|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
18-307 |
2.58e-62 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 215.20 E-value: 2.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 18 IPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCGANL 97
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 98 EHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGlQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVW 177
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 178 AARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLL 257
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907089607 258 DAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 307
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
16-274 |
5.78e-60 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 208.27 E-value: 5.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 16 ENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCGA 95
Cdd:COG0666 32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 96 NLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGlQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPL 175
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 176 VWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQD 255
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
250
....*....|....*....
gi 1907089607 256 LLDAGTYVNIPDRSGDTVL 274
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
84-373 |
7.54e-58 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 202.11 E-value: 7.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 84 IHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQYSvYPIIWAAGRGHADIVHLLLQNGAK 163
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGA-LLLLAAALAGDLLVALLLLAAGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 164 VNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMI 243
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 244 ASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDIL 323
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907089607 324 QCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPL 373
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
10-241 |
1.28e-57 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 201.72 E-value: 1.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 10 INYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEE 89
Cdd:COG0666 59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 90 LLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGlQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDK 169
Cdd:COG0666 139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907089607 170 YGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTAL 241
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| KAP_NTPase |
pfam07693 |
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases ... |
441-954 |
1.89e-57 |
|
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases are sporadically distributed across a wide phylogenetic range in bacteria and in animals. Many of the prokaryotic KAP NTPases are encoded in plasmids and tend to undergo disruption to form pseudogenes. A unique feature of all eukaryotic and certain bacterial KAP NTPases is the presence of two or four transmembrane helices inserted into the P-loop NTPase domain. These transmembrane helices anchor KAP NTPases in the membrane such that the P-loop domain is located on the intracellular side.
Pssm-ID: 462231 Cd Length: 293 Bit Score: 201.07 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 441 YDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFagqqieplfqfswlivflilllcgglglvfaft 520
Cdd:pfam07693 1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 521 vdtnlaiavslsflallyiffiviyfggrqegeswnwawalstrlarhigylellfklmfvnppelpeqttkalPVRFLF 600
Cdd:pfam07693 48 --------------------------------------------------------------------------NEEFII 53
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 601 TDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDSQGKKK--WKKTCCLPSFIIFLFIVGciiagitll 678
Cdd:pfam07693 54 VYFNPWSFSGQDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKigLIFGVAIILALTGLVVAI--------- 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 679 aifrvdpkhltvnailisiasivglafvlncrtwwqvldsllnsqrkrlhsaasklhklksEGFMKVLKCEV-ELMARMA 757
Cdd:pfam07693 125 -------------------------------------------------------------EEPMKKLQTEIeELRSDIE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 758 KTIDSftqNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLrdsNINGHDYMRN 837
Cdd:pfam07693 144 STLKD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPNVVFILAADEEILKKALEANYESGL---EIDGQKYLEK 217
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 838 IVHLPVFLNSRGLSNARKFLVTSAtngdiscseatgvqedadrrvsQNSLGEMTKLGSKTALnrrdtyrrrqmqrtitrq 917
Cdd:pfam07693 218 IIQVPFTLPPLSLRQLKKFLMLSF----------------------DNSEEGTSSKDRDETL------------------ 257
|
490 500 510
....*....|....*....|....*....|....*..
gi 1907089607 918 MSFDLTKLLVTEDwFSDISPQTMRRLLNIVSVTGRLL 954
Cdd:pfam07693 258 RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
122-394 |
9.09e-56 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 196.33 E-value: 9.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 122 LLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEG 201
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 202 ANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGG 281
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 282 HVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAR 361
Cdd:COG0666 165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
|
250 260 270
....*....|....*....|....*....|...
gi 1907089607 362 VSAVDKKGDTPLHVAIRGRSRRLAELLLRNPKD 394
Cdd:COG0666 245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
151-415 |
5.19e-53 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 188.24 E-value: 5.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 151 ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 230
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 231 NLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWA 310
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 311 VEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLLr 390
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL- 239
|
250 260
....*....|....*....|....*
gi 1907089607 391 npKDGRLLYRPNKAGETPYNIDCSH 415
Cdd:COG0666 240 --EAGADLNAKDKDGLTALLLAAAA 262
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
42-133 |
2.64e-27 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 107.12 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 42 LMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCgANLEHRDMgGWTALMWACYKGRTDVVE 121
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1907089607 122 LLLSHGANPSVT 133
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
49-378 |
3.78e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 116.60 E-value: 3.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 49 GNVEIVKELIKNGANC-NLEDLDNWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHG 127
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCiNISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 128 ANPSVTGLqysvyPIIwaagrgHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmta 207
Cdd:PHA02874 92 VDTSILPI-----PCI------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 208 livavkggytqsvkeilkrnpnVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVR 287
Cdd:PHA02874 150 ----------------------VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 288 ALLQKYADIDIRGQDNKTALYWAVEKGNATMvrDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGARVSAVD 366
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKD 285
|
330
....*....|..
gi 1907089607 367 KKGDTPLHVAIR 378
Cdd:PHA02874 286 NKGENPIDTAFK 297
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
2-400 |
8.54e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 115.16 E-value: 8.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 2 SVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKE 81
Cdd:PHA02876 142 SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 82 GHIHIVEELLKCGANLEHRDMGGWTALmwacykgrtdvvelllshganpSVTGLQYSVypiiwaagrghadivhLLLQNG 161
Cdd:PHA02876 222 KNIDTIKAIIDNRSNINKNDLSLLKAI----------------------RNEDLETSL----------------LLYDAG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 162 AKVNCSDKYGTTPLVWAARKGHL-ECVKHLLAMGADVDQEGANSMTALIVAVKGGY-TQSVKEILKRNPNVNLTDKDGNT 239
Cdd:PHA02876 264 FSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYIT 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 240 ALMIASK-EGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATM 318
Cdd:PHA02876 344 PLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYM 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 319 -VRDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSrrLAELLLR---NPK 393
Cdd:PHA02876 424 sVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHygaELR 501
|
....*..
gi 1907089607 394 DGRLLYR 400
Cdd:PHA02876 502 DSRVLHK 508
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
43-362 |
2.22e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 108.96 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 43 MIAAEQGNVEIVKELIKNGANCNLEDLDNWTAL---ISASKEGHIHIVEELLKCGANLEHRDMGGWTAL-MWACYKGRTD 118
Cdd:PHA03095 19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 119 VVELLLSHGANPSVTGLqYSVYPI-IWAAG-RGHADIVHLLLQNGAKVNCSDKYGTTPL-VWAARKG-HLECVKHLLAMG 194
Cdd:PHA03095 99 VIKLLIKAGADVNAKDK-VGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNaNVELLRLLIDAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 195 ADVDQEGANSMTAL---IVAVKgGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIE--IVQDLLDAGTYVNIPDRS 269
Cdd:PHA03095 178 ADVYAVDDRFRSLLhhhLQSFK-PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 270 GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTE-------ICTKDGETPLIK 342
Cdd:PHA03095 257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAEtvaatlnTASVAGGDIPSD 336
|
330 340
....*....|....*....|
gi 1907089607 343 ATKmrnIEVVELLLDKGARV 362
Cdd:PHA03095 337 ATR---LCVAKVVLRGAFSL 353
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
153-403 |
3.14e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 107.83 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 153 IVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQS-VKEI----LKRN 227
Cdd:PHA03100 17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdVKEIvkllLEYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 228 PNVNLTDKDGNTALMIAS--KEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHV--EIVRALLQKYADIDIrgqdn 303
Cdd:PHA03100 97 ANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 304 KTALYWAVEKGNATMVRDILqcnpdteictkdGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRR 383
Cdd:PHA03100 172 KNRVNYLLSYGVPINIKDVY------------GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
250 260
....*....|....*....|....*
gi 1907089607 384 LAELLLRN-----PKDGRLLYRPNK 403
Cdd:PHA03100 240 IFKLLLNNgpsikTIIETLLYFKDK 264
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
40-279 |
6.68e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 103.89 E-value: 6.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 40 TPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEEL-----------------------LKCGAN 96
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 97 LEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQySVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLV 176
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 177 WAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKggYTQSVKEILKRNPNVNLTDKDGNTALMIA-SKEGHIEIVQD 255
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDI 273
|
250 260
....*....|....*....|....
gi 1907089607 256 LLDAGTYVNIPDRSGDTVLIGAVR 279
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTAFK 297
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
12-264 |
1.81e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 102.44 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 12 YVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQG-----NVEIVKELIKNGANCNLEDLDNWTALISAS--KEGHI 84
Cdd:PHA03100 42 AKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 85 HIVEELLKCGANLEHRDMGGWTALMWA--CYKGRTDVVELLLSHGANPSVTglqysvypiiwaagrghaDIVHLLLQNGA 162
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAK------------------NRVNYLLSYGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 163 KVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN--------LTD 234
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKtiietllyFKD 263
|
250 260 270
....*....|....*....|....*....|
gi 1907089607 235 KDGNTALMIASKEGHIEIVQdLLDAGTYVN 264
Cdd:PHA03100 264 KDLNTITKIKMLKKSIMYMF-LLDPGFYKN 292
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
175-267 |
2.09e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 93.26 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 175 LVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKrNPNVNLTDkDGNTALMIASKEGHIEIVQ 254
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1907089607 255 DLLDAGTYVNIPD 267
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
113-411 |
4.76e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 101.19 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 113 YKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLA 192
Cdd:PHA02874 10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 193 MGADVDqegansmtalIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDT 272
Cdd:PHA02874 90 NGVDTS----------ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 273 VLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATkMRNIEVV 352
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 353 ELLLDKgARVSAVDKKGDTPLHVAIRGR-SRRLAELLLRNPKDgrLLYRPNKaGETPYNI 411
Cdd:PHA02874 239 ELLINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKAD--ISIKDNK-GENPIDT 294
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
108-199 |
3.44e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 89.79 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 108 LMWACYKGRTDVVELLLSHGANPSVTgLQYSVYPIIWAAGRGHADIVHLLLQNgAKVNCSDkYGTTPLVWAARKGHLECV 187
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|..
gi 1907089607 188 KHLLAMGADVDQ 199
Cdd:pfam12796 78 KLLLEKGADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
13-101 |
8.57e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.63 E-value: 8.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNgANCNLEDlDNWTALISASKEGHIHIVEELLK 92
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 1907089607 93 CGANLEHRD 101
Cdd:pfam12796 83 KGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
208-299 |
4.35e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 208 LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTyVNIPDrSGDTVLIGAVRGGHVEIVR 287
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1907089607 288 ALLQKYADIDIR 299
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
274-366 |
8.38e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.86 E-value: 8.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 274 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRdILQCNPDTEICTkDGETPLIKATKMRNIEVVE 353
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1907089607 354 LLLDKGARVSAVD 366
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
241-335 |
1.30e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.09 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 241 LMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLqKYADIDIRGqDNKTALYWAVEKGNATMVR 320
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|....*
gi 1907089607 321 DILQCNPDteICTKD 335
Cdd:pfam12796 79 LLLEKGAD--INVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
18-307 |
2.09e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 90.47 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 18 IPALKALLEKCKDVDERNECGQTPLMI--AAEQGNVEIVKELIKNGANCNLEDLDNWT---ALISaSKEGHIHIVEELLK 92
Cdd:PHA03095 97 LDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLK-SRNANVELLRLLID 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 93 CGANLEHRDMGGWTALMWAC--YKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHL-LLQNGAKVNCSDK 169
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLpLLIAGISINARNR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 170 YGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKdgntALMIASKEGH 249
Cdd:PHA03095 256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGG 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907089607 250 IEIVQDLLDAGTYVNIpdRSGDTVLIGAVRGGHVEIVRALLQKYADI-DIRGQDNKTAL 307
Cdd:PHA03095 332 DIPSDATRLCVAKVVL--RGAFSLLPEPIRAYHADFIRECEAEIAVMrTTRIGTGVSLL 388
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
182-399 |
2.33e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 89.67 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 182 GHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRN--PNVNLTDKDgnTALMIASKEGHIEIVQDLLDA 259
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGaiPDVKYPDIE--SELHDAVEEGDVKAVEELLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 260 GTYVN-IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGET 338
Cdd:PHA02875 91 GKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907089607 339 PLIKATKMRNIEVVELLLDKGARVSAVDKKGD-TPLHVAIRGRSRRLAELLLRNPKDGRLLY 399
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
74-298 |
4.08e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 88.89 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 74 ALISASKEGHIHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTglqysvYPIIW-----AAGR 148
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVK------YPDIEselhdAVEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 149 GHADIVHLLLQNGAKVN-CSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRN 227
Cdd:PHA02875 79 GDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907089607 228 PNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGD-TVLIGAVRGGHVEIVRALLQKYADIDI 298
Cdd:PHA02875 159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
220-390 |
1.04e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.08 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 220 VKEILKRNPNVNLTDKDGNTAL---MIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVE-IVRALLQKYAD 295
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 296 IDIRGQDNKTAL--YWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGARVSAVDKKGDT 371
Cdd:PHA03095 110 VNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRS 189
|
170 180
....*....|....*....|..
gi 1907089607 372 PLH---VAIRGRSRRLAELLLR 390
Cdd:PHA03095 190 LLHhhlQSFKPRARIVRELIRA 211
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
204-436 |
4.74e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 82.70 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 204 SMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAG---TYVNIPDRSGDTVligavrg 280
Cdd:PHA02874 35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtSILPIPCIEKDMI------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 281 ghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGA 360
Cdd:PHA02874 108 ------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089607 361 RVSAVDKKGDTPLHVAIRGRSRRLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSILTQIFGARHLSPTETDG 436
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDH---GNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDG 254
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
307-394 |
7.71e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.38 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 307 LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGArvSAVDKKGDTPLHVAIRGRSRRLAE 386
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
....*...
gi 1907089607 387 LLLRNPKD 394
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-232 |
2.84e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 80.04 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 38 GQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCGA---NLEHRDmgGWTALMWACYK 114
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATIL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 115 GRTDVVELLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMG 194
Cdd:PHA02875 113 KKLDIMKLLIARGADPDIPNTDKFS-PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907089607 195 ADVDQEGAN-SMTALIVAVKGGYTQSVKEILKRNPNVNL 232
Cdd:PHA02875 192 ANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
31-257 |
1.05e-14 |
|
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: 79.67 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 31 VDERNECGQ-----TPLMIAAEQGNVEIVKELIKNgancnlEDLDNW-------TALISASKEGHIHIVEELLKCGANLE 98
Cdd:cd22192 5 LDELHLLQQkriseSPLLLAAKENDVQAIKKLLKC------PSCDLFqrgalgeTALHVAALYDNLEAAVVLMEAAPELV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 99 HRDMG-----GWTALMWACYKGRTDVVELLLSHGA---NPSVTG----------LQYSVYPIIWAAGRGHADIVHLLLQN 160
Cdd:cd22192 79 NEPMTsdlyqGETALHIAVVNQNLNLVRELIARGAdvvSPRATGtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 161 GAKVNCSDKYGTTPLvwaarkghlecvkHLLAMGAdvDQEGANSMTALIVA-VKGGYTQSVKEIlkrnPNvnltdKDGNT 239
Cdd:cd22192 159 GADIRAQDSLGNTVL-------------HILVLQP--NKTFACQMYDLILSyDKEDDLQPLDLV----PN-----NQGLT 214
|
250
....*....|....*...
gi 1907089607 240 ALMIASKEGHIEIVQDLL 257
Cdd:cd22192 215 PFKLAAKEGNIVMFQHLV 232
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
13-230 |
1.07e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.49 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 13 VEEENIPALKALLEKCKDVDER-NECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELL 91
Cdd:PHA02875 76 VEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 92 KCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVN----CS 167
Cdd:PHA02875 156 DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNimfmIE 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907089607 168 DKYGTTplvwaarkghLECVKHllaMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 230
Cdd:PHA02875 236 GEECTI----------LDMICN---MCTNLESEAIDALIADIAIRIHKKTIRRDEGFKNNMST 285
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
41-352 |
1.70e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 71.83 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 41 PLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLkcgANLEHRDMG-GWTALMWACYKGRTDV 119
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFyTLVAIKDAFNNRNVEI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 120 VE-LLLSHGANPSVTGLQY----SVYPIIwaagrgHADIVHLLLQNGAKVNCSDKY-GTTPLVWAARKGHLECVKHLLAM 193
Cdd:PHA02878 117 FKiILTNRYKNIQTIDLVYidkkSKDDII------EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 194 GADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKE-GHIEIVQDLLDAGTYVNIPDR-SGD 271
Cdd:PHA02878 191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 272 TVLIGAVRGGHVeiVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNpdteICTKDGETPLIKATK--MRNI 349
Cdd:PHA02878 271 TALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN----ICLLKRIKPDIKNSEgfIDNM 344
|
...
gi 1907089607 350 EVV 352
Cdd:PHA02878 345 DCI 347
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
118-358 |
1.97e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 71.79 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 118 DVVELLLShGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLV-----WAARKGHLECVKHLLA 192
Cdd:PHA02798 19 STVKLLIK-SCNPNEIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 193 MGADVDQEGANSMTALIVAVKGGYTQSVKEIL---KRNPNVNLTDKDGNTALMIASKEGH---IEIVQDLLDAGTYVNIP 266
Cdd:PHA02798 98 NGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 267 -----------------DRSGDTVLIGAVRGGHV-------------EIVRALLQ--------------KYADIDIRGQD 302
Cdd:PHA02798 178 nnkekydtlhcyfkyniDRIDADILKLFVDNGFIinkenkshkkkfmEYLNSLLYdnkrfkknildfifSYIDINQVDEL 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089607 303 NKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDK 358
Cdd:PHA02798 258 GFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK 313
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
152-320 |
2.11e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 72.21 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 152 DIVHLLLQNGAKVNcsDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN 231
Cdd:PLN03192 508 NVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 232 LTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNiPDRSGDtVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAV 311
Cdd:PLN03192 586 IRDANGNTALWNAISAKHHKIFRILYHFASISD-PHAAGD-LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
|
....*....
gi 1907089607 312 EKGNATMVR 320
Cdd:PLN03192 664 AEDHVDMVR 672
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
220-419 |
3.38e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 71.06 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 220 VKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLD-------AGTYVNIPDrsgdtvligAVRGGHVEIVRALLQK 292
Cdd:PHA02878 53 VKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvFYTLVAIKD---------AFNNRNVEIFKIILTN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 293 YA----DIDIRGQDNKTAlywaVEKGNATMVRDILQCNPDTEICTKD-GETPLIKATKMRNIEVVELLLDKGARVSAVDK 367
Cdd:PHA02878 124 RYkniqTIDLVYIDKKSK----DDIIEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907089607 368 KGDTPLHVAIRGRSRRLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSI 419
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLEN---GASTDARDKCGNTPLHISVGYCKDY 248
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
173-358 |
7.27e-12 |
|
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: 70.43 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 173 TPLVWAARKGHLECVKHLLAM-GADVDQEGANSMTALIVAVKGGYTQSVKEILKRNP---NVNLTDK--DGNTALMIASK 246
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvNEPMTSDlyQGETALHIAVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 247 EGHIEIVQDLLDAGTYVNIPdRS---------------GDTVLIGAVRGGHVEIVRALLQKYADIdiRGQDN--KTALYW 309
Cdd:cd22192 99 NQNLNLVRELIARGADVVSP-RAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADI--RAQDSlgNTVLHI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907089607 310 AVEKGNAT----MVRDILQCNP-DTEIC-----TKDGETPLIKATKMRNIEVVELLLDK 358
Cdd:cd22192 176 LVLQPNKTfacqMYDLILSYDKeDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
432-845 |
8.21e-12 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 69.17 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 432 TETDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGqqieplfqfswlivflilllcg 511
Cdd:COG4928 1 NETEEDLLGRKKYAESLANLIKSSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 512 glglvfaftvdtnlaiavslsflallyifFIVIYFggrqegeswnwawalstrlarhigylellfklmfvNPpelpeqtt 591
Cdd:COG4928 59 -----------------------------VIVVYF-----------------------------------NA-------- 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 592 kalpvrFLFTDYNRLssvggetsLAEMIATLSDACEREfgflatrlfrvfKTEDSQGKKKWKKtcclpsfiiflfivgcI 671
Cdd:COG4928 67 ------WLYDGEEDL--------LAALLSEIAAELEKK------------KKKDKKAAKKLKK----------------Y 104
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 672 IAGITLLAIfrvdpkhltvnailisIASIVGLafvlncrtWWQVLDSLLNSQRKRLHSAASK-LHKLKSEgFMKVLKcev 750
Cdd:COG4928 105 AKRLSKLAL----------------KAGLLGG--------PAEAVAEALKALLKKEYKSKKKsIEAFREE-LEELLK--- 156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 751 ELMARmaktidsftqnqtRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNsvlrdSNIN 830
Cdd:COG4928 157 ELKGK-------------RLVVFIDDLDRCEPDEAIEVLELIKLFFDFPNVVFVLAFDREILEHALKERYG-----EDID 218
|
410
....*....|....*
gi 1907089607 831 GHDYMRNIVHLPVFL 845
Cdd:COG4928 219 AREYLEKIIQVPFRL 233
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
174-377 |
1.18e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.14 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 174 PLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKrnpnVNLTDKDGNTALMI--ASKEGHIE 251
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTLVAIkdAFNNRNVE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 252 IVQDLLdAGTYVNIpdRSGDTVLIGAVRGGHV---EIVRALLQKYADIDIRGQDN-KTALYWAVEKGNATMVRDILQCNP 327
Cdd:PHA02878 116 IFKIIL-TNRYKNI--QTIDLVYIDKKSKDDIieaEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907089607 328 DTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAI 377
Cdd:PHA02878 193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
3-170 |
1.92e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 69.13 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 3 VLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEG 82
Cdd:PLN03192 523 PNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 83 HIHIVEELLKCgANLEHRDMGGwTALMWACYKGRTDVVELLLSHGAN------PSVTGLQYsvypiiwAAGRGHADIVHL 156
Cdd:PLN03192 603 HHKIFRILYHF-ASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNvdsedhQGATALQV-------AMAEDHVDMVRL 673
|
170
....*....|....
gi 1907089607 157 LLQNGAKVNCSDKY 170
Cdd:PLN03192 674 LIMNGADVDKANTD 687
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
142-297 |
2.16e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 69.13 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 142 IIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYtQSVK 221
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH-HKIF 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 222 EILKR-----NPNVnltdkdGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADI 296
Cdd:PLN03192 608 RILYHfasisDPHA------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
.
gi 1907089607 297 D 297
Cdd:PLN03192 682 D 682
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
152-381 |
4.35e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 67.60 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 152 DIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLA--MGADVDQEGANSMTA------------LIVAVKGGYT 217
Cdd:PHA02878 51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsiNKCSVFYTLVAIKDAfnnrnveifkiiLTNRYKNIQT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 218 QSVKEILKRNPN-----------------VNLTDKD-GNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVR 279
Cdd:PHA02878 131 IDLVYIDKKSKDdiieaeitklllsygadINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 280 GGHVEIVRALLQKYADIDIRGQDNKTALYWAVEK-GNATMVRDILQCNPDTEI-CTKDGETPLIKAtkMRNIEVVELLLD 357
Cdd:PHA02878 211 HYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSS--IKSERKLKLLLE 288
|
250 260
....*....|....*....|....
gi 1907089607 358 KGARVSAVDKKGDTPLHVAIRGRS 381
Cdd:PHA02878 289 YGADINSLNSYKLTPLSSAVKQYL 312
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
9-257 |
5.61e-11 |
|
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: 67.80 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 9 VINYVEEENIPALKALLEKCK--DVDERNECGQTPLMIAAEQGNVEIVKELIKNgANCNLEDLDnwTALISASKEGHiHI 86
Cdd:TIGR00870 21 FLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLN-LSCRGAVGD--TLLHAISLEYV-DA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 87 VEELL-------KCGANLEH---RDMG----GWTALMWACYKGRTDVVELLLSHGAN-------------PSVTGLQYSV 139
Cdd:TIGR00870 97 VEAILlhllaafRKSGPLELandQYTSeftpGITALHLAAHRQNYEIVKLLLERGASvparacgdffvksQGVDSFYHGE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 140 YPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTplvwaarkghlecVKHLLAMGADVDQEG---ANSMTALIVAVKGG- 215
Cdd:TIGR00870 177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNT-------------LLHLLVMENEFKAEYeelSCQMYNFALSLLDKl 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907089607 216 -YTQSVKEILKRnpnvnltdkDGNTALMIASKEGHIEIVQDLL 257
Cdd:TIGR00870 244 rDSKELEVILNH---------QGLTPLKLAAKEGRIVLFRLKL 277
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
204-411 |
7.03e-11 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 66.96 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 204 SMTALIVAVKGGYTQSVKEILKrNPNVNLTDKD--GNTALMIASKEGHIEIVQDLLDAG-TYVNIPDRS----GDTVLIG 276
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLK-CPSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApELVNEPMTSdlyqGETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 277 AVRGGHVEIVRALLQKYADID---------IRGQDNKtaLYWavekgnatmvrdilqcnpdteictkdGETPLIKATKMR 347
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVspratgtffRPGPKNL--IYY--------------------------GEHPLSFAACVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907089607 348 NIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLA----ELLLRNPKDGRL--LYR-PNKAGETPYNI 411
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpLDLvPNNQGLTPFKL 218
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
141-191 |
1.57e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.05 E-value: 1.57e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907089607 141 PIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLL 191
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
194-366 |
2.16e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 65.66 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 194 GADVDQEGANSmtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTV 273
Cdd:PLN03192 518 GEHDDPNMASN---LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 274 LIGAVRGGHVEIVRALLQkYADIdirgQDNKTA---LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIE 350
Cdd:PLN03192 595 LWNAISAKHHKIFRILYH-FASI----SDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669
|
170
....*....|....*.
gi 1907089607 351 VVELLLDKGARVSAVD 366
Cdd:PLN03192 670 MVRLLIMNGADVDKAN 685
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
98-263 |
5.59e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.50 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 98 EHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVW 177
Cdd:PLN03192 519 EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRT-PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWN 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 178 AARKGHLECVKHLLAMGADVDQEGANSMtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLL 257
Cdd:PLN03192 598 AISAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
....*.
gi 1907089607 258 DAGTYV 263
Cdd:PLN03192 676 MNGADV 681
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
21-181 |
6.50e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 63.75 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 21 LKALLEKCKDVDERNE-CGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCGANLEH 99
Cdd:PHA02878 150 TKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 100 RDMGGWTALMWAC-YKGRTDVVELLLSHGANPSV-------TGLQYSVYpiiwaagrgHADIVHLLLQNGAKVNCSDKYG 171
Cdd:PHA02878 230 RDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAksyilglTALHSSIK---------SERKLKLLLEYGADINSLNSYK 300
|
170
....*....|
gi 1907089607 172 TTPLVWAARK 181
Cdd:PHA02878 301 LTPLSSAVKQ 310
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
40-91 |
2.00e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 2.00e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907089607 40 TPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELL 91
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
24-78 |
7.81e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 53.12 E-value: 7.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089607 24 LLEKC-KDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISA 78
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
71-124 |
9.48e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.05 E-value: 9.48e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907089607 71 NWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLL 124
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
283-391 |
1.30e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 59.65 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 283 VEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATmVRDILQC------NPDT-EICtkdGETPLIkaTKMRN---IEVV 352
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEK-VKDIVRLlleagaDVNApERC---GFTPLH--LYLYNattLDVI 100
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907089607 353 ELLLDKGARVSAVDKKGDTPLHVAIRGRSRR--LAELLLRN 391
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRK 141
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
237-290 |
2.24e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 2.24e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907089607 237 GNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALL 290
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
314-390 |
2.40e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.14 E-value: 2.40e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907089607 314 GNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLLR 390
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
13-58 |
2.73e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 2.73e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907089607 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELI 58
Cdd:pfam13637 9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
205-257 |
5.26e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 5.26e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907089607 205 MTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLL 257
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
6-175 |
6.10e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 57.28 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 6 SQSVINY-VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHI 84
Cdd:PHA02874 124 LKTFLHYaIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 85 HIVEELLKCGANLEHRDMGGWTALMWACYKGRTdVVELLLShgaNPSV--------TGLQYSV-YPIiwaagrgHADIVH 155
Cdd:PHA02874 204 ACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLIN---NASIndqdidgsTPLHHAInPPC-------DIDIID 272
|
170 180
....*....|....*....|
gi 1907089607 156 LLLQNGAKVNCSDKYGTTPL 175
Cdd:PHA02874 273 ILLYHKADISIKDNKGENPI 292
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1-129 |
7.52e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 56.98 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 1 MSVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQ--GNVEIVKELIKNGAN--------------- 63
Cdd:PHA03100 69 STPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANvniknsdgenllhly 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 64 --CNLEDLD----------------------------------NWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTA 107
Cdd:PHA03100 149 leSNKIDLKilkllidkgvdinaknrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
|
170 180
....*....|....*....|..
gi 1907089607 108 LMWACYKGRTDVVELLLSHGAN 129
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLNNGPS 250
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
10-291 |
8.92e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 56.67 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 10 INYVEEENIPALKALLEKCKDVDErnEC-GQTPLMIAAEQGNV--EIVKELIKNGANCNLEDLDNwTALISASKEGHI-- 84
Cdd:PHA02989 8 ILYSDTVDKNALEFLLRTGFDVNE--EYrGNSILLLYLKRKDVkiKIVKLLIDNGADVNYKGYIE-TPLCAVLRNREIts 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 85 ----HIVEELLKCGANLEHRDMGGWTALMWACYK---GRTDVVELLLSHGAN-PSVTGLQ-YSVYPIIWAAGRGHADIVH 155
Cdd:PHA02989 85 nkikKIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFLLSKGINvNDVKNSRgYNLLHMYLESFSVKKDVIK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 156 LLLQNGakVNCSDK---YGTTPLVWAARKG----HLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKE------ 222
Cdd:PHA02989 165 ILLSFG--VNLFEKtslYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNNGSESVLESFLDNNKILSKKEfkvlnf 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907089607 223 ILKRnPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQ 291
Cdd:PHA02989 243 ILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
338-389 |
9.20e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 9.20e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907089607 338 TPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLL 389
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
104-158 |
1.23e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 1.23e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907089607 104 GWTALMWACYKGRTDVVELLLSHGANPSVTGLQySVYPIIWAAGRGHADIVHLLL 158
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
157-211 |
2.63e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 2.63e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089607 157 LLQNG-AKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVA 211
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
171-221 |
3.92e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 3.92e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907089607 171 GTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVK 221
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
12-174 |
4.12e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 52.51 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 12 YVEEENIPALKALLekcKDVDERNECGQTPLMIAAEQ--GNVEIVKELIKNGANCNLEDLD-NWTAL---ISASKEGHIH 85
Cdd:PHA02859 28 YVEKDDIEGVKKWI---KFVNDCNDLYETPIFSCLEKdkVNVEILKFLIENGADVNFKTRDnNLSALhhyLSFNKNVEPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 86 IVEELLKCGANLEHRDMGGWTAL-MWAC-YKGRTDVVELLLSHGANPsvTGLQYSVYPIIWAAGRGHAD--IVHLLLQNG 161
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLhMYMCnFNVRINVIKLLIDSGVSF--LNKDFDNNNILYSYILFHSDkkIFDFLTSLG 182
|
170
....*....|...
gi 1907089607 162 AKVNCSDKYGTTP 174
Cdd:PHA02859 183 IDINETNKSGYNC 195
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
38-66 |
1.17e-06 |
|
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: 46.43 E-value: 1.17e-06
10 20
....*....|....*....|....*....
gi 1907089607 38 GQTPLMIAAEQGNVEIVKELIKNGANCNL 66
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
38-68 |
1.47e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 46.13 E-value: 1.47e-06
10 20 30
....*....|....*....|....*....|..
gi 1907089607 38 GQTPLMIAAEQ-GNVEIVKELIKNGANCNLED 68
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
226-277 |
1.48e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 1.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907089607 226 RNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGA 277
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
146-257 |
2.05e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 146 AGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmtalivavkggytqsvkeilk 225
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD----------------------------- 140
|
90 100 110
....*....|....*....|....*....|..
gi 1907089607 226 rnpnVNLTDKDGNTALMIASKEGHIEIVQDLL 257
Cdd:PTZ00322 141 ----PTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
51-328 |
2.91e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 52.14 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 51 VEIVKELIKNGANCNLEDLDNWTALISaskeghihIVEELLKcganlehrdmggwtalmwacYKGRTDVVELLLSHGANP 130
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCT--------ILSNIKD--------------------YKHMLDIVKILIENGADI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 131 SVTGL--QYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECVKHLLAMGADVDQ----EG 201
Cdd:PHA02798 103 NKKNSdgETPLYCLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThnnkEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 202 ANSMTALIvavKGGYTQSVKEILKRNPNVNLTDKDGNTAlmiaSKEGHIEIVQDLLDAG------------TYVNIPDRS 269
Cdd:PHA02798 183 YDTLHCYF---KYNIDRIDADILKLFVDNGFIINKENKS----HKKKFMEYLNSLLYDNkrfkknildfifSYIDINQVD 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907089607 270 --GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPD 328
Cdd:PHA02798 256 elGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
37-65 |
3.09e-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: 45.33 E-value: 3.09e-06
10 20
....*....|....*....|....*....
gi 1907089607 37 CGQTPLMIAAEQGNVEIVKELIKNGANCN 65
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-133 |
5.51e-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: 44.59 E-value: 5.51e-06
10 20 30
....*....|....*....|....*....|.
gi 1907089607 104 GWTALMWACYK-GRTDVVELLLSHGANPSVT 133
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
104-132 |
7.02e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 44.12 E-value: 7.02e-06
10 20
....*....|....*....|....*....
gi 1907089607 104 GWTALMWACYKGRTDVVELLLSHGANPSV 132
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
5-231 |
9.44e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 50.22 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 5 ISQSVINYVEEENIpaLKALLEKCKDVDERNECGQTPLMIAAEQG---NVEIVKELIKNGANCNLEDLDNWTALISASKE 81
Cdd:PHA02798 78 ILSNIKDYKHMLDI--VKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 82 GH---IHIVEELLKCGANL-EHRDMGGWTALmwACY------KGRTDVVELLLSHG------ANPSVTGLQYSVYPIIWA 145
Cdd:PHA02798 156 NHhidIEIIKLLLEKGVDInTHNNKEKYDTL--HCYfkynidRIDADILKLFVDNGfiinkeNKSHKKKFMEYLNSLLYD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 146 AGRGHADIVHLLLQNgAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILK 225
Cdd:PHA02798 234 NKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILN 312
|
....*.
gi 1907089607 226 RNPNVN 231
Cdd:PHA02798 313 KKPNKN 318
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
46-126 |
1.26e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.28 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 46 AEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLS 125
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
.
gi 1907089607 126 H 126
Cdd:PTZ00322 170 H 170
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
52-235 |
1.31e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 49.74 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 52 EIVKELIKNGANCNLEDLDNWTALISASKEGHIH---IVEELLKCGANL-EHRDMGGWTAL-MW-ACYKGRTDVVELLLS 125
Cdd:PHA02989 89 KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINncdMLRFLLSKGINVnDVKNSRGYNLLhMYlESFSVKKDVIKILLS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 126 HGANPSVTGLQYSVYPI-IWAagRGHADIVHL-----LLQNGA------------------------------------- 162
Cdd:PHA02989 169 FGVNLFEKTSLYGLTPMnIYL--RNDIDVISIkvikyLIKKGVnietnnngsesvlesfldnnkilskkefkvlnfilky 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907089607 163 -KVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDK 235
Cdd:PHA02989 247 iKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLKPGKYLIKK 320
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
236-268 |
1.36e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 43.43 E-value: 1.36e-05
10 20 30
....*....|....*....|....*....|....
gi 1907089607 236 DGNTALMIAS-KEGHIEIVQDLLDAGTYVNIPDR 268
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
123-175 |
1.43e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 1.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907089607 123 LLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPL 175
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
178-423 |
1.43e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.08 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 178 AARKGHLECVKHLLAMGADVDQEGANSM--TALIVAVKGGYTQSVKEILKRNPNVNLTdkdGNTALMIASKEGHiEIVQD 255
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPKKLNINCPDRLgrSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISLEYV-DAVEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 256 LL--------DAGTYVNIPDRSGD------TVLIGAVRGGHVEIVRALLQKYADIDIRGqdnktalywaveKGNATMVRD 321
Cdd:TIGR00870 100 ILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARA------------CGDFFVKSQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 322 ILQcnpdteiCTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAI---------RGRSRRLAELLLR-- 390
Cdd:TIGR00870 168 GVD-------SFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSll 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1907089607 391 -NPKDGRLLYR-PNKAGETPYNIDCSHQKSILTQI 423
Cdd:TIGR00870 241 dKLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRL 275
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
284-451 |
1.51e-05 |
|
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: 49.76 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 284 EIVRALLQ--------------KYADIDIRGQdnkTALYWAVEKGNATMVRDILQCNPDTEICTKD-------------- 335
Cdd:cd22194 111 EIVRILLAfaeengildrfinaEYTEEAYEGQ---TALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyf 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 336 GETPLIKATKMRNIEVVELLLDKGAR-VSAVDKKGDTPLH----VAIRGRSR-----RLAELLLRNPKDGRLLYRPNKAG 405
Cdd:cd22194 188 GETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHalvtVAEDSKTQndfvkRMYDMILLKSENKNLETIRNNEG 267
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907089607 406 ETPYNIDCSHQK-SILTQIFG-------ARHLSPTETDgdmLGYDLYSSALADI 451
Cdd:cd22194 268 LTPLQLAAKMGKaEILKYILSreikekpNRSLSRKFTD---WAYGPVSSSLYDL 318
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
170-198 |
3.51e-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: 42.19 E-value: 3.51e-05
10 20
....*....|....*....|....*....
gi 1907089607 170 YGTTPLVWAARKGHLECVKHLLAMGADVD 198
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
30-257 |
3.64e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 48.72 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 30 DVDERNECGQTPLMIAAeqgnveivkelikngANCNLEDLDNWTALISASKEGHIhiVEELLKCGANLEHRDmgGWTALM 109
Cdd:cd21882 18 SAYQRGATGKTCLHKAA---------------LNLNDGVNEAIMLLLEAAPDSGN--PKELVNAPCTDEFYQ--GQTALH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 110 WACYKGRTDVVELLLSHGANPSV------------TGLQYSVYPIIWAAGRGHADIVHLLLQNGAK---VNCSDKYGTTp 174
Cdd:cd21882 79 IAIENRNLNLVRLLVENGADVSAratgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNT- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 175 lvwaarkghlecVKHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrnpnvnlTDKDGNTALMIASKEGH 249
Cdd:cd21882 158 ------------VLHALVLQADNTPENSAFVCQmynllLSYGAHLDPTQQLEEI---------PNHQGLTPLKLAAVEGK 216
|
....*...
gi 1907089607 250 IEIVQDLL 257
Cdd:cd21882 217 IVMFQHIL 224
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
60-257 |
4.51e-05 |
|
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: 48.26 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 60 NGANC------NLEDLDNWTALI---SASKEGHihiveelLKCGANLEHRD--MGGWTALMWACYKGRTDVVELLLSHGA 128
Cdd:cd22196 46 TGKTCllkamlNLHNGQNDTISLlldIAEKTGN-------LKEFVNAAYTDsyYKGQTALHIAIERRNMHLVELLVQNGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 129 -------------NPSVTGLQYSVYPIIWAAGRGHADIVHLLLQN---GAKVNCSDKYGTTplvwaarkghlecVKHLLA 192
Cdd:cd22196 119 dvharasgeffkkKKGGPGFYFGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNT-------------VLHALV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089607 193 MGADVDQEGANSMTALivavkggYTQSVKEILKRNPNVNL---TDKDGNTALMIASKEGHIEIVQDLL 257
Cdd:cd22196 186 EVADNTPENTKFVTKM-------YNEILILGAKIRPLLKLeeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
32-257 |
6.04e-05 |
|
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: 47.93 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 32 DERNECGQTPLMIAAEQGNVeivKELIKngANCNLEDLDNWTALISASKEGHIHIVEELLKCGANLEHRDMGGWtalmwa 111
Cdd:cd22197 60 DGVNACIMPLLEIDKDSGNP---KPLVN--AQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRF------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 112 cYKGRTDvvelllshganpsvTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKvncsdkygttPLVWAARKGHLECVKHLL 191
Cdd:cd22197 129 -FQKKQG--------------TCFYFGELPLSLAACTKQWDVVNYLLENPHQ----------PASLQAQDSLGNTVLHAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907089607 192 AMGADVDQEGansmTALIVAVkggYTQSVKEILKRNPNVNL---TDKDGNTALMIASKEGHIEIVQDLL 257
Cdd:cd22197 184 VMIADNSPEN----SALVIKM---YDGLLQAGARLCPTVQLeeiSNHEGLTPLKLAAKEGKIEIFRHIL 245
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-132 |
6.14e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 41.47 E-value: 6.14e-05
10 20
....*....|....*....|....*....
gi 1907089607 104 GWTALMWACYKGRTDVVELLLSHGANPSV 132
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
170-199 |
6.34e-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: 6.34e-05
10 20 30
....*....|....*....|....*....|.
gi 1907089607 170 YGTTPLVWAA-RKGHLECVKHLLAMGADVDQ 199
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
305-356 |
6.52e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 6.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907089607 305 TALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLL 356
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
90-133 |
7.65e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 7.65e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1907089607 90 LLKCG-ANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVT 133
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK 45
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
117-209 |
8.12e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 46.51 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 117 TDVVELLLSHGANPSV---TGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGT-TPLVWAARKGHLECVKHLLA 192
Cdd:PHA02884 46 TDIIDAILKLGADPEApfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLS 125
|
90
....*....|....*..
gi 1907089607 193 MGADVDQEgANSMTALI 209
Cdd:PHA02884 126 YGADINIQ-TNDMVTPI 141
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
13-257 |
8.90e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 47.45 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 13 VEEENIPALKALLEKCKDVDERNECGQTP--LM---IAAEQGNVEIVKELIkngaNCNLEDLDNWTALISASKEGHIhiV 87
Cdd:cd22194 53 VSEAAVEELGELLKELKDLSRRRRKTDVPdfLMhklTASDTGKTCLMKALL----NINENTKEIVRILLAFAEENGI--L 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 88 EELLKcgANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSV-------------TGLQYSVYPIIWAAGRGHADIV 154
Cdd:cd22194 127 DRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpkykhEGFYFGETPLALAACTNQPEIV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 155 HLLLQNGAK-VNCSDKYGTTPLvwaarkghlecvkHLLAMGADvDQEGANSMTalivavkggyTQSVKEILKRNPNVNL- 232
Cdd:cd22194 205 QLLMEKESTdITSQDSRGNTVL-------------HALVTVAE-DSKTQNDFV----------KRMYDMILLKSENKNLe 260
|
250 260
....*....|....*....|....*..
gi 1907089607 233 --TDKDGNTALMIASKEGHIEIVQDLL 257
Cdd:cd22194 261 tiRNNEGLTPLQLAAKMGKAEILKYIL 287
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
211-411 |
9.85e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.97 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 211 AVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVL--IGAVRGGHVEIVRA 288
Cdd:PHA02946 46 GIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 289 LLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGARVSAVD 366
Cdd:PHA02946 126 LVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907089607 367 KKGDTPLHVAIRGRSRRLAELLLRNPKDGrlLYRPNKAGETPYNI 411
Cdd:PHA02946 206 HDGNTPLHIVCSKTVKNVDIINLLLPSTD--VNKQNKFGDSPLTL 248
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
236-364 |
1.04e-04 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.38 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 236 DGNTALMIASKEGHIEIVQDLLD--AGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYadiDIRGQDNKTALYWAVEK 313
Cdd:TIGR00870 16 DEEKAFLPAAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENENLELTELLLNL---SCRGAVGDTLLHAISLE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907089607 314 G----NATMvRDILQCNPDT-------EICTKD---GETPLIKATKMRNIEVVELLLDKGARVSA 364
Cdd:TIGR00870 93 YvdavEAIL-LHLLAAFRKSgplelanDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
189-290 |
1.26e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 189 HLLAMGADVDQEGANSMTA-LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPD 267
Cdd:PTZ00322 66 HNLTTEEVIDPVVAHMLTVeLCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
|
90 100
....*....|....*....|...
gi 1907089607 268 RSGDTVLIGAVRGGHVEIVRALL 290
Cdd:PTZ00322 146 KDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
270-320 |
1.57e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 1.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907089607 270 GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVR 320
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
349-413 |
2.52e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 43.33 E-value: 2.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089607 349 IEVVELLLDKGARVSAVDKK-GDTPLHVAIRGRSRRLAELLLRNPKDGRLLYrpNKAGETPYNIDC 413
Cdd:PHA02736 71 QEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEIL--NYAFKTPYYVAC 134
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
269-356 |
2.54e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 269 SGDTVliGAvrgghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN 348
Cdd:PTZ00322 92 SGDAV--GA---------RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
....*...
gi 1907089607 349 IEVVELLL 356
Cdd:PTZ00322 161 REVVQLLS 168
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
274-394 |
2.58e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 45.37 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 274 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVE 353
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907089607 354 LLLDKGARVSAV-DKKGDTPLHVAIRGRSRRLAELLLRNPKD 394
Cdd:PHA02875 86 ELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
104-257 |
2.73e-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: 45.56 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 104 GWTALMWACYKGRTDVVELLLSHGA-----------NPSV--TGLQYSVYPIIWAAGRGHADIVHLLLQNG---AKVNCS 167
Cdd:cd22193 76 GQTALHIAIERRQGDIVALLVENGAdvhahakgrffQPKYqgEGFYFGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 168 DKYGTTPLvwaarkghlecvkHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrnpnvnlTDKDGNTALM 242
Cdd:cd22193 156 DSRGNTVL-------------HALVTVADNTKENTKFVTRmydmiLIRGAKLCPTVELEEI---------RNNDGLTPLQ 213
|
170
....*....|....*
gi 1907089607 243 IASKEGHIEIVQDLL 257
Cdd:cd22193 214 LAAKMGKIEILKYIL 228
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
303-437 |
3.61e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.98 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 303 NKTALYWAVEKGNATMVRDILQC--NPDTEIctKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAI-RG 379
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIgiNPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVeEG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089607 380 RSRRLAELLLRNPKDGRLLYrpnKAGETPYNIDCSHQKSILTQIFGARHLSPTETDGD 437
Cdd:PHA02875 80 DVKAVEELLDLGKFADDVFY---KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
57-108 |
3.76e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 3.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907089607 57 LIKNG-ANCNLEDLDNWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTAL 108
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
355-411 |
4.72e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 4.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089607 355 LLDKG-ARVSAVDKKGDTPLHVAIRGRSRRLAELLLRNPKDGRLlyrPNKAGETPYNI 411
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL---KDEEGLTALDL 55
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
141-169 |
5.29e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.81 E-value: 5.29e-04
10 20 30
....*....|....*....|....*....|
gi 1907089607 141 PIIWAAGR-GHADIVHLLLQNGAKVNCSDK 169
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
236-265 |
6.16e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 6.16e-04
10 20 30
....*....|....*....|....*....|
gi 1907089607 236 DGNTALMIASKEGHIEIVQDLLDAGTYVNI 265
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
335-367 |
6.44e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.81 E-value: 6.44e-04
10 20 30
....*....|....*....|....*....|....
gi 1907089607 335 DGETPLIKA-TKMRNIEVVELLLDKGARVSAVDK 367
Cdd:pfam00023 1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
70-101 |
7.47e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.42 E-value: 7.47e-04
10 20 30
....*....|....*....|....*....|...
gi 1907089607 70 DNWTAL-ISASKEGHIHIVEELLKCGANLEHRD 101
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
22-103 |
9.50e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 22 KALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCgaNLEHRD 101
Cdd:PTZ00322 99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH--SQCHFE 176
|
..
gi 1907089607 102 MG 103
Cdd:PTZ00322 177 LG 178
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
339-424 |
1.16e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 43.72 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 339 PLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLLRNPKDGRLLYRPNKAGETPYNIDCSHQKS 418
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
|
....*.
gi 1907089607 419 ILTQIF 424
Cdd:PHA02878 120 ILTNRY 125
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
173-198 |
1.73e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.62 E-value: 1.73e-03
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
322-376 |
1.76e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089607 322 ILQCNP-DTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVA 376
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
90-158 |
2.63e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.58 E-value: 2.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907089607 90 LLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLL 158
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT-PLELAEENGFREVVQLLS 168
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
294-343 |
2.83e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 2.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907089607 294 ADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKA 343
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
256-307 |
2.86e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 2.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907089607 256 LLDAGTY-VNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 307
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
120-204 |
3.61e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.19 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089607 120 VELLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQ 199
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRT-PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
|
....*
gi 1907089607 200 EGANS 204
Cdd:PTZ00322 177 LGANA 181
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
270-298 |
4.31e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.41 E-value: 4.31e-03
10 20
....*....|....*....|....*....
gi 1907089607 270 GDTVLIGAVRGGHVEIVRALLQKYADIDI 298
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
270-299 |
5.24e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.11 E-value: 5.24e-03
10 20 30
....*....|....*....|....*....|.
gi 1907089607 270 GDTVL-IGAVRGGHVEIVRALLQKYADIDIR 299
Cdd:pfam00023 2 GNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
17-71 |
7.19e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.39 E-value: 7.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907089607 17 NIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDN 71
Cdd:PLN03192 634 DLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
70-98 |
7.70e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 7.70e-03
10 20
....*....|....*....|....*....
gi 1907089607 70 DNWTALISASKEGHIHIVEELLKCGANLE 98
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
141-166 |
7.78e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 7.78e-03
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
335-364 |
9.85e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.26 E-value: 9.85e-03
10 20 30
....*....|....*....|....*....|
gi 1907089607 335 DGETPLIKATKMRNIEVVELLLDKGARVSA 364
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| |
