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Conserved domains on  [gi|665821243|ref|NP_001287904|]
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ankyrin repeat domain-containing protein 42 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-264 1.33e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 1.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  30 IHDAVRAGDVKQLSEIVVRGASINELDvLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACV 109
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKD-DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 110 QALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVD 189
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665821243 190 YNGNLPVHLAAMEGHLHCFKFLVSRMssATQVLKAFNDNGENVLDLAQRFFKQNILQFIQGAEYEGKDLEDQETL 264
Cdd:COG0666  217 NDGKTALDLAAENGNLEIVKLLLEAG--ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 super family cl39094
ankyrin repeat protein; Provisional
112-444 1.19e-11

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 476869 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 112 LIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHG-RLGC----LQLLVKWGCSIE 186
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKyNLTDvkeiVKLLLEYGANVN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 187 DVDYNGNLPVHLAAME--GHLHCFKFLVSRMSSATQVlkafNDNGENVLDLaqrFFKQNilqfiqgaeyegkdledqetl 264
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIK----NSDGENLLHL---YLESN--------------------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 265 afpghvaafKGDLGMLKKLVEDGV---------------ININERADNGSTPMHKAAGQGHIECLQWLIKMGADSNITNK 329
Cdd:PHA03100 153 ---------KIDLKILKLLIDKGVdinaknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 330 AGERPSDVAKRFAHLAAVKLLeeLQKYdiDDENEIDENdVKYFirhgvegstdakDDLCLSDLDKTDARMrayKKIVELR 409
Cdd:PHA03100 224 YGDTPLHIAILNNNKEIFKLL--LNNG--PSIKTIIET-LLYF------------KDKDLNTITKIKMLK---KSIMYMF 283
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 665821243 410 HLLEIAESNYKHLGGITE-EDLKQK-KEQLESEKTIK 444
Cdd:PHA03100 284 LLDPGFYKNRKLIENSKSlKDVINEcEKEIERMKEIK 320
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
426-482 1.94e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665821243 426 TEEDLKQKKEQLES-EKTIKELQGQLEYERLRREKLECQLDEYRAEVDQLRETLEKIQ 482
Cdd:COG4372   64 LEEELEQARSELEQlEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-264 1.33e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 1.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  30 IHDAVRAGDVKQLSEIVVRGASINELDvLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACV 109
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKD-DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 110 QALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVD 189
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665821243 190 YNGNLPVHLAAMEGHLHCFKFLVSRMssATQVLKAFNDNGENVLDLAQRFFKQNILQFIQGAEYEGKDLEDQETL 264
Cdd:COG0666  217 NDGKTALDLAAENGNLEIVKLLLEAG--ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-156 1.83e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243   64 LHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALImNGANLTAQDDrGCTPLHLAATHGHSFTLQ 143
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 665821243  144 IMLRSGVDPSVTD 156
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
48-226 1.34e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.30  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  48 RGASINELDvLHKFTPLHW--AAHSGSLECLHWLLWHGADITHVTTRGWTASHIAA--IRGQDACVQALIMNGANLTAQD 123
Cdd:PHA03095 141 KGADVNALD-LYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATD 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 124 DRGCTPLHLAATHGHSFTLQI--MLRSGVDPSVTDKREWRPVHYAA-FHGRLGCLQLLvKWGCSIEDVDYNGNLPVHLAA 200
Cdd:PHA03095 220 MLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAvFNNPRACRRLI-ALGADINAVSSDGNTPLSLMV 298
                        170       180
                 ....*....|....*....|....*.
gi 665821243 201 MEGHLHCFKFLVSRMSSATQVLKAFN 226
Cdd:PHA03095 299 RNNNGRAVRAALAKNPSAETVAATLN 324
PHA03100 PHA03100
ankyrin repeat protein; Provisional
112-444 1.19e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 112 LIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHG-RLGC----LQLLVKWGCSIE 186
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKyNLTDvkeiVKLLLEYGANVN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 187 DVDYNGNLPVHLAAME--GHLHCFKFLVSRMSSATQVlkafNDNGENVLDLaqrFFKQNilqfiqgaeyegkdledqetl 264
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIK----NSDGENLLHL---YLESN--------------------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 265 afpghvaafKGDLGMLKKLVEDGV---------------ININERADNGSTPMHKAAGQGHIECLQWLIKMGADSNITNK 329
Cdd:PHA03100 153 ---------KIDLKILKLLIDKGVdinaknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 330 AGERPSDVAKRFAHLAAVKLLeeLQKYdiDDENEIDENdVKYFirhgvegstdakDDLCLSDLDKTDARMrayKKIVELR 409
Cdd:PHA03100 224 YGDTPLHIAILNNNKEIFKLL--LNNG--PSIKTIIET-LLYF------------KDKDLNTITKIKMLK---KSIMYMF 283
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 665821243 410 HLLEIAESNYKHLGGITE-EDLKQK-KEQLESEKTIK 444
Cdd:PHA03100 284 LLDPGFYKNRKLIENSKSlKDVINEcEKEIERMKEIK 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
197-328 1.03e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  197 HLAAMEGHLHCFKFLVSRMSSATQVlkafNDNGENVLdlaqrffkqnilqfiqgaeyegkdledqetlafpgHVAAFKGD 276
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQ----DKNGRTAL-----------------------------------HLAAKNGH 42
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665821243  277 LGMLKKLVEDGVININeraDNGSTPMHKAAGQGHIECLQWLIKMGADSNITN 328
Cdd:pfam12796  43 LEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
62-202 1.70e-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: 47.31  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  62 TPLHWAAHSGSLECLHWLL-WHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANL-----TAQDDRGCTPLHLAAT 135
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmTSDLYQGETALHIAVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 136 HGHSFTLQIMLRSGVD---PSVTDK--REWR---------PVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLPVHLAAM 201
Cdd:cd22192   99 NQNLNLVRELIARGADvvsPRATGTffRPGPknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                 .
gi 665821243 202 E 202
Cdd:cd22192  179 Q 179
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
59-87 3.37e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 3.37e-05
                           10        20
                   ....*....|....*....|....*....
gi 665821243    59 HKFTPLHWAAHSGSLECLHWLLWHGADIT 87
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
348-482 6.32e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.53  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 348 KLLEELQKYDiddeNEIDEndvkyfIRHGVEGSTDAKDDLcLSDLDKTDARMRAYKK-IVELRHLLEIAESNYKHLggit 426
Cdd:COG1579    7 RALLDLQELD----SELDR------LEHRLKELPAELAEL-EDELAALEARLEAAKTeLEDLEKEIKRLELEIEEV---- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 665821243 427 EEDLKQKKEQLESEKTIKE---LQGQLEYERLRREKLECQLDEYRAEVDQLRETLEKIQ 482
Cdd:COG1579   72 EARIKKYEEQLGNVRNNKEyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
426-482 1.94e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665821243 426 TEEDLKQKKEQLES-EKTIKELQGQLEYERLRREKLECQLDEYRAEVDQLRETLEKIQ 482
Cdd:COG4372   64 LEEELEQARSELEQlEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
297-326 2.22e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 2.22e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 665821243   297 NGSTPMHKAAGQGHIECLQWLIKMGADSNI 326
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
62-134 8.68e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243   62 TPLHWAAHSGSLECLHWLLWHGADITH-------VTTRGWT-ASH------IAAIRGQDACVQALIMNGANLTAQDDRGC 127
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDsFYHgesplnAAACLGSPSIVALLSEDPADILTADSLGN 209

                  ....*..
gi 665821243  128 TPLHLAA 134
Cdd:TIGR00870 210 TLLHLLV 216
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
427-482 1.44e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.75  E-value: 1.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665821243  427 EEDLKQKKEQL-ESEKTIKELQGQLEYERLRREKLECQLDEYRAEVDQLRETLEKIQ 482
Cdd:pfam20492  19 EEETKKAQEELeESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEA 75
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
430-486 5.23e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 5.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665821243  430 LKQKKEQLESEKTIKELQ-GQLEYE------RLRREKLECQLDEYRAEVDQLRETLEKIQVPNF 486
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKiSDLEDElnkddfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQE 585
eNOPS_SF cd12931
NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All ...
427-470 5.51e-03

NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All members in this family contain a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRM1 and RRM2), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain with a long helical C-terminal extension. The NOPS domain specifically binds to RRM2 domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies. PSF has an additional large N-terminal domain that differentiates it from other family members. The p54nrb/PSF/PSP1 family includes 54 kDa nuclear RNA- and DNA-binding protein (p54nrb), polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF) and paraspeckle protein 1 (PSP1), which are ubiquitously expressed and are well conserved in vertebrates. p54nrb, also termed NONO or NMT55, is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. PSF, also termed POMp100, is also a multi-functional protein that binds RNA, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and many factors, and mediates diverse activities in the cell. PSP1, also termed PSPC1, is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. The cellular function of PSP1 remains unknown currently. The family also includes some p54nrb/PSF/PSP1 homologs from invertebrate species. For instance, the Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA) and Chironomus tentans hrp65 gene encoding protein Hrp65. D. melanogaster NONA is involved in eye development and behavior and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans Hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore.


Pssm-ID: 240579 [Multi-domain]  Cd Length: 90  Bit Score: 36.07  E-value: 5.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 665821243 427 EEDLKQKKEQLEseKTIKElqgqleyerlRREKLECQLDEYRAE 470
Cdd:cd12931   57 YELEKQQREQLE--KELKE----------AREKLEAEMEAARYE 88
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
428-490 5.97e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.05  E-value: 5.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665821243 428 EDLKQKKEQLES-EKTIKELQGQLEYERLRREKLECQLDEYRAEVDQLRetlekiQVPNFVAMV 490
Cdd:PRK03992   1 ERLEALEERNSElEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK------SPPLIVATV 58
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-264 1.33e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 1.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  30 IHDAVRAGDVKQLSEIVVRGASINELDvLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACV 109
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKD-DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 110 QALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVD 189
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665821243 190 YNGNLPVHLAAMEGHLHCFKFLVSRMssATQVLKAFNDNGENVLDLAQRFFKQNILQFIQGAEYEGKDLEDQETL 264
Cdd:COG0666  217 NDGKTALDLAAENGNLEIVKLLLEAG--ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-297 1.43e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  49 GASINELDVLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCT 128
Cdd:COG0666   43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 129 PLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLPVHLAAMEGHLHCF 208
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 209 KFLVSRMSSATqvlkAFNDNGENVLDLAQRFFKQNILQFIQgaEYEGKDLEDQETLAFPGHVAAFKGDLGMLKKLVEDGV 288
Cdd:COG0666  203 KLLLEAGADVN----AKDNDGKTALDLAAENGNLEIVKLLL--EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276

                 ....*....
gi 665821243 289 ININERADN 297
Cdd:COG0666  277 LLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-368 2.55e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.28  E-value: 2.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  42 LSEIVVRGASINELDVLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTA 121
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 122 QDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLPVHLAAM 201
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 202 EGHLHCFKFLVSRmsSATqvLKAFNDNGENVLdlaqrffkqnilqfiqgaeyegkdledqetlafpgHVAAFKGDLGMLK 281
Cdd:COG0666  163 NGNLEIVKLLLEA--GAD--VNARDNDGETPL-----------------------------------HLAAENGHLEIVK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 282 KLVEDGViNINERADNGSTPMHKAAGQGHIECLQWLIKMGADSNITNKAGERPSDVAKRFAHLAAVKLLEELQKYDIDDE 361
Cdd:COG0666  204 LLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282

                 ....*..
gi 665821243 362 NEIDEND 368
Cdd:COG0666  283 LDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-194 4.04e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 4.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  17 ANPCSRKKVHFGSIHDAVRAGDVKQLSEIVVRGASINELDvLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTA 96
Cdd:COG0666  111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  97 SHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQ 176
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
                        170
                 ....*....|....*...
gi 665821243 177 LLVKWGCSIEDVDYNGNL 194
Cdd:COG0666  270 LLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
111-434 2.51e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 2.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 111 ALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDY 190
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 191 NGNLPVHLAAMEGHLHCFKFLVsrmssatqvlkafnDNGENVldlaqrffkqnilqfiqgaeyEGKDLEDQETLafpgHV 270
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLL--------------EAGADV---------------------NARDKDGETPL----HL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 271 AAFKGDLGMLKKLVEDGvININERADNGSTPMHKAAGQGHIECLQWLIKMGADSNITNKAGERPSDVAKRFAHLAAVKLL 350
Cdd:COG0666  127 AAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 351 EELQKyDIDDENEIDENDVKYFIRHGVEGSTDAKDDLCLSDLDKTDARMRAYKKIVELRHLLEIAESNYKHLGGITEEDL 430
Cdd:COG0666  206 LEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284

                 ....
gi 665821243 431 KQKK 434
Cdd:COG0666  285 LLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-156 1.83e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243   64 LHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALImNGANLTAQDDrGCTPLHLAATHGHSFTLQ 143
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 665821243  144 IMLRSGVDPSVTD 156
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
98-189 7.80e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 7.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243   98 HIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLrSGVDPSVTDKReWRPVHYAAFHGRLGCLQL 177
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNG-RTALHYAARSGHLEIVKL 79
                          90
                  ....*....|..
gi 665821243  178 LVKWGCSIEDVD 189
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
48-226 1.34e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.30  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  48 RGASINELDvLHKFTPLHW--AAHSGSLECLHWLLWHGADITHVTTRGWTASHIAA--IRGQDACVQALIMNGANLTAQD 123
Cdd:PHA03095 141 KGADVNALD-LYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATD 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 124 DRGCTPLHLAATHGHSFTLQI--MLRSGVDPSVTDKREWRPVHYAA-FHGRLGCLQLLvKWGCSIEDVDYNGNLPVHLAA 200
Cdd:PHA03095 220 MLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAvFNNPRACRRLI-ALGADINAVSSDGNTPLSLMV 298
                        170       180
                 ....*....|....*....|....*.
gi 665821243 201 MEGHLHCFKFLVSRMSSATQVLKAFN 226
Cdd:PHA03095 299 RNNNGRAVRAALAKNPSAETVAATLN 324
PHA02874 PHA02874
ankyrin repeat protein; Provisional
45-239 2.21e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  45 IVVRGASINELDVLHKfTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDD 124
Cdd:PHA02874 110 ILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 125 RGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRlGCLQLLVKwGCSIEDVDYNGNLPVHLAAmegH 204
Cdd:PHA02874 189 NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAI---N 263
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 665821243 205 LHCFKFLVSRMSSATQVLKAFNDNGENVLDLAQRF 239
Cdd:PHA02874 264 PPCDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
PHA02874 PHA02874
ankyrin repeat protein; Provisional
34-403 2.27e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.08  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  34 VRAGDVKQLSEIV-VRGASINeLDVLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRG----WTASHIAA------- 101
Cdd:PHA02874   9 IYSGDIEAIEKIIkNKGNCIN-ISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIphplLTAIKIGAhdiikll 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 102 -IRGQDACV-----------QALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFH 169
Cdd:PHA02874  88 iDNGVDTSIlpipciekdmiKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 170 GRLGCLQLLVKWGCSIEDVDYNGNLPVHLAAMEGHLHCFKFLVsrmssatqvlkafnDNGENVLDLAQRFFKqnilqfiq 249
Cdd:PHA02874 168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI--------------DHGNHIMNKCKNGFT-------- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 250 gaeyegkdledqetlafPGHVAAFKgDLGMLKKLVEDGVININERadNGSTPMHKAAGQG-HIECLQWLIKMGADSNITN 328
Cdd:PHA02874 226 -----------------PLHNAIIH-NRSAIELLINNASINDQDI--DGSTPLHHAINPPcDIDIIDILLYHKADISIKD 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 329 KAGERPSDVAKRF-----------AHLAAVKLLEELQKYDIDDENEIDENDV-KYFIRHGVEGSTDAKDDLCLSDLDKTD 396
Cdd:PHA02874 286 NKGENPIDTAFKYinkdpvikdiiANAVLIKEADKLKDSDFLEHIEIKDNKEfSDFIKECNEEIEDMKKTKCGCDKNIFD 365

                 ....*..
gi 665821243 397 ARMRAYK 403
Cdd:PHA02874 366 LCLIRIK 372
PHA03095 PHA03095
ankyrin-like protein; Provisional
34-334 3.36e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  34 VRAGDVKQLseiVVRGASINELDVLHKfTPLHWAAHSGS---LECLHWLLWHGADITHVTTRGWTASHIAAIRGQDA-CV 109
Cdd:PHA03095  25 VTVEEVRRL---LAAGADVNFRGEYGK-TPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 110 QALIMNGANLTAQDDRGCTPLH--LAATHGHSFTLQIMLRSGVDPSVTDKREWRPVH-YAAFHG-RLGCLQLLVKWGCSI 185
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADV 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 186 EDVDYNGNLPVHlaameghlhcfKFLVSRMSSAtqvlkafndngenvldlaqRFFKQNIlqfIQGAEYEGKDLEDQETLa 265
Cdd:PHA03095 181 YAVDDRFRSLLH-----------HHLQSFKPRA-------------------RIVRELI---RAGCDPAATDMLGNTPL- 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665821243 266 fpgHVAAFKGDLGMLK--KLVEDGVInINERADNGSTPMHKAAGQGHIECLQWLIKMGADSNITNKAGERP 334
Cdd:PHA03095 227 ---HSMATGSSCKRSLvlPLLIAGIS-INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
Ank_2 pfam12796
Ankyrin repeats (3 copies);
30-123 2.95e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243   30 IHDAVRAGDVKQLSEIVVRGASINELDVLHKfTPLHWAAHSGSLECLHWLLWHGAdiTHVTTRGWTASHIAAIRGQDACV 109
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 665821243  110 QALIMNGANLTAQD 123
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
130-214 3.01e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  130 LHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKwgCSIEDVDYNGNLPVHLAAMEGHLHCFK 209
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78

                  ....*
gi 665821243  210 FLVSR 214
Cdd:pfam12796  79 LLLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
30-185 1.13e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.72  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  30 IHDAVRAGDVKQLSEIVVRGASINelDVLHK--FTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDA 107
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 108 CVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKR-EWRPVHYAAFHGRLGCLQLLVKWG--CS 184
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGadCN 229

                 .
gi 665821243 185 I 185
Cdd:PHA02875 230 I 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
26-214 2.36e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  26 HFGSIHDAVRAGDVKQLSEIVVRGASINELDVLHkFTPLHWAA--HSGSLECLHWLLWHGADITHVTTRGWTASHIAAIR 103
Cdd:PHA03100  73 HYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNG-ITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLES 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 104 GQD--ACVQALIMNGANLTAQDdrgctplhlaathghsfTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKW 181
Cdd:PHA03100 152 NKIdlKILKLLIDKGVDINAKN-----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL 214
                        170       180       190
                 ....*....|....*....|....*....|...
gi 665821243 182 GCSIEDVDYNGNLPVHLAAMEGHLHCFKFLVSR 214
Cdd:PHA03100 215 GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247
PHA03100 PHA03100
ankyrin repeat protein; Provisional
112-444 1.19e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 112 LIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHG-RLGC----LQLLVKWGCSIE 186
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKyNLTDvkeiVKLLLEYGANVN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 187 DVDYNGNLPVHLAAME--GHLHCFKFLVSRMSSATQVlkafNDNGENVLDLaqrFFKQNilqfiqgaeyegkdledqetl 264
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIK----NSDGENLLHL---YLESN--------------------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 265 afpghvaafKGDLGMLKKLVEDGV---------------ININERADNGSTPMHKAAGQGHIECLQWLIKMGADSNITNK 329
Cdd:PHA03100 153 ---------KIDLKILKLLIDKGVdinaknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 330 AGERPSDVAKRFAHLAAVKLLeeLQKYdiDDENEIDENdVKYFirhgvegstdakDDLCLSDLDKTDARMrayKKIVELR 409
Cdd:PHA03100 224 YGDTPLHIAILNNNKEIFKLL--LNNG--PSIKTIIET-LLYF------------KDKDLNTITKIKMLK---KSIMYMF 283
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 665821243 410 HLLEIAESNYKHLGGITE-EDLKQK-KEQLESEKTIK 444
Cdd:PHA03100 284 LLDPGFYKNRKLIENSKSlKDVINEcEKEIERMKEIK 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
197-328 1.03e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  197 HLAAMEGHLHCFKFLVSRMSSATQVlkafNDNGENVLdlaqrffkqnilqfiqgaeyegkdledqetlafpgHVAAFKGD 276
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQ----DKNGRTAL-----------------------------------HLAAKNGH 42
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665821243  277 LGMLKKLVEDGVININeraDNGSTPMHKAAGQGHIECLQWLIKMGADSNITN 328
Cdd:pfam12796  43 LEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
269-350 1.16e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  269 HVAAFKGDLGMLKKLVEDGViNINERADNGSTPMHKAAGQGHIECLQWLIKmGADSNITNKaGERPSDVAKRFAHLAAVK 348
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                  ..
gi 665821243  349 LL 350
Cdd:pfam12796  79 LL 80
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
133-358 1.23e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.12  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 133 AATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLPVHLAAMEGHLHCFkflv 212
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF---- 607
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 213 srmssatqvlkafndngenvldlaqrffkqNIL-QFIQGAE-YEGKDLedqetLAFpghvAAFKGDLGMLKKLVEDGvIN 290
Cdd:PLN03192 608 ------------------------------RILyHFASISDpHAAGDL-----LCT----AAKRNDLTAMKELLKQG-LN 647
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665821243 291 INERADNGSTPMHKAAGQGHIECLQWLIKMGADsnitnkagerpSDVAKRFAHLAAVKLLEELQKYDI 358
Cdd:PLN03192 648 VDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD-----------VDKANTDDDFSPTELRELLQKREL 704
Ank_4 pfam13637
Ankyrin repeats (many copies);
62-113 1.83e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 1.83e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665821243   62 TPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALI 113
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
159-212 4.86e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 4.86e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 665821243  159 EWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLPVHLAAMEGHLHCFKFLV 212
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
269-318 2.42e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 2.42e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665821243  269 HVAAFKGDLGMLKKLVEDGViNINERADNGSTPMHKAAGQGHIECLQWLI 318
Cdd:pfam13637   6 HAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
128-179 9.06e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 9.06e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665821243  128 TPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLV 179
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
29-350 1.04e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.77  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  29 SIHDAVRAGDVKQLSEIVVRGASINELDVlHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDAC 108
Cdd:PHA02876 148 LIKERIQQDELLIAEMLLEGGADVNAKDI-YCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 109 VQALIMNGANLTAQDdrgcTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCL-QLLVKWGCSIED 187
Cdd:PHA02876 227 IKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNA 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 188 VDYNGNLPVHLAAMEGH-LHCFKFLVSRMSSATQVLKAFNDNGENVLDLAQrfFKQNILQFIQ-GAEYEGKDLEDQEtla 265
Cdd:PHA02876 303 KNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDR--NKDIVITLLElGANVNARDYCDKT--- 377
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 266 fPGHVAAFKGDLGMLKKLVEDGViNINERADNGSTPMHKA-AGQGHIECLQWLIKMGADSNITNKAGERPSDVA-KRFAH 343
Cdd:PHA02876 378 -PIHYAAVRNNVVIINTLLDYGA-DIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYAcKKNCK 455

                 ....*..
gi 665821243 344 LAAVKLL 350
Cdd:PHA02876 456 LDVIEML 462
Ank_5 pfam13857
Ankyrin repeats (many copies);
283-338 7.97e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 7.97e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665821243  283 LVEDGVININERADNGSTPMHKAAGQGHIECLQWLIKMGADSNITNKAGERPSDVA 338
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
67-228 1.01e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  67 AAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIM- 145
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILy 611
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 146 -LRSGVDPSVTDKRewrpVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLPVHLAAMEGHLHCFKFLVsrMSSATqVLKA 224
Cdd:PLN03192 612 hFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI--MNGAD-VDKA 684

                 ....
gi 665821243 225 FNDN 228
Cdd:PLN03192 685 NTDD 688
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
98-195 1.02e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  98 HIAAiRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQL 177
Cdd:PTZ00322  88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                         90
                 ....*....|....*...
gi 665821243 178 LVkwGCSIEDVDYNGNLP 195
Cdd:PTZ00322 167 LS--RHSQCHFELGANAK 182
Ank_4 pfam13637
Ankyrin repeats (many copies);
93-138 1.09e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.09e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 665821243   93 GWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGH 138
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PHA02878 PHA02878
ankyrin repeat protein; Provisional
49-215 1.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  49 GASINELDVLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCT 128
Cdd:PHA02878 157 GADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 129 PLHLAATHGHSFT-LQIMLRSGVDPSVTDK-REWRPVHYAAFHGRLgcLQLLVKWGCSIEDVDYNGNLPVHLAAMEGH-L 205
Cdd:PHA02878 237 PLHISVGYCKDYDiLKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQYLcI 314
                        170
                 ....*....|
gi 665821243 206 HCFKFLVSRM 215
Cdd:PHA02878 315 NIGRILISNI 324
Ank_4 pfam13637
Ankyrin repeats (many copies);
298-350 2.85e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 2.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665821243  298 GSTPMHKAAGQGHIECLQWLIKMGADSNITNKAGERPSDVAKRFAHLAAVKLL 350
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
32-253 2.09e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  32 DAVRAGDVKQLSEIVVRGASINeLDVLHKFTPLHWAAHSGSLECLHWLLWHGA--DITHVTTRgwTASHIAAIRGQDACV 109
Cdd:PHA02875   8 DAILFGELDIARRLLDIGINPN-FEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDAVEEGDVKAV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 110 QALIMNGanlTAQDD----RGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSI 185
Cdd:PHA02875  85 EELLDLG---KFADDvfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665821243 186 EDVDYNGNLPVHLAAMEGHLHCFKFL---------VSRMSSATQVLKAFNDNGENVLDL-AQRFFKQNILQFIQGAEY 253
Cdd:PHA02875 162 DIEDCCGCTPLIIAMAKGDIAICKMLldsganidyFGKNGCVAALCYAIENNKIDIVRLfIKRGADCNIMFMIEGEEC 239
PHA02878 PHA02878
ankyrin repeat protein; Provisional
109-199 3.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.49  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 109 VQALIMNGANLTAQD-DRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIED 187
Cdd:PHA02878 150 TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
                         90
                 ....*....|..
gi 665821243 188 VDYNGNLPVHLA 199
Cdd:PHA02878 230 RDKCGNTPLHIS 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
84-133 5.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 5.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665821243   84 ADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLA 133
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
62-202 1.70e-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: 47.31  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  62 TPLHWAAHSGSLECLHWLL-WHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANL-----TAQDDRGCTPLHLAAT 135
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmTSDLYQGETALHIAVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 136 HGHSFTLQIMLRSGVD---PSVTDK--REWR---------PVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLPVHLAAM 201
Cdd:cd22192   99 NQNLNLVRELIARGADvvsPRATGTffRPGPknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                 .
gi 665821243 202 E 202
Cdd:cd22192  179 Q 179
Ank_4 pfam13637
Ankyrin repeats (many copies);
30-80 2.04e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665821243   30 IHDAVRAGDVKQLSEIVVRGASINELDVLHkFTPLHWAAHSGSLECLHWLL 80
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNG-ETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
118-203 2.12e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 118 NLTAQDDRGCTPLH--------LAAThGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVD 189
Cdd:PTZ00322  67 NLTTEEVIDPVVAHmltvelcqLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
                         90
                 ....*....|....
gi 665821243 190 YNGNLPVHLAAMEG 203
Cdd:PTZ00322 146 KDGKTPLELAEENG 159
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
297-329 2.59e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 2.59e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 665821243  297 NGSTPMHKAAGQ-GHIECLQWLIKMGADSNITNK 329
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
59-87 3.37e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 3.37e-05
                           10        20
                   ....*....|....*....|....*....
gi 665821243    59 HKFTPLHWAAHSGSLECLHWLLWHGADIT 87
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
62-214 4.89e-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: 46.16  E-value: 4.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  62 TPLHWAAHSGSLECLHWLLWHGADIthVTTRG-------------WTASHI---AAIRGQDACVQALIMNGANLTAQDDR 125
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADV--VSPRAtgtffrpgpknliYYGEHPlsfAACVGNEEIVRLLIEHGADIRAQDSL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 126 GCTPLH-LAATHGHSFTLQI--MLRSgvdpsvtdkREWrpvhyaafHGRLGCLQLLvkwgcsiedVDYNGNLPVHLAAME 202
Cdd:cd22192  169 GNTVLHiLVLQPNKTFACQMydLILS---------YDK--------EDDLQPLDLV---------PNNQGLTPFKLAAKE 222
                        170
                 ....*....|..
gi 665821243 203 GHLHCFKFLVSR 214
Cdd:cd22192  223 GNIVMFQHLVQK 234
PHA02878 PHA02878
ankyrin repeat protein; Provisional
79-199 5.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  79 LLWHGADITHVTT-RGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDK 157
Cdd:PHA02878 153 LLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 665821243 158 REWRPVHYAAfhGRL---GCLQLLVKWGCSIEDVDYNGNL-PVHLA 199
Cdd:PHA02878 233 CGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYILGLtALHSS 276
Ank_5 pfam13857
Ankyrin repeats (many copies);
58-100 5.95e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 5.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 665821243   58 LHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIA 100
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
59-88 6.27e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 6.27e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 665821243   59 HKFTPLHWAAHSGSLECLHWLLWHGADITH 88
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
348-482 6.32e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.53  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 348 KLLEELQKYDiddeNEIDEndvkyfIRHGVEGSTDAKDDLcLSDLDKTDARMRAYKK-IVELRHLLEIAESNYKHLggit 426
Cdd:COG1579    7 RALLDLQELD----SELDR------LEHRLKELPAELAEL-EDELAALEARLEAAKTeLEDLEKEIKRLELEIEEV---- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 665821243 427 EEDLKQKKEQLESEKTIKE---LQGQLEYERLRREKLECQLDEYRAEVDQLRETLEKIQ 482
Cdd:COG1579   72 EARIKKYEEQLGNVRNNKEyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
Ank_5 pfam13857
Ankyrin repeats (many copies);
117-166 6.96e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 6.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665821243  117 ANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYA 166
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
29-166 8.96e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 8.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  29 SIHDAVRAGDVKQLSEIVVRGASINELDVLHKfTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQD-A 107
Cdd:PHA02878 171 ALHYATENKDQRLTELLLSYGANVNIPDKTNN-SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyD 249
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665821243 108 CVQALIMNGANLTAQDD-RGCTPLHLAAthgHS-FTLQIMLRSGVDPSVTDKREWRPVHYA 166
Cdd:PHA02878 250 ILKLLLEHGVDVNAKSYiLGLTALHSSI---KSeRKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
118-331 8.99e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 8.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 118 NLTAQDdrGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDY-NGNLPV 196
Cdd:PHA02875  29 NFEIYD--GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 197 HLAAMEGHLHCFKFLVSRmssatqvlkafndngenvldlaqrffkqnilqfiqgaeyeGKDLEDQETLAF-PGHVAAFKG 275
Cdd:PHA02875 107 HLATILKKLDIMKLLIAR----------------------------------------GADPDIPNTDKFsPLHLAVMMG 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665821243 276 DLGMLKKLVED-GVININERAdnGSTPMHKAAGQGHIECLQWLIKMGADSNITNKAG 331
Cdd:PHA02875 147 DIKGIELLIDHkACLDIEDCC--GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
PHA02946 PHA02946
ankyin-like protein; Provisional
33-198 9.43e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.04  E-value: 9.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  33 AVRAGDVKQLSEIVVRGASINELDVLHKFtPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTAshIAAIRGQDACV--- 109
Cdd:PHA02946  46 GIKGLDERFVEELLHRGYSPNETDDDGNY-PLHIASKINNNRIVAMLLTHGADPNACDKQHKTP--LYYLSGTDDEVier 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 110 -QALIMNGANLT-AQDDRGCTPLhLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVH--YAAFHGRLGCLQLLVKWGCSI 185
Cdd:PHA02946 123 iNLLVQYGAKINnSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISP 201
                        170
                 ....*....|...
gi 665821243 186 EDVDYNGNLPVHL 198
Cdd:PHA02946 202 SKPDHDGNTPLHI 214
PHA03095 PHA03095
ankyrin-like protein; Provisional
42-138 1.48e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  42 LSEIVVRGASINELDVLHKfTPLHWAAHSGSLECLHW--LLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANL 119
Cdd:PHA03095 205 VRELIRAGCDPAATDMLGN-TPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI 283
                         90
                 ....*....|....*....
gi 665821243 120 TAQDDRGCTPLHLAATHGH 138
Cdd:PHA03095 284 NAVSSDGNTPLSLMVRNNN 302
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
269-350 1.56e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 269 HVAAfKGDLGMLKKLVEDGViNINERADNGSTPMHKAAGQGHIECLQWLIKMGADSNITNKAGERPSDVAKRFAHLAAVK 348
Cdd:PTZ00322  88 QLAA-SGDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                 ..
gi 665821243 349 LL 350
Cdd:PTZ00322 166 LL 167
PHA02798 PHA02798
ankyrin-like protein; Provisional
109-332 1.58e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 109 VQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQI---MLRSGVDPSVTDKREWRpvhyaafhgrlgCLQLLVKWGCSI 185
Cdd:PHA02798  92 VKILIENGADINKKNSDGETPLYCLLSNGYINNLEIllfMIENGADTTLLDKDGFT------------MLQVYLQSNHHI 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 186 E------------DVDYNGNlpvhlaaMEGH--LHC-FKFLVSRMSSatQVLKAFNDNGEnVLDLAQRFFKQNILQFIQG 250
Cdd:PHA02798 160 DieiiklllekgvDINTHNN-------KEKYdtLHCyFKYNIDRIDA--DILKLFVDNGF-IINKENKSHKKKFMEYLNS 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 251 AEYEGKDLeDQETLAFpghvaAFKgdlgmlkklvedgVININERADNGSTPMHKAAGQGHIECLQWLIKMGADSNITNKA 330
Cdd:PHA02798 230 LLYDNKRF-KKNILDF-----IFS-------------YIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITEL 290

                 ..
gi 665821243 331 GE 332
Cdd:PHA02798 291 GN 292
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
426-482 1.94e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665821243 426 TEEDLKQKKEQLES-EKTIKELQGQLEYERLRREKLECQLDEYRAEVDQLRETLEKIQ 482
Cdd:COG4372   64 LEEELEQARSELEQlEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
297-326 2.22e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 2.22e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 665821243   297 NGSTPMHKAAGQGHIECLQWLIKMGADSNI 326
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
302-363 2.31e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 2.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665821243  302 MHKAAGQGHIECLQWLIKMGADSNITNKAGERPSDVAKRFAHLAAVKLLeeLQKYDIDDENE 363
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL--LEHADVNLKDN 60
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
297-326 3.17e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 3.17e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 665821243  297 NGSTPMHKAAGQGHIECLQWLIKMGADSNI 326
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
101-213 3.27e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.12  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 101 AIRGQDA-CVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGR--LGCLQL 177
Cdd:PHA02946  46 GIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINL 125
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 665821243 178 LVKWGCSIED-VDYNGNLPVhLAAMEGHLHCFKFLVS 213
Cdd:PHA02946 126 LVQYGAKINNsVDEEGCGPL-LACTDPSERVFKKIMS 161
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
59-90 3.49e-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: 38.04  E-value: 3.49e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 665821243   59 HKFTPLHWAA-HSGSLECLHWLLWHGADITHVT 90
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
49-118 6.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 6.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  49 GASINELDVlHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGAN 118
Cdd:PHA03100 182 GVPINIKDV-YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
84-214 6.95e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  84 ADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQ-----------DDR---GCTPLHLAATHGHSFTLQIMLRSG 149
Cdd:cd22194  132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLMEKE 211
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665821243 150 VDP-SVTDKREWRPVH-----------YAAFHGRLGCLQLLVKWGCSIEDVDYNGNL-PVHLAAMEGHLHCFKFLVSR 214
Cdd:cd22194  212 STDiTSQDSRGNTVLHalvtvaedsktQNDFVKRMYDMILLKSENKNLETIRNNEGLtPLQLAAKMGKAEILKYILSR 289
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
62-134 8.68e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243   62 TPLHWAAHSGSLECLHWLLWHGADITH-------VTTRGWT-ASH------IAAIRGQDACVQALIMNGANLTAQDDRGC 127
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDsFYHgesplnAAACLGSPSIVALLSEDPADILTADSLGN 209

                  ....*..
gi 665821243  128 TPLHLAA 134
Cdd:TIGR00870 210 TLLHLLV 216
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
125-157 1.03e-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: 1.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 665821243  125 RGCTPLHLAATH-GHSFTLQIMLRSGVDPSVTDK 157
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
427-482 1.44e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.75  E-value: 1.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665821243  427 EEDLKQKKEQL-ESEKTIKELQGQLEYERLRREKLECQLDEYRAEVDQLRETLEKIQ 482
Cdd:pfam20492  19 EEETKKAQEELeESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEA 75
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
57-147 2.13e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  57 VLHKFT-PLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAAT 135
Cdd:PTZ00322  78 VAHMLTvELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
                         90
                 ....*....|..
gi 665821243 136 HGHSFTLQIMLR 147
Cdd:PTZ00322 158 NGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
125-154 2.21e-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: 2.21e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 665821243   125 RGCTPLHLAATHGHSFTLQIMLRSGVDPSV 154
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
92-124 2.60e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 2.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 665821243   92 RGWTASHIAAIR-GQDACVQALIMNGANLTAQDD 124
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
HalX pfam08663
HalX domain; HalX is a domain of unknown function, previously (mis)annotated as HoxA-like ...
430-479 2.92e-03

HalX domain; HalX is a domain of unknown function, previously (mis)annotated as HoxA-like transcriptional regulator.


Pssm-ID: 400823  Cd Length: 68  Bit Score: 36.45  E-value: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665821243  430 LKQKKEQLESEKTIKELQGQLEYERLRREklecqLDEYRAEVDQLRETLE 479
Cdd:pfam08663  15 LASKRAVLEAEKSEAELADSEEYQELEAR-----IEELRAELDETLDELD 59
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
430-486 5.23e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 5.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665821243  430 LKQKKEQLESEKTIKELQ-GQLEYE------RLRREKLECQLDEYRAEVDQLRETLEKIQVPNF 486
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKiSDLEDElnkddfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQE 585
eNOPS_SF cd12931
NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All ...
427-470 5.51e-03

NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All members in this family contain a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRM1 and RRM2), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain with a long helical C-terminal extension. The NOPS domain specifically binds to RRM2 domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies. PSF has an additional large N-terminal domain that differentiates it from other family members. The p54nrb/PSF/PSP1 family includes 54 kDa nuclear RNA- and DNA-binding protein (p54nrb), polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF) and paraspeckle protein 1 (PSP1), which are ubiquitously expressed and are well conserved in vertebrates. p54nrb, also termed NONO or NMT55, is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. PSF, also termed POMp100, is also a multi-functional protein that binds RNA, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and many factors, and mediates diverse activities in the cell. PSP1, also termed PSPC1, is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. The cellular function of PSP1 remains unknown currently. The family also includes some p54nrb/PSF/PSP1 homologs from invertebrate species. For instance, the Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA) and Chironomus tentans hrp65 gene encoding protein Hrp65. D. melanogaster NONA is involved in eye development and behavior and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans Hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore.


Pssm-ID: 240579 [Multi-domain]  Cd Length: 90  Bit Score: 36.07  E-value: 5.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 665821243 427 EEDLKQKKEQLEseKTIKElqgqleyerlRREKLECQLDEYRAE 470
Cdd:cd12931   57 YELEKQQREQLE--KELKE----------AREKLEAEMEAARYE 88
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
84-214 5.89e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.39  E-value: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243  84 ADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQ---------DDRGC-----TPLHLAATHGHSFTLQIMLRSG 149
Cdd:cd22193   67 AEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHakgrffqpkYQGEGfyfgeLPLSLAACTNQPDIVQYLLENE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 150 ---VDPSVTDKREWRPVHY-----------AAFHGRL--GCLQLLVKW--GCSIEDVDYNGNL-PVHLAAMEGHLHCFKF 210
Cdd:cd22193  147 hqpADIEAQDSRGNTVLHAlvtvadntkenTKFVTRMydMILIRGAKLcpTVELEEIRNNDGLtPLQLAAKMGKIEILKY 226

                 ....
gi 665821243 211 LVSR 214
Cdd:cd22193  227 ILQR 230
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
428-490 5.97e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.05  E-value: 5.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665821243 428 EDLKQKKEQLES-EKTIKELQGQLEYERLRREKLECQLDEYRAEVDQLRetlekiQVPNFVAMV 490
Cdd:PRK03992   1 ERLEALEERNSElEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK------SPPLIVATV 58
PHA02878 PHA02878
ankyrin repeat protein; Provisional
162-350 6.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 6.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 162 PVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLPVHLAAMEGHLHCFKFLVS-----RMSSATQVLK-AFNDNGENVLD- 234
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcSVFYTLVAIKdAFNNRNVEIFKi 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821243 235 -LAQRFFKQNILQFIQGAEYEGKDLEDQEtlafpghvaafkgdlgMLKKLVEDGV-ININERaDNGSTPMHKAAGQGHIE 312
Cdd:PHA02878 120 iLTNRYKNIQTIDLVYIDKKSKDDIIEAE----------------ITKLLLSYGAdINMKDR-HKGNTALHYATENKDQR 182
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 665821243 313 CLQWLIKMGADSNITNKAGERPSDVAKRFAHLAAVKLL 350
Cdd:PHA02878 183 LTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHIL 220
Ank_5 pfam13857
Ankyrin repeats (many copies);
150-199 9.29e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 9.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665821243  150 VDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLPVHLA 199
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
 
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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