd:cd22459     5 RLLCPVSKAGSVIGKGGEIIKQLRQETGARIKVED 39
KH-I_PCBP_rpt1 cd22438
first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
626-680 1.71e-03

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: 38.39  E-value: 1.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193206531  626 ASRVIGKGGSNVNAVREATGAIIEINkiqeSNKQAERTVLAKGTPEMVRYAMNII 680
Cdd:cd22438    10 VGSIIGKKGETIKKFREESGARINIS----DGSCPERIVTVTGTTDAVFKAFELI 60
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
618-651 1.89e-03

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: 38.23  E-value: 1.89e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 193206531  618 KLTIPAYAASRVIGKGGSNVNAVREATGAIIEIN 651
Cdd:cd02393     7 TIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIE 40
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
185-274 1.99e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  185 SMNGHREATRVLLEKGSDINAQiETNRNTALTLASFQGRTEVVKLLLAYNANVEHRAKTGLTPLMECASGGYVDVGNLLI 264
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
                          90
                  ....*....|....*
gi 193206531  265 A-----AGADTNASP 274
Cdd:PTZ00322  169 RhsqchFELGANAKP 183
KH-I_PEPPER_like_rpt3 cd22461
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
616-683 2.28e-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: 37.92  E-value: 2.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193206531  616 SWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKqaERTVLAKGTPEMVRYAMNII-NYM 683
Cdd:cd22461     3 SQQMQIPLSYADAIIGTAGANISYIRRTSGATITIQETRGAPG--EMTVEIHGTQSQVQTAQQLIqNFM 69
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
618-650 2.86e-03

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


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 37.55  E-value: 2.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 193206531  618 KLTI-PAYAASrVIGKGGSNVNAVREATGAIIEI 650
Cdd:cd02394     5 TIEIdPKFHGH-IIGKGGANIKRIREESGVSIRI 37
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
49-73 3.26e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 3.26e-03
                           10        20
                   ....*....|....*....|....*
gi 193206531    49 ACANGHKDIVELLLKEGANIEHRDK 73
Cdd:pfam00023   10 AGRRGNLEIVKLLLSKGADVNARDK 34
KH-I_PCBP1_2_rpt2 cd22518
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
611-673 3.52e-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: 3.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206531  611 TRNESSWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNkQAERTVLAKGTPEMV 673
Cdd:cd22518     3 SRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPN-STERAITIAGIPQSI 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
83-162 3.73e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   83 ATAGHSSVVEVLLKNHAAIEAQsDRTKDTALSLACSGGRKDVVELLLAHGANKEHRNVSDYTPLSLASSGGYIEIVNMLL 162
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCR-DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
177-206 3.74e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.74e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 193206531   177 GISPLMLAS-MNGHREATRVLLEKGSDINAQ 206
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
311-340 4.35e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 4.35e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 193206531    311 KGCTALWLACNGGYLSTAQALLEKGADPDM 340
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
115-197 4.46e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531  115 LACSGgrkDVV--ELLLAHGANKEHRNVSDYTPLSLASSGGYIEIVNMLLTAGSEINSRtgSKLGISPLMLASMNGHREA 192
Cdd:PTZ00322   89 LAASG---DAVgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL--DKDGKTPLELAEENGFREV 163

                  ....*
gi 193206531  193 TRVLL 197
Cdd:PTZ00322  164 VQLLS 168
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
74-205 4.59e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531    74 KGFSPliiAATAGHSSVVEVLLKNHAAIEAQS-DRTKDTALSLACSGGR-KDVVELLLAHGankehRNVSDYTPLSLASS 151
Cdd:TIGR00870   19 KAFLP---AAERGDLASVYRDLEEPKKLNINCpDRLGRSALFVAAIENEnLELTELLLNLS-----CRGAVGDTLLHAIS 90
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206531   152 GGYIEIVNMLLT----------AGSEINSRTGSKL--GISPLMLASMNGHREATRVLLEKGSDINA 205
Cdd:TIGR00870   91 LEYVDAVEAILLhllaafrksgPLELANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPA 156
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
629-681 5.03e-03

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: 36.80  E-value: 5.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 193206531  629 VIGKGGSNVNAVREATGAIIEInkiqESNKQAERTVLAKGTPEMVRYAMNIIN 681
Cdd:cd22411    14 IIGKGGATIKKIREETNTRIDL----PEENSDSDVITITGKKEDVEKARERIL 62
KH-I_HNRNPK_rpt2 cd22433
second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
626-673 6.56e-03

second 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 second one.


Pssm-ID: 411861 [Multi-domain]  Cd Length: 70  Bit Score: 36.85  E-value: 6.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 193206531  626 ASRVIGKGGSNVNAVREATGAIIEINKiQESNKQAERTVLAKGTPEMV 673
Cdd:cd22433    13 AGCIIGRAGFKIKELREKTGATIKVYS-ECCPRSTDRVVQIGGKPDKV 59
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
48-69 6.77e-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: 35.64  E-value: 6.77e-03
                            10        20
                    ....*....|....*....|..
gi 193206531     48 IACANGHKDIVELLLKEGANIE 69
Cdd:smart00248    8 LAAENGNLEVVKLLLDKGADIN 29
KH-I_PCBP1_2_rpt3 cd22521
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
615-681 8.02e-03

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: 36.57  E-value: 8.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193206531  615 SSWKLTIPAYAASRVIGKGGSNVNAVREATGAIIEI-NKIQESNkqaERTVLAKGTPEMVRYAMNIIN 681
Cdd:cd22521     5 TSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIaNPVEGST---DRQVTITGSAASISLAQYLIN 69
KH-I_RCF3_like_rpt5 cd22463
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
619-680 8.15e-03

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: 36.64  E-value: 8.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193206531  619 LTIPAYAASRVIGKGGSNVNAVREATGAIIEINKIQESNKQAERTVLAKGTPEMVRYAMNII 680
Cdd:cd22463     6 FQIPEAVVGLIIGKSGNTIKQISERSGAFVAIVQDRYPLEETQKILRISGTEEQLKRAQSLV 67
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
110-139 8.31e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 8.31e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 193206531   110 DTALSLAC-SGGRKDVVELLLAHGANKEHRN 139
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
110-136 9.10e-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: 35.26  E-value: 9.10e-03
                            10        20
                    ....*....|....*....|....*..
gi 193206531    110 DTALSLACSGGRKDVVELLLAHGANKE 136
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
KH-I_IGF2BP3_rpt4 cd22501
fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
619-659 9.60e-03

fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 3 (IGF2BP3) and similar proteins; IGF2BP3, also called IGF2 mRNA-binding protein 3 (IMP-3), or hepatocellular carcinoma autoantigen p62, or IGF-II mRNA-binding protein 3, or VICKZ family member 3 (VICKZ3), or KH domain-containing protein overexpressed in cancer, or KOC, is primarily found in the nucleolus, where it can bind to the 5' UTR of the insulin-like growth factor II leader 3 mRNA and may repress translation of insulin-like growth factor II during late development. It acts as an RNA-binding factor that may recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. IGF2BP3 binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. It also binds to beta-actin/ACTB and MYC transcripts. IGF2BP3 can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP2 in an RNA-dependent manner. IGF2BP3 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: 411929  Cd Length: 66  Bit Score: 36.21  E-value: 9.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 193206531  619 LTIPAYAASRVIGKGGSNVNAVREATGA--IIEINKIQESNKQ 659
Cdd:cd22501     4 IKVPSYAAGRVIGKGGKTVNELQNLTSAevVVPRDQTPDENDQ 46
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
67-208 9.68e-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: 40.45  E-value: 9.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531    67 NIEHRDKKGFSPLIIAATAGHSSVVEVLLKNHAaieaQSDRTKDTALsLACSGGRKDVVELLLAH-------GANKEHRN 139
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIENENLELTELLLNLS----CRGAVGDTLL-HAISLEYVDAVEAILLHllaafrkSGPLELAN 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206531   140 VS-------DYTPLSLASSGGYIEIVNMLLTAGSEINSR------------TGSKLGISPLMLASMNGHREATRVLLEKG 200
Cdd:TIGR00870  119 DQytseftpGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDP 198

                   ....*...
gi 193206531   201 SDINAQIE 208
Cdd:TIGR00870  199 ADILTADS 206
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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