NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039791295|ref|XP_017168526|]
View 

uncharacterized protein Potefam3c isoform X1 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-209 2.07e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:COG0666    90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791295 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 209
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 368-516 7.50e-08

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


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 55.69  E-value: 7.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 368 PTQSTCAADCRAPADAEPNSSTCAAVNGAPVNvepTPSQLAPHSGAPADVEPTTSQCAPDCEDP--AVIEPTHStcaADS 445
Cdd:pfam05109 449 PSSTHVPTNLTAPASTGPTVSTADVTSPTPAG---TTSGASPVTPSPSPRDNGTESKAPDMTSPtsAVTTPTPN---ATS 522

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039791295 446 RAPADIEPTPSQLAPDRGAPADVEP-THSTCAADTRIPADIEPSPSQCAPDSPAPSDIEQITSPCPSDSSES 516
Cdd:pfam05109 523 PTPAVTTPTPNATSPTLGKTSPTSAvTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPT 594
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-209 2.07e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:COG0666    90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791295 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 209
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
89-180 1.18e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.96  E-value: 1.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  89 LHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHnADPNLIDfSGNTALHHAISRGNLRIVK 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1039791295 169 MLLEHNVDIEAK 180
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-191 1.74e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.40  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  78 VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHH 157
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039791295 158 AISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 368-516 7.50e-08

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 55.69  E-value: 7.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 368 PTQSTCAADCRAPADAEPNSSTCAAVNGAPVNvepTPSQLAPHSGAPADVEPTTSQCAPDCEDP--AVIEPTHStcaADS 445
Cdd:pfam05109 449 PSSTHVPTNLTAPASTGPTVSTADVTSPTPAG---TTSGASPVTPSPSPRDNGTESKAPDMTSPtsAVTTPTPN---ATS 522

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039791295 446 RAPADIEPTPSQLAPDRGAPADVEP-THSTCAADTRIPADIEPSPSQCAPDSPAPSDIEQITSPCPSDSSES 516
Cdd:pfam05109 523 PTPAVTTPTPNATSPTLGKTSPTSAvTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPT 594
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 54-205 2.51e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLEN-----NSSINIRDDEGCTPLIKATQR 128
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 129 DNVDCASVLLTHNADP---------------NLIDFsGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQ-LAT 192
Cdd:cd22192   100 QNLNLVRELIARGADVvspratgtffrpgpkNLIYY-GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVL 178

                         170
                  ....*....|....*.
gi 1039791295 193 FEQKP---EMVEFLAA 205
Cdd:cd22192   179 QPNKTfacQMYDLILS 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 151-179 6.18e-07

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: 46.04  E-value: 6.18e-07
                           10        20
                   ....*....|....*....|....*....
gi 1039791295  151 GNTALHHAISRGNLRIVKMLLEHNVDIEA 179
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
374-532 3.13e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 47.15  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 374 AADCRAPADAEPNSSTCAAVNGAPVNVEPTPSQLAPhsGAPADVEPTTSQCAPDCEDPAVIEPTHSTCAADSRAPADIEP 453
Cdd:PRK07003  382 APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAA--AAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASA 459

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039791295 454 TPSQLAPDRGAPADVEPThSTCAADTRIPADIEPSPSQCAPDSPAPSDIEQitSPCPSDSSESDEkydLETGEEPSPVA 532
Cdd:PRK07003  460 DSRCDERDAQPPADSGSA-SAPASDAPPDAAFEPAPRAAAPSAATPAAVPD--ARAPAAASREDA---PAAAAPPAPEA 532
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 57-180 4.80e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 4.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  57 RAASVGDLDTTEKLIHSSQH-HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSiniRDDEGCTPLIKATQR--DNV-D 132
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKKlNINCPDRLGRSALFVAAIENENLELTELLLNLSC---RGAVGDTLLHAISLEyvDAVeA 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039791295 133 CASVLLTHNA---------DPNLIDFS-GNTALHHAISRGNLRIVKMLLEHNVDIEAK 180
Cdd:TIGR00870 100 ILLHLLAAFRksgplelanDQYTSEFTpGITALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-209 2.07e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:COG0666    90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791295 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 209
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-209 1.32e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:COG0666    56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791295 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAK 209
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-206 3.58e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 3.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIhssQHH--VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV 131
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLL---EAGadVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039791295 132 DCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAK 206
Cdd:COG0666   200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-208 6.15e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 6.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  55 LQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCA 134
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039791295 135 SVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCA 208
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
Ank_2 pfam12796
Ankyrin repeats (3 copies);
89-180 1.18e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.96  E-value: 1.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  89 LHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHnADPNLIDfSGNTALHHAISRGNLRIVK 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1039791295 169 MLLEHNVDIEAK 180
Cdd:pfam12796  79 LLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-188 8.97e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 8.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIhssQH--HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV 131
Cdd:COG0666   156 PLHLAAANGNLEIVKLLL---EAgaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039791295 132 DCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPL 188
Cdd:COG0666   233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-191 1.74e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.40  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  78 VDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHH 157
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039791295 158 AISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-206 2.55e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 2.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 122 LIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHnVDIEAKTeYGLTPLQLATFEQKPEMVE 201
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*
gi 1039791295 202 FLAAK 206
Cdd:pfam12796  79 LLLEK 83
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 68-203 3.90e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.95  E-value: 3.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  68 EKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPL-----IKATQRDNVDCASVLLTHNA 142
Cdd:PHA03100   18 IKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGA 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039791295 143 DPNLIDFSGNTALHHAISR--GNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKP--EMVEFL 203
Cdd:PHA03100   98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLL 162
Ank_2 pfam12796
Ankyrin repeats (3 copies);
55-148 5.45e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 5.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  55 LQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSsINIRDDeGCTPLIKATQRDNVDCA 134
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1039791295 135 SVLLTHNADPNLID 148
Cdd:pfam12796  78 KLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-206 9.37e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 9.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  70 LIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDF 149
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039791295 150 SGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAK 206
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_5 pfam13857
Ankyrin repeats (many copies);
137-191 1.37e-13

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 65.45  E-value: 1.37e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791295 137 LLTH-NADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 96-183 4.72e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 4.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  96 NHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNV 175
Cdd:PHA03100  170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                  ....*...
gi 1039791295 176 DIEAKTEY 183
Cdd:PHA03100  250 SIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 69-191 9.50e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 9.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  69 KLIHSSQHHVDESDRRK-RTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLI 147
Cdd:PHA02878  151 KLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR 230

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039791295 148 DFSGNTALHHAISR-GNLRIVKMLLEHNVDIEAKTE-YGLTPLQLA 191
Cdd:PHA02878  231 DKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSS 276
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-191 1.13e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  42 YPLYLIGYDP----IGPLQRAASVGDLDTTEKLIHSSQHH----------VDESDRRKRTSLHYACAHNHPD-----VVT 102
Cdd:PHA02878   72 TPLHIICKEPnklgMKEMIRSINKCSVFYTLVAIKDAFNNrnveifkiilTNRYKNIQTIDLVYIDKKSKDDiieaeITK 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 103 LLLENNSSINIRD-DEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKT 181
Cdd:PHA02878  152 LLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231

                         170
                  ....*....|
gi 1039791295 182 EYGLTPLQLA 191
Cdd:PHA02878  232 KCGNTPLHIS 241
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-191 1.34e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.29  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIhSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPL-IKATQRDNVD 132
Cdd:PHA02878  171 ALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYD 249

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 133 CASVLLTHNADPNLIDF-SGNTALHHAISrgNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:PHA02878  250 ILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 67-191 3.56e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 3.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  67 TEKLIHSSQHHVDESDRRKRTSLHYACAH--NHPDVVTLLLENNSSINIRDDEGCTPL---------------------I 123
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlylesnkidlkilkllidkgV 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039791295 124 KATQRDNVDCasvLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:PHA03100  168 DINAKNRVNY---LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 58-219 6.27e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.74  E-value: 6.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  58 AASVGDLDTTEKLIHSSQHhVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVL 137
Cdd:PLN03192  532 VASTGNAALLEELLKAKLD-PDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 138 --LTHNADPNlidfSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLA---AKCAKSSV 212
Cdd:PLN03192  611 yhFASISDPH----AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImngADVDKANT 686


                  ....*..
gi 1039791295 213 TPSWSPS 219
Cdd:PLN03192  687 DDDFSPT 693
PHA03095 PHA03095
ankyrin-like protein; Provisional
 99-206 6.45e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 6.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  99 DVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASV---LLTHNADPNLIDFSGNTALHHAISRGN-LRIVKMLLEHN 174
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039791295 175 VDIEAKTEYGLTPLQ--LATFEQKPEMVEFLAAK 206
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRK 141
PHA03095 PHA03095
ankyrin-like protein; Provisional
 78-205 1.02e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  78 VDESDRRKRTSLH-YACAHN-HPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASV--LLTHNADPNLIDFSGNT 153
Cdd:PHA03095  110 VNAKDKVGRTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAGADVYAVDDRFRS 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039791295 154 ALH-HAIS-RGNLRIVKMLLEHNVDIEAKTEYGLTPLQ-LATFE--QKPEMVEFLAA 205
Cdd:PHA03095  190 LLHhHLQSfKPRARIVRELIRAGCDPAATDMLGNTPLHsMATGSscKRSLVLPLLIA 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
86-138 4.32e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 4.32e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039791295  86 RTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLL 138
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-188 1.26e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.89  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  89 LHYACaHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV-DCASVLLTHNADPNLIDFSGNTALHHAISRGNLR-- 165
Cdd:PHA03095   55 LHYSS-EKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpk 133

                          90       100
                  ....*....|....*....|...
gi 1039791295 166 IVKMLLEHNVDIEAKTEYGLTPL 188
Cdd:PHA03095  134 VIRLLLRKGADVNALDLYGMTPL 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-218 1.66e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 1.66e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039791295 155 LHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAKSSVTPSWSP 218
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTA 64
PHA03095 PHA03095
ankyrin-like protein; Provisional
 82-179 2.11e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 2.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  82 DRRKRTSLHYACAHNHPD--VVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAI 159
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298

                          90       100
                  ....*....|....*....|
gi 1039791295 160 SRGNLRIVKMLLEHNVDIEA 179
Cdd:PHA03095  299 RNNNGRAVRAALAKNPSAET 318
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 54-212 3.17e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYG-LTPLQLATFEQKPEMVEFLAAKCAKSSV 212
Cdd:PHA02875  151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-203 8.78e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 8.78e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039791295 151 GNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFL 203
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-188 3.64e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  77 HVDESDRRKRTSLH-YACAHNHPDVVTLLLENNSSINIRDDEGCTPLIK--ATQRDNVDCASVLLTHNADPNLIDFSGNT 153
Cdd:PHA03095   75 DVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039791295 154 ALHHAISRGN--LRIVKMLLEHNVDIEAKTEYGLTPL 188
Cdd:PHA03095  155 PLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLL 191
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 86-220 4.48e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 4.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  86 RTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLR 165
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039791295 166 IVKMLLEHNV---DIEAKTeyGLTPLQLATFEQKPEMVEFLAAKCAKSSVTPSWSPSP 220
Cdd:PHA02875   83 AVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-115 6.12e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 6.12e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039791295  54 PLQRAASVGDLDTTEKLIhsSQHHVDESDRrKRTSLHYACAHNHPDVVTLLLENNSSINIRD 115
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
81-125 8.18e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 8.18e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1039791295  81 SDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKA 125
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 87-190 2.75e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  87 TSLHYACAHNHPDVVTLLLENNSSINIRDdegcTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNL-R 165
Cdd:PHA02876  213 SVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsR 288

                          90       100
                  ....*....|....*....|....*
gi 1039791295 166 IVKMLLEHNVDIEAKTEYGLTPLQL 190
Cdd:PHA02876  289 LVPKLLERGADVNAKNIKGETPLYL 313
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-201 3.07e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.51  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTeKLIHSSQHHVDESDRRKRTSLHYACAHNHpDVVTLLLeNNSSINIRDDEGCTPLIKATQRD-NVD 132
Cdd:PHA02874  193 PLHNAAEYGDYACI-KLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAINPPcDID 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 133 CASVLLTHNADPNLIDFSGNTALHHAISRGN-LRIVKMLLEHNVdieAKTEYGltPLQLATFEQKPEMVE 201
Cdd:PHA02874  270 IIDILLYHKADISIKDNKGENPIDTAFKYINkDPVIKDIIANAV---LIKEAD--KLKDSDFLEHIEIKD 334
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 77-148 4.85e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.83  E-value: 4.85e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039791295  77 HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLID 148
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-191 6.86e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 6.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIHSSqhhVDESdrrkrtSLHYACAHNhpDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDC 133
Cdd:PHA02874   71 PLLTAIKIGAHDIIKLLIDNG---VDTS------ILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLES 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039791295 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLA 191
Cdd:PHA02874  140 IKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNA 197
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 368-516 7.50e-08

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 55.69  E-value: 7.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 368 PTQSTCAADCRAPADAEPNSSTCAAVNGAPVNvepTPSQLAPHSGAPADVEPTTSQCAPDCEDP--AVIEPTHStcaADS 445
Cdd:pfam05109 449 PSSTHVPTNLTAPASTGPTVSTADVTSPTPAG---TTSGASPVTPSPSPRDNGTESKAPDMTSPtsAVTTPTPN---ATS 522

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039791295 446 RAPADIEPTPSQLAPDRGAPADVEP-THSTCAADTRIPADIEPSPSQCAPDSPAPSDIEQITSPCPSDSSES 516
Cdd:pfam05109 523 PTPAVTTPTPNATSPTLGKTSPTSAvTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPT 594
Ank_5 pfam13857
Ankyrin repeats (many copies);
104-158 7.63e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 7.63e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791295 104 LLENNS-SINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHA 158
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 134-211 9.92e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 9.92e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039791295 134 ASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLATFEQKPEMVEFLAAKCAKSS 211
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 54-205 2.51e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  54 PLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLLEN-----NSSINIRDDEGCTPLIKATQR 128
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 129 DNVDCASVLLTHNADP---------------NLIDFsGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQ-LAT 192
Cdd:cd22192   100 QNLNLVRELIARGADVvspratgtffrpgpkNLIYY-GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVL 178

                         170
                  ....*....|....*.
gi 1039791295 193 FEQKP---EMVEFLAA 205
Cdd:cd22192   179 QPNKTfacQMYDLILS 194
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 89-193 2.77e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 51.36  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  89 LHYACAHN---HPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNV--DCASVLLTHNADPNLIDFSGNTALH-HAISRG 162
Cdd:PHA02859   91 LHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVriNVIKLLIDSGVSFLNKDFDNNNILYsYILFHS 170

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039791295 163 NLRIVKMLLEHNVDIEAKTEYGLTPLQLATF 193
Cdd:PHA02859  171 DKKIFDFLTSLGIDINETNKSGYNCYDLIKF 201
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 151-179 6.18e-07

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: 46.04  E-value: 6.18e-07
                           10        20
                   ....*....|....*....|....*....
gi 1039791295  151 GNTALHHAISRGNLRIVKMLLEHNVDIEA 179
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 148-207 9.17e-07

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: 52.07  E-value: 9.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039791295 148 DFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTE--------------YGLTPLQLATFEQKPEMVEFLAAKC 207
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKE 211
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 151-182 1.30e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.97  E-value: 1.30e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1039791295 151 GNTALHHAISR-GNLRIVKMLLEHNVDIEAKTE 182
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 51-191 1.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  51 PIGPLQRAASVGDLDTTEKLIHSSQHHVDESDRRKRTSLHYAC-AHNHPDVV-TLLLENNSSINIRD----------DEG 118
Cdd:PHA02876   41 PFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICiIPNVMDIViSLTLDCDIILDIKYasiilnkhklDEA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 119 CTPLIKAT-------------------------QRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEH 173
Cdd:PHA02876  121 CIHILKEAisgndihydkinesieymklikeriQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200

                         170
                  ....*....|....*...
gi 1039791295 174 NVDIEAKTEYGLTPLQLA 191
Cdd:PHA02876  201 GADVNIIALDDLSVLECA 218
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 151-179 1.45e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 44.94  E-value: 1.45e-06
                          10        20
                  ....*....|....*....|....*....
gi 1039791295 151 GNTALHHAISRGNLRIVKMLLEHNVDIEA 179
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 80-174 1.59e-06

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 50.04  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  80 ESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEgcTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAI 159
Cdd:PHA02791   25 KADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAV 102

                          90
                  ....*....|....*
gi 1039791295 160 SRGNLRIVKMLLEHN 174
Cdd:PHA02791  103 DSGNMQTVKLFVKKN 117
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-199 2.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  55 LQRAASVGDLDTTeKLIHSSQHHVDESDRRKRTSLHYAC-AHNHPDVVTLLLENNSSINIRDDEGCTPL----------- 122
Cdd:PHA02876  244 LLKAIRNEDLETS-LLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLylmakngydte 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 123 -----------IKATQR-------------DNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDIE 178
Cdd:PHA02876  323 nirtlimlgadVNAADRlyitplhqastldRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402

                         170       180
                  ....*....|....*....|.
gi 1039791295 179 AKTEYGLTPLQLATFEQKPEM 199
Cdd:PHA02876  403 ALSQKIGTALHFALCGTNPYM 423
Ank_4 pfam13637
Ankyrin repeats (many copies);
54-105 2.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 2.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039791295  54 PLQRAASVGDLDTTeKLIHSSQHHVDESDRRKRTSLHYACAHNHPDVVTLLL 105
Cdd:pfam13637   4 ALHAAAASGHLELL-RLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 99-190 7.70e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.68  E-value: 7.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  99 DVVTLLLENNSSINIRDDEGCTPL--IKATQRD---NVDCASVLLTHNADPNLIDFSGNTALHHAISRG---NLRIVKML 170
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctILSNIKDykhMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFM 131

                          90       100
                  ....*....|....*....|
gi 1039791295 171 LEHNVDIEAKTEYGLTPLQL 190
Cdd:PHA02798  132 IENGADTTLLDKDGFTMLQV 151
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 86-116 2.19e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 2.19e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039791295  86 RTSLHYACAH-NHPDVVTLLLENNSSINIRDD 116
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 101-173 2.92e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.92e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039791295 101 VTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEH 173
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
374-532 3.13e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 47.15  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 374 AADCRAPADAEPNSSTCAAVNGAPVNVEPTPSQLAPhsGAPADVEPTTSQCAPDCEDPAVIEPTHSTCAADSRAPADIEP 453
Cdd:PRK07003  382 APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAA--AAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASA 459

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039791295 454 TPSQLAPDRGAPADVEPThSTCAADTRIPADIEPSPSQCAPDSPAPSDIEQitSPCPSDSSESDEkydLETGEEPSPVA 532
Cdd:PRK07003  460 DSRCDERDAQPPADSGSA-SAPASDAPPDAAFEPAPRAAAPSAATPAAVPD--ARAPAAASREDA---PAAAAPPAPEA 532
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 57-180 4.80e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 4.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  57 RAASVGDLDTTEKLIHSSQH-HVDESDRRKRTSLHYACAHNHPDVVTLLLENNSSiniRDDEGCTPLIKATQR--DNV-D 132
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKKlNINCPDRLGRSALFVAAIENENLELTELLLNLSC---RGAVGDTLLHAISLEyvDAVeA 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039791295 133 CASVLLTHNA---------DPNLIDFS-GNTALHHAISRGNLRIVKMLLEHNVDIEAK 180
Cdd:TIGR00870 100 ILLHLLAAFRksgplelanDQYTSEFTpGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
342-532 4.81e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.41  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 342 GNKPPIFRPFPRKHRIHVLEAPGDIEPTQSTCAAdcrAPADAEPNSSTCAAVNGAPVNVEPTPSQLAPHSGAPADVEPTT 421
Cdd:PRK12323  371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPA---APAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGA 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 422 SqcAPDCEDPAVIEPTHSTCAADSRAPAdieptpsqlAPDRGAPADVEPTHSTCAADTRIPAdIEPSPSQCAPDSP---- 497
Cdd:PRK12323  448 P--APAPAPAAAPAAAARPAAAGPRPVA---------AAAAAAPARAAPAAAPAPADDDPPP-WEELPPEFASPAPaqpd 515

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039791295 498 -APSDIEQITSPCPSDSSESDEKYDLETGEEPSPVA 532
Cdd:PRK12323  516 aAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAP 551
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 86-113 5.04e-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: 5.04e-05
                           10        20
                   ....*....|....*....|....*...
gi 1039791295   86 RTSLHYACAHNHPDVVTLLLENNSSINI 113
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 100-177 6.82e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 6.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039791295 100 VVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDI 177
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
PHA02798 PHA02798
ankyrin-like protein; Provisional
 99-177 7.57e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.60  E-value: 7.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  99 DVVTLLLENNSSINIRDDEGCTP---LIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGN---LRIVKMLLE 172
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPlycLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLE 169


                  ....*
gi 1039791295 173 HNVDI 177
Cdd:PHA02798  170 KGVDI 174
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 359-523 1.09e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  359 VLEAPGDIEPTQSTCAADCRAPADAEPNSSTCAAVNGAPvnvEPTPSqlAPHSGAPADVEPTTSQCAPDCEDPAVIEPTH 438
Cdd:PHA03307    76 GTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSP---DPPPP--TPPPASPPPSPAPDLSEMLRPVGSPGPPPAA 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  439 STCAA--DSRAPADIEPTPSQLAPdrgaPADVEPTHSTCAADTRIPADIEPSPSQCAPDSPAPSDIEQITSPCPSDSSES 516
Cdd:PHA03307   151 SPPAAgaSPAAVASDAASSRQAAL----PLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR 226


                   ....*..
gi 1039791295  517 DEKYDLE 523
Cdd:PHA03307   227 SAADDAG 233
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
345-534 1.44e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 345 PPIFRPFPRKHRIHVLEAPGDIEPTQSTCAADCRAPADAEPNSSTCAAVNGAPVNV-EPTPSQLA-PHSGAPADVEPTTS 422
Cdd:PRK12323  392 PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGApAPAPAPAAaPAAAARPAAAGPRP 471

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 423 QCAPDCEDPAVIEPTHSTCAADSRAPA--DIEPTPSQLAPDRGAPA----DVEPTHSTCAADTRIPADIEPSPSQCAPDS 496
Cdd:PRK12323  472 VAAAAAAAPARAAPAAAPAPADDDPPPweELPPEFASPAPAQPDAApagwVAESIPDPATADPDDAFETLAPAPAAAPAP 551

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039791295 497 PAPSDIEQITSPCPSDSSEsDEKYDLETGEEPSPVADL 534
Cdd:PRK12323  552 RAAAATEPVVAPRPPRASA-SGLPDMFDGDWPALAARL 588
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 86-113 2.10e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 2.10e-04
                          10        20
                  ....*....|....*....|....*...
gi 1039791295  86 RTSLHYACAHNHPDVVTLLLENNSSINI 113
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 100-188 2.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 43.96  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 100 VVTLLLENNSSINIRDDEGCTPL---IKATQRDNVDCASVLLTHNADPN-LIDFSGNTALHHAISRGNLR--IVKMLLEH 173
Cdd:PHA02989   90 IVKLLLKFGADINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVNdVKNSRGYNLLHMYLESFSVKkdVIKILLSF 169

                          90
                  ....*....|....*.
gi 1039791295 174 NVDIEAKTE-YGLTPL 188
Cdd:PHA02989  170 GVNLFEKTSlYGLTPM 185
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
374-498 2.47e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.07  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 374 AADCRAPADAEPNSSTCAAVNGAPVNVEPTPSQLAPHSGAPADVEPTTSQCAPDCEDPAVIEPThSTCAADSRAPADIEP 453
Cdd:PRK07003  414 AAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSA-SAPASDAPPDAAFEP 492

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039791295 454 TPSQLAP-DRGAPADVEPTHSTCAADTRIPADIEPSPSQCAPDSPA 498
Cdd:PRK07003  493 APRAAAPsAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPA 538
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 111-176 2.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 2.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791295 111 INIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVD 176
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 79-140 2.82e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 2.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039791295  79 DESDRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTH 140
Cdd:PTZ00322  109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 149-203 3.87e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.63  E-value: 3.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039791295 149 FSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTE--------------YGLTPLQLATFEQKPEMVEFL 203
Cdd:cd22193    74 YEGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYL 142
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 368-516 3.88e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.75  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 368 PTQSTCAADCRAPADAEPNSSTcaavnGAPVNVEPTPSQLAPHSGAP----ADVEPTTSQCAPDCEDPAVIEPTHSTCAA 443
Cdd:pfam05109 425 PESTTTSPTLNTTGFAAPNTTT-----GLPSSTHVPTNLTAPASTGPtvstADVTSPTPAGTTSGASPVTPSPSPRDNGT 499

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039791295 444 DSRAPADIEPTPSQLAPdrgAPADVEPThstcaadtriPADIEPSPSQCAPDSPAPSDIEQITSPCPSDSSES 516
Cdd:pfam05109 500 ESKAPDMTSPTSAVTTP---TPNATSPT----------PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT 559
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 86-206 5.26e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  86 RTSLHYACAHNHPDVVTLLLENNSSINIR------DDEGCT-------PLIKATQRDNVDCASVLLTHNADPNLI---DF 149
Cdd:cd21882    74 QTALHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALeaqDS 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039791295 150 SGNTALHHAISRGN---------------LRIVKMLLEHNVDIEAKTEY-GLTPLQLATFEQKPEMVEFLAAK 206
Cdd:cd21882   154 LGNTVLHALVLQADntpensafvcqmynlLLSYGAHLDPTQQLEEIPNHqGLTPLKLAAVEGKIVMFQHILQR 226
PHA03247 PHA03247
large tegument protein UL36; Provisional
 345-499 5.64e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 5.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  345 PPIFRPFPRKHRIhVLEAPGDIEPTQSTCAADCRAPADAEPNSSTCAAVNGAPVNVEPTPSQLAPHSGAPADVEPTTSqc 424
Cdd:PHA03247  2703 PPPPTPEPAPHAL-VSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP-- 2779

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039791295  425 apdcedPAVIEPTHSTCAADSRAPADIEPTPSQLAPDRGAPADVEPTHSTcaadtriPADIEPSPSQCAPDSPAP 499
Cdd:PHA03247  2780 ------PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS-------PAGPLPPPTSAQPTAPPP 2841
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 362-516 6.06e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.98  E-value: 6.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 362 APGDIEPTQSTCAADCRAPADAEPNSS----TCAAVNGAPVNVEPTPSQLAPHSG----APADVEPTTSQCAPDcedPAV 433
Cdd:pfam05109 486 SPVTPSPSPRDNGTESKAPDMTSPTSAvttpTPNATSPTPAVTTPTPNATSPTLGktspTSAVTTPTPNATSPT---PAV 562

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 434 IEPTHS----TCAADSRAPADIEPTPSQLAPDRGAPA-DVEPTHSTCAADTRIPADIEP---------------SPSQCA 493
Cdd:pfam05109 563 TTPTPNatipTLGKTSPTSAVTTPTPNATSPTVGETSpQANTTNHTLGGTSSTPVVTSPpknatsavttgqhniTSSSTS 642

                         170       180
                  ....*....|....*....|...
gi 1039791295 494 PDSPAPSDIEQITSPCPSDSSES 516
Cdd:pfam05109 643 SMSLRPSSISETLSPSTSDNSTS 665
PHA03247 PHA03247
large tegument protein UL36; Provisional
 362-530 7.03e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 7.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  362 APGDIEPTQSTCAADCRAPADAEPNSSTCAAVN-GAPVNVEPTPSQLAPHSGAPAdvEPTTSQCApdceDPAViepthst 440
Cdd:PHA03247  2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVApGGDVRRRPPSRSPAAKPAAPA--RPPVRRLA----RPAV------- 2891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  441 caadSRAPADIEPTPSQLAPDRGAPADVEPTHSTCAADTRIPADIEPSPSQcaPDSPAPSDIEQITSPCPSDSSESDEKY 520
Cdd:PHA03247  2892 ----SRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR--PQPPLAPTTDPAGAGEPSGAVPQPWLG 2965

                          170
                   ....*....|
gi 1039791295  521 DLETGEEPSP 530
Cdd:PHA03247  2966 ALVPGRVAVP 2975
PHA03247 PHA03247
large tegument protein UL36; Provisional
 369-532 7.33e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 7.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  369 TQSTCAADCRAPADAEPNSSTCAAVNGAPvnvepTPSQLAPHSGAPADVEPTTSQCAPDCEDPAVIEPTHSTCAADSRAP 448
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAPPAAPAAG-----PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  449 ADIEPTP--SQLAPDRGAPADVEPTHSTCAA-----DTRIPADIEPSPSQcaPDSPAPSDIEQITSPCPSDSSESDEKYD 521
Cdd:PHA03247  2825 AGPLPPPtsAQPTAPPPPPGPPPPSLPLGGSvapggDVRRRPPSRSPAAK--PAAPARPPVRRLARPAVSRSTESFALPP 2902

                          170
                   ....*....|.
gi 1039791295  522 LETGEEPSPVA 532
Cdd:PHA03247  2903 DQPERPPQPQA 2913
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-214 9.76e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.31  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 120 TPLIKATQRDNVDCASVLLT-HNADPNLIDFSGNTALHHAISRGNLRIVKMLLEH-----NVDIEAKTEYGLTPLQLATF 193
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVV 98

                          90       100
                  ....*....|....*....|.
gi 1039791295 194 EQKPEMVEFLAAKCAkSSVTP 214
Cdd:cd22192    99 NQNLNLVRELIARGA-DVVSP 118
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 118-203 9.85e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 9.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 118 GCTPLIKATQRDN---VDCASVLLthNADPNLID-------------FSGNTALHHAISRGNLRIVKMLLEHNVDIEAKT 181
Cdd:cd21882    26 GKTCLHKAALNLNdgvNEAIMLLL--EAAPDSGNpkelvnapctdefYQGQTALHIAIENRNLNLVRLLVENGADVSARA 103

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039791295 182 E-------------YGLTPLQLATFEQKPEMVEFL 203
Cdd:cd21882   104 TgrffrkspgnlfyFGELPLSLAACTNQEEIVRLL 138
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 149-203 1.10e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.10  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039791295 149 FSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTE--------------YGLTPLQLATFEQKPEMVEFL 203
Cdd:cd22196    92 YKGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFL 160
PHA02917 PHA02917
ankyrin-like protein; Provisional
 82-140 1.10e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 41.91  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  82 DRRKRTSLHYACAHNHPDVVTLLLENNSSINIRDDEGCTPL-IKATQRDNVDCASVLLTH 140
Cdd:PHA02917  449 DKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIaIAINESRNIELLKMLLCH 508
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 110-172 1.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.65  E-value: 1.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039791295 110 SINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLE 172
Cdd:PHA02989  248 KINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 404-514 1.60e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 404 PSQLAPHSGAPADVEPTTSQCAPdcEDPAVIEPTHSTCAADSRAPADIEPTPSQLAPdRGAPADVEPThstcAADTRIPA 483
Cdd:PRK14951  371 EAAAPAEKKTPARPEAAAPAAAP--VAQAAAAPAPAAAPAAAASAPAAPPAAAPPAP-VAAPAAAAPA----AAPAAAPA 443

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039791295 484 DIEPSPSQCAPDSPAPSDIEQITSPCPSDSS 514
Cdd:PRK14951  444 AVALAPAPPAQAAPETVAIPVRVAPEPAVAS 474
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
343-550 1.78e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 343 NKPPIFRPFPRKHRIHVLEAPGDIEPTQStcAADCRAPADAEPNSSTCAAVNGAPVNVEPTPSQ--LAPHSGAPADVEPT 420
Cdd:PRK07003  423 AEAPPAAPAPPATADRGDDAADGDAPVPA--KANARASADSRCDERDAQPPADSGSASAPASDAppDAAFEPAPRAAAPS 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 421 --TSQCAPDCEDPAVIEPTHSTCAADSRAPADIEPTPSQLAPDR---GAPADVEPTHStcaADTRIPAD--------IEP 487
Cdd:PRK07003  501 aaTPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAAragGAAAALDVLRN---AGMRVSSDrgaraaaaAKP 577

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 488 SPSQCAPDSPAPSdieQITSPCPSDSSESDEKYDLETGEEPSPVADLD-------EDIAEDFYDALeSAD 550
Cdd:PRK07003  578 AAAPAAAPKPAAP---RVAVQVPTPRARAATGDAPPNGAARAEQAAESrgapppwEDIPPDDYVPL-SAD 643
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 361-529 2.28e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 40.73  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 361 EAPGDIEPTQStcAADcrAPADAEPNSSTCAAVNGAPVNVEP----TPSQlaPHSGAPADVEPTTSQCAPDCEDPAVIEP 436
Cdd:PRK13108  280 EAPGALRGSEY--VVD--EALEREPAELAAAAVASAASAVGPvgpgEPNQ--PDDVAEAVKAEVAEVTDEVAAESVVQVA 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 437 T---HSTCAADSRAPADIE-PTPSQLAPDRGAPADVEPTHSTcAADTRiPADIEPSpsqcAPDSPAPSDIEqiTSPCPSD 512
Cdd:PRK13108  354 DrdgESTPAVEETSEADIErEQPGDLAGQAPAAHQVDAEAAS-AAPEE-PAALASE----AHDETEPEVPE--KAAPIPD 425

                         170
                  ....*....|....*..
gi 1039791295 513 SSESDEKYDLETGEEPS 529
Cdd:PRK13108  426 PAKPDELAVAGPGDDPA 442
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 402-499 2.92e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.82  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 402 PTPSQLAPHSGAPAdvepttSQCAPDCEDPAVIEPthstcaADSRAPA----DIEPTPSQLA-PDRGAPADVEPTHSTCA 476
Cdd:PRK14959  398 PTPGTQGPQGTAPA------AGMTPSSAAPATPAP------SAAPSPRvpwdDAPPAPPRSGiPPRPAPRMPEASPVPGA 465

                          90       100
                  ....*....|....*....|...
gi 1039791295 477 ADTrIPADIEPSPSQCAPDSPAP 499
Cdd:PRK14959  466 PDS-VASASDAPPTLGDPSDTAE 487
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 120-192 4.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 4.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039791295 120 TPLIKATQRDNVDCASVLLTHNADPN-LIDFSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTEYGLTPLQLAT 192
Cdd:PHA02884   72 NPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAL 145
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 99-188 4.43e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.28  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  99 DVVTLLLENNSSINIRDDEGCTPLIKATQRDNV--DCASVLLTHNADPNLIDFSGNTALHHAISRG-------------- 162
Cdd:PHA02716  298 SVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdndi 377

                          90       100
                  ....*....|....*....|....*.
gi 1039791295 163 NLRIVKMLLEHNVDIEAKTEYGLTPL 188
Cdd:PHA02716  378 RLDVIQCLISLGADITAVNCLGYTPL 403
PHA02946 PHA02946
ankyin-like protein; Provisional
 89-192 5.68e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  89 LHYACAHNHPD--VVTLLLENNSSINIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRI 166
Cdd:PHA02946   41 LHAYCGIKGLDerFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVI 120

                          90       100
                  ....*....|....*....|....*....
gi 1039791295 167 --VKMLLEHNVDIEAKT-EYGLTPLQLAT 192
Cdd:PHA02946  121 erINLLVQYGAKINNSVdEEGCGPLLACT 149
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 117-146 6.46e-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: 34.49  E-value: 6.46e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039791295  117 EGCTPLIKATQRDNVDCASVLLTHNADPNL 146
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 80-203 9.14e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 39.07  E-value: 9.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295  80 ESDRRKRTSLHYACAHNHPDVVTLLLE--NNSSINIRDDE------GCTPLIKA--TQRDNVD-CASVLLTHNADPN--- 145
Cdd:cd22197     1 DPNRFDRDRLFSVVSRGNPEELAGLLEylRRTSKYLTDSEytegstGKTCLMKAvlNLQDGVNaCIMPLLEIDKDSGnpk 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039791295 146 -LID-------FSGNTALHHAISRGNLRIVKMLLEHNVDIEAKTE-------------YGLTPLQLATFEQKPEMVEFL 203
Cdd:cd22197    81 pLVNaqctdeyYRGHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYL 159
PHA02798 PHA02798
ankyrin-like protein; Provisional
 111-177 9.72e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.05  E-value: 9.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039791295 111 INIRDDEGCTPLIKATQRDNVDCASVLLTHNADPNLIDFSGNTALHHAISRGNLRIVKMLLEHNVDI 177
Cdd:PHA02798  251 INQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNK 317
PHA03378 PHA03378
EBNA-3B; Provisional
 365-499 9.77e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.28  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 365 DIEPTQSTCAADCRAPADAEP-NSSTCAAVNGAPVNVEP---TPSQLAPHSGAPADVEPTTSQCAPDCEDPAVIEPTHST 440
Cdd:PHA03378  658 EITPYKPTWTQIGHIPYQPSPtGANTMLPIQWAPGTMQPpprAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPP 737

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791295 441 CAADSRAPADiEPTPSQLAPDRGAPADVEPTHSTCAADTRI-PADIEPSPSQCAPDSPAP 499
Cdd:PHA03378  738 AAAPGRARPP-AAAPGRARPPAAAPGRARPPAAAPGAPTPQpPPQAPPAPQQRPRGAPTP 796
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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