|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
18-307 |
1.17e-61 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 213.28 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 18 IPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEGHVHIVEELLRCGVNV 97
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 98 EHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGlQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVW 177
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 178 AARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 884884283 258 DAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 307
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
16-274 |
7.22e-59 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 205.19 E-value: 7.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 16 ENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEGHVHIVEELLRCGV 95
Cdd:COG0666 32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 96 NVEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGlQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPL 175
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 176 VWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQD 255
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
250
....*....|....*....
gi 884884283 256 LLDAGTYVNIPDRSGDTVL 274
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
105-373 |
9.17e-58 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 202.11 E-value: 9.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 105 WTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHL 184
Cdd:COG0666 21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 185 ECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVN 264
Cdd:COG0666 101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 265 IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKAT 344
Cdd:COG0666 181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
|
250 260
....*....|....*....|....*....
gi 884884283 345 KMRNIEVVELLLDKGAKVSAVDKKGDTPL 373
Cdd:COG0666 261 AAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
10-241 |
1.96e-56 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 198.25 E-value: 1.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 10 INYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEGHVHIVEE 89
Cdd:COG0666 59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 90 LLRCGVNVEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGlQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDK 169
Cdd:COG0666 139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 884884283 170 YGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTAL 241
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
122-394 |
5.27e-56 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 197.10 E-value: 5.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 122 LLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEG 201
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 202 ANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGG 281
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 282 HVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAK 361
Cdd:COG0666 165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
|
250 260 270
....*....|....*....|....*....|...
gi 884884283 362 VSAVDKKGDTPLHIAIRGRSRKLAELLLRNPKD 394
Cdd:COG0666 245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
|
|
| KAP_NTPase |
pfam07693 |
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases ... |
441-954 |
6.89e-55 |
|
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: 193.75 E-value: 6.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 441 YDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFagqqieplfqfswlivfltlllcgavglvftft 520
Cdd:pfam07693 1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 521 ldlslgvavalsclalvyiflvviyfggrregeswnwawvlstrlarhigylellfklmfvnppelpeqttkalPVRFLF 600
Cdd:pfam07693 48 --------------------------------------------------------------------------NEEFII 53
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 601 TDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEESQGKKK--WKKTCCLPSFIIFLFLLGcivagitll 678
Cdd:pfam07693 54 VYFNPWSFSGQDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKigLIFGVAIILALTGLVVAI--------- 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 679 avfrvdsrhltvnavlismasvvglafvlncrtwwqvldsllnsqrkrlhhaasrlhklksEGFMKVLKWEV-ELMAKMA 757
Cdd:pfam07693 125 -------------------------------------------------------------EEPMKKLQTEIeELRSDIE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 758 KTIDSftqNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLSSVLrdsNINGHDYMRN 837
Cdd:pfam07693 144 STLKD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPNVVFILAADEEILKKALEANYESGL---EIDGQKYLEK 217
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 838 IVHLPVFLNSRGLGGARRFLVTSAtngdiacsdapglqedadrrvsQNSLGELTKLGSRTALnrrdtyrrrqmqrtitrq 917
Cdd:pfam07693 218 IIQVPFTLPPLSLRQLKKFLMLSF----------------------DNSEEGTSSKDRDETL------------------ 257
|
490 500 510
....*....|....*....|....*....|....*..
gi 884884283 918 MSFDLTKLLVTEDwFSDISPQTMRRLLNIVSVTGRLL 954
Cdd:pfam07693 258 RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
151-415 |
1.90e-53 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 189.39 E-value: 1.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 151 ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 230
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 231 NLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWA 310
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 311 VEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLr 390
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL- 239
|
250 260
....*....|....*....|....*
gi 884884283 391 npKDGRLLYRPNKAGETPYNIDCSH 415
Cdd:COG0666 240 --EAGADLNAKDKDGLTALLLAAAA 262
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
42-133 |
4.94e-27 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 106.35 E-value: 4.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 42 LMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEGHVHIVEELLRCgVNVEHRDMgGWTALMWACYKGRTDVVE 121
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 884884283 122 LLLSHGANPSVT 133
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
2-400 |
2.75e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 116.70 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 2 SVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKE 81
Cdd:PHA02876 142 SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 82 GHVHIVEELLRCGVNVEHRDMGGWTALmwacykgrtdvvelllshganpSVTGLQYSVypiiwaagrghadivhLLLQNG 161
Cdd:PHA02876 222 KNIDTIKAIIDNRSNINKNDLSLLKAI----------------------RNEDLETSL----------------LLYDAG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 162 AKVNCSDKYGTTPLVWAARKGHL-ECVKHLLAMGADVDQEGANSMTALIVAVKGGY-TQSVKEILKRNPNVNLTDKDGNT 239
Cdd:PHA02876 264 FSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYIT 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 240 ALMIASK-EGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATM 318
Cdd:PHA02876 344 PLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYM 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 319 -VRDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSrkLAELLLR---NPK 393
Cdd:PHA02876 424 sVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHygaELR 501
|
....*..
gi 884884283 394 DGRLLYR 400
Cdd:PHA02876 502 DSRVLHK 508
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
49-378 |
2.76e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 114.29 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 49 GNLEIVKELIKSGANC-NLEDLDNWTALISASKEGHVHIVEELLRCGVNVEHRDMGGWTALMWACYKGRTDVVELLLSHG 127
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCiNISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 128 ANPSVTGLqysvyPIIwaagrgHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmta 207
Cdd:PHA02874 92 VDTSILPI-----PCI------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 208 livavkggytqsvkeilkrnpnVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVR 287
Cdd:PHA02874 150 ----------------------VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 288 ALLQKYADIDIRGQDNKTALYWAVEKGNATMvrDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGAKVSAVD 366
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKD 285
|
330
....*....|..
gi 884884283 367 KKGDTPLHIAIR 378
Cdd:PHA02874 286 NKGENPIDTAFK 297
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
153-403 |
1.95e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 111.30 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 153 IVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQS-VKEI----LKRN 227
Cdd:PHA03100 17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdVKEIvkllLEYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 228 PNVNLTDKDGNTALMIAS--KEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHV--EIVRALLQKYADIDIrgqdn 303
Cdd:PHA03100 97 ANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 304 KTALYWAVEKGNATMVRDILqcnpdteictkdGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRK 383
Cdd:PHA03100 172 KNRVNYLLSYGVPINIKDVY------------GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
250 260
....*....|....*....|....*
gi 884884283 384 LAELLLRN-----PKDGRLLYRPNK 403
Cdd:PHA03100 240 IFKLLLNNgpsikTIIETLLYFKDK 264
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
12-298 |
2.23e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 105.13 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 12 YVEEENIPALKALLEKCkDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEGHVhiveelL 91
Cdd:PHA03100 10 SRIIKVKNIKYIIMEDD-LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYN------L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 92 RCGVNvehrdmggwtalmwacykgrtdVVELLLSHGANPSVTGlQYSVYPIIWAAGR--GHADIVHLLLQNGAKVNCSDK 169
Cdd:PHA03100 83 TDVKE----------------------IVKLLLEYGANVNAPD-NNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 170 YGTTPLVWAARKGH--LECVKHLLAMGADVDQegansmtalivavkggyTQSVKEILKRNPNVNLTDKDGNTALMIASKE 247
Cdd:PHA03100 140 DGENLLHLYLESNKidLKILKLLIDKGVDINA-----------------KNRVNYLLSYGVPINIKDVYGFTPLHYAVYN 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 884884283 248 GHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDI 298
Cdd:PHA03100 203 NNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
43-330 |
5.65e-23 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 104.72 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 43 MIAAEQGNLEIVKELIKSGANCNLEDLDNWTAL---ISASKEGHVHIVEELLRCGVNVEHRDMGGWTAL-MWACYKGRTD 118
Cdd:PHA03095 19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 119 VVELLLSHGANPSVTGLqYSVYPI-IWAAG-RGHADIVHLLLQNGAKVNCSDKYGTTPL-VWAARKG-HLECVKHLLAMG 194
Cdd:PHA03095 99 VIKLLIKAGADVNAKDK-VGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNaNVELLRLLIDAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 195 ADVDQEGANSMTAL---IVAVKgGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTE--IVQDLLDAGTYVNIPDRS 269
Cdd:PHA03095 178 ADVYAVDDRFRSLLhhhLQSFK-PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRY 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 884884283 270 GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTE 330
Cdd:PHA03095 257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
175-267 |
4.52e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.10 E-value: 4.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 175 LVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKrNPNVNLTDkDGNTALMIASKEGHTEIVQ 254
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 884884283 255 DLLDAGTYVNIPD 267
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
9-279 |
4.77e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 101.19 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 9 VINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANCN---LEDLDNWTalisaskeghvh 85
Cdd:PHA02874 39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpIPCIEKDM------------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 86 iVEELLRCGVNVEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQySVYPIIWAAGRGHADIVHLLLQNGAKVN 165
Cdd:PHA02874 107 -IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 166 CSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKggYTQSVKEILKRNPNVNLTDKDGNTALMIA- 244
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAi 262
|
250 260 270
....*....|....*....|....*....|....*
gi 884884283 245 SKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVR 279
Cdd:PHA02874 263 NPPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
113-411 |
6.10e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 100.81 E-value: 6.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 113 YKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLA 192
Cdd:PHA02874 10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 193 MGADVDqegansmtalIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDT 272
Cdd:PHA02874 90 NGVDTS----------ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 273 VLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATkMRNIEVV 352
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 353 ELLLDKgAKVSAVDKKGDTPLHIAIRGR-SRKLAELLLRNPKDgrLLYRPNKaGETPYNI 411
Cdd:PHA02874 239 ELLINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKAD--ISIKDNK-GENPIDT 294
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
108-199 |
3.39e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 89.79 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 108 LMWACYKGRTDVVELLLSHGANPSVTgLQYSVYPIIWAAGRGHADIVHLLLQNgAKVNCSDkYGTTPLVWAARKGHLECV 187
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|..
gi 884884283 188 KHLLAMGADVDQ 199
Cdd:pfam12796 78 KLLLEKGADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
142-234 |
8.96e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.25 E-value: 8.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 142 IIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLA-MGADVDQEGansMTALIVAVKGGYTQSV 220
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNG---RTALHYAARSGHLEIV 77
|
90
....*....|....
gi 884884283 221 KEILKRNPNVNLTD 234
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
12-264 |
1.76e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 96.27 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 12 YVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQG-----NLEIVKELIKSGANCNLEDLDNWTALISAS--KEGHV 84
Cdd:PHA03100 42 AKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 85 HIVEELLRCGVNVEHRDMGGWTALMWA--CYKGRTDVVELLLSHGANPSVTglqysvypiiwaagrghaDIVHLLLQNGA 162
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAK------------------NRVNYLLSYGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 163 KVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN--------LTD 234
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKtiietllyFKD 263
|
250 260 270
....*....|....*....|....*....|
gi 884884283 235 KDGNTALMIASKEgHTEIVQDLLDAGTYVN 264
Cdd:PHA03100 264 KDLNTITKIKMLK-KSIMYMFLLDPGFYKN 292
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
208-299 |
3.43e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.71 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 208 LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTyVNIPDrSGDTVLIGAVRGGHVEIVR 287
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 884884283 288 ALLQKYADIDIR 299
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
13-101 |
1.00e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.55 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKSgANCNLEDlDNWTALISASKEGHVHIVEELLR 92
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 884884283 93 CGVNVEHRD 101
Cdd:pfam12796 83 KGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
274-366 |
5.77e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.24 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 274 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRdILQCNPDTEICTkDGETPLIKATKMRNIEVVE 353
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 884884283 354 LLLDKGAKVSAVD 366
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
241-335 |
1.43e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.09 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 241 LMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLqKYADIDIRGqDNKTALYWAVEKGNATMVR 320
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|....*
gi 884884283 321 DILQCNPDteICTKD 335
Cdd:pfam12796 79 LLLEKGAD--INVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
74-298 |
1.61e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 90.05 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 74 ALISASKEGHVHIVEELLRCGVNVEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTglqysvYPIIW-----AAGR 148
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVK------YPDIEselhdAVEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 149 GHADIVHLLLQNGAKVN-CSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRN 227
Cdd:PHA02875 79 GDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 884884283 228 PNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGD-TVLIGAVRGGHVEIVRALLQKYADIDI 298
Cdd:PHA02875 159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
220-390 |
3.09e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 90.08 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 220 VKEILKRNPNVNLTDKDGNTAL---MIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVE-IVRALLQKYAD 295
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 296 IDIRGQDNKTAL--YWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGAKVSAVDKKGDT 371
Cdd:PHA03095 110 VNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRS 189
|
170 180
....*....|....*....|..
gi 884884283 372 PLHI---AIRGRSRKLAELLLR 390
Cdd:PHA03095 190 LLHHhlqSFKPRARIVRELIRA 211
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
182-399 |
3.44e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 89.28 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 182 GHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRN--PNVNLTDKDgnTALMIASKEGHTEIVQDLLDA 259
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGaiPDVKYPDIE--SELHDAVEEGDVKAVEELLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 260 GTYVN-IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGET 338
Cdd:PHA02875 91 GKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 884884283 339 PLIKATKMRNIEVVELLLDKGAKVSAVDKKGD-TPLHIAIRGRSRKLAELLLRNPKDGRLLY 399
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
21-292 |
2.60e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 87.00 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 21 LKALLEKCKDVDERNECGQTPLMIAAEQGN-LEIVKELIKSGANCNLEDLDNWTAL--ISASKEGHVHIVEELLRCGVNV 97
Cdd:PHA03095 66 VRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 98 EHRDMGGWTALmwACYKGRTDV----VELLLSHGANPSVTGL-------QYSVYPiiwaagRGHADIVHLLLQNGAKVNC 166
Cdd:PHA03095 146 NALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVYAVDDrfrsllhHHLQSF------KPRARIVRELIRAGCDPAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 167 SDKYGTTPLvwaarkghlecvkHLLAMGAdvdqeganSMTALIVAvkggytqsvkEILKRNPNVNLTDKDGNTALMIASK 246
Cdd:PHA03095 218 TDMLGNTPL-------------HSMATGS--------SCKRSLVL----------PLLIAGISINARNRYGQTPLHYAAV 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 884884283 247 EGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQK 292
Cdd:PHA03095 267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
18-307 |
7.13e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.85 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 18 IPALKALLEKCKDVDERNECGQTPLMI--AAEQGNLEIVKELIKSGANCNLEDLDNWT---ALISaSKEGHVHIVEELLR 92
Cdd:PHA03095 97 LDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLK-SRNANVELLRLLID 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 93 CGVNVEHRDMGGWTALMWAC--YKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHL-LLQNGAKVNCSDK 169
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLpLLIAGISINARNR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 170 YGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKdgntALMIASKEGH 249
Cdd:PHA03095 256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGG 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 884884283 250 TEIVQDLLDAGTYVNIpdRSGDTVLIGAVRGGHVEIVRALLQKYADI-DIRGQDNKTAL 307
Cdd:PHA03095 332 DIPSDATRLCVAKVVL--RGAFSLLPEPIRAYHADFIRECEAEIAVMrTTRIGTGVSLL 388
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
204-436 |
8.49e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 85.02 E-value: 8.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 204 SMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAG---TYVNIPDRSGDTVligavrg 280
Cdd:PHA02874 35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtSILPIPCIEKDMI------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 281 ghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGA 360
Cdd:PHA02874 108 ------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 884884283 361 KVSAVDKKGDTPLHIAIRGRSRKLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSILTQIFGARHLSPTETDG 436
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDH---GNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDG 254
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
151-376 |
9.14e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.46 E-value: 9.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 151 ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEIL-KR 226
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 227 NPNVNLTDKDGNTALMI--ASKEGHTEIVQDLLDAGTYVNIPDRSGDT---VLIGAvRGGHVEIVRALLQKYADI---DI 298
Cdd:PHA03095 107 GADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKS-RNANVELLRLLIDAGADVyavDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 299 RGQdnkTALYWAVE--KGNATMVRDILQCNPDTEICTKDGETPLIKA---TKMRNIeVVELLLDKGAKVSAVDKKGDTPL 373
Cdd:PHA03095 186 RFR---SLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRS-LVLPLLIAGISINARNRYGQTPL 261
|
...
gi 884884283 374 HIA 376
Cdd:PHA03095 262 HYA 264
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
307-394 |
1.27e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.69 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 307 LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAkvSAVDKKGDTPLHIAIRGRSRKLAE 386
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
....*...
gi 884884283 387 LLLRNPKD 394
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
13-247 |
6.65e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 82.62 E-value: 6.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANC---------------------------- 64
Cdd:PHA02878 45 VEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCsvfytlvaikdafnnrnveifkiiltnr 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 65 --NLEDLDNwTALISASKEGHV--HIVEELLRCG--VNVEHRDMGGwTALMWACYKGRTDVVELLLSHGANPSVTGLQYS 138
Cdd:PHA02878 125 ykNIQTIDL-VYIDKKSKDDIIeaEITKLLLSYGadINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 139 vYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWA-ARKGHLECVKHLLAMGADVD-QEGANSMTALIVAVKGgy 216
Cdd:PHA02878 203 -SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNaKSYILGLTALHSSIKS-- 279
|
250 260 270
....*....|....*....|....*....|.
gi 884884283 217 TQSVKEILKRNPNVNLTDKDGNTALMIASKE 247
Cdd:PHA02878 280 ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
31-257 |
3.90e-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: 77.75 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 31 VDERNECGQ-----TPLMIAAEQGNLEIVKELIKSgancnlEDLDNW-------TALISASKEGHVHIVEELLRCG---V 95
Cdd:cd22192 5 LDELHLLQQkriseSPLLLAAKENDVQAIKKLLKC------PSCDLFqrgalgeTALHVAALYDNLEAAVVLMEAApelV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 96 NVE-HRDM-GGWTALMWACYKGRTDVVELLLSHGA---NPSVTG----------LQYSVYPIIWAAGRGHADIVHLLLQN 160
Cdd:cd22192 79 NEPmTSDLyQGETALHIAVVNQNLNLVRELIARGAdvvSPRATGtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 161 GAKVNCSDKYGTTPLvwaarkghlecvkHLLAMGAdvDQEGANSMTALIVA-VKGGYTQSVKEIlkrnPNvnltdKDGNT 239
Cdd:cd22192 159 GADIRAQDSLGNTVL-------------HILVLQP--NKTFACQMYDLILSyDKEDDLQPLDLV----PN-----NQGLT 214
|
250
....*....|....*...
gi 884884283 240 ALMIASKEGHTEIVQDLL 257
Cdd:cd22192 215 PFKLAAKEGNIVMFQHLV 232
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
220-419 |
9.96e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 75.69 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 220 VKEILKRNPNVNLTDKDGNTAL--------MIASKEGHTEIVQDLLdAGTYVNIPDrsgdtvligAVRGGHVEIVRALLQ 291
Cdd:PHA02878 53 VKSLLTRGHNVNQPDHRDLTPLhiickepnKLGMKEMIRSINKCSV-FYTLVAIKD---------AFNNRNVEIFKIILT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 292 KYA----DIDIRGQDNKTAlywaVEKGNATMVRDILQCNPDTEICTKD-GETPLIKATKMRNIEVVELLLDKGAKVSAVD 366
Cdd:PHA02878 123 NRYkniqTIDLVYIDKKSK----DDIIEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 884884283 367 KKGDTPLHIAIRGRSRKLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSI 419
Cdd:PHA02878 199 KTNNSPLHHAVKHYNKPIVHILLEN---GASTDARDKCGNTPLHISVGYCKDY 248
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
41-352 |
2.72e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 74.53 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 41 PLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEGHVHIVEELLR----CGVNVEHRdmggwtALMWACYKGR 116
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkCSVFYTLV------AIKDAFNNRN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 117 TDVVE-LLLSHGANPSVTGLQY----SVYPIIwaagrgHADIVHLLLQNGAKVNCSDKY-GTTPLVWAARKGHLECVKHL 190
Cdd:PHA02878 114 VEIFKiILTNRYKNIQTIDLVYidkkSKDDII------EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 191 LAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKE-GHTEIVQDLLDAGTYVNIPDR- 268
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYi 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 269 SGDTVLIGAVRGGHVeiVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNpdteICTKDGETPLIKATK--M 346
Cdd:PHA02878 268 LGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN----ICLLKRIKPDIKNSEgfI 341
|
....*.
gi 884884283 347 RNIEVV 352
Cdd:PHA02878 342 DNMDCI 347
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
13-230 |
2.83e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 73.87 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 13 VEEENIPALKALLEKCKDVDER-NECGQTPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEGHVHIVEELL 91
Cdd:PHA02875 76 VEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 92 RCGVNVEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVN----CS 167
Cdd:PHA02875 156 DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNimfmIE 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 884884283 168 DKYGTTplvwaarkghLECVKHllaMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 230
Cdd:PHA02875 236 GEECTI----------LDMICN---MCTNLESEAIDALIADIAIRIHKKTIRRDEGFKNNMST 285
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
152-320 |
1.31e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 72.98 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 152 DIVHLLLQNGAKVNcsDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN 231
Cdd:PLN03192 508 NVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 232 LTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNiPDRSGDtVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAV 311
Cdd:PLN03192 586 IRDANGNTALWNAISAKHHKIFRILYHFASISD-PHAAGD-LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
|
....*....
gi 884884283 312 EKGNATMVR 320
Cdd:PLN03192 664 AEDHVDMVR 672
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
118-358 |
8.42e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 69.86 E-value: 8.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 118 DVVELLLShGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLV-----WAARKGHLECVKHLLA 192
Cdd:PHA02798 19 STVKLLIK-SCNPNEIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 193 MGADVDQEGANSMTALIVAVKGGYTQSVKEIL---KRNPNVNLTDKDGNTALMIASKEGHT---EIVQDLLDAGTYVNIP 266
Cdd:PHA02798 98 NGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 267 -----------------DRSGDTVLIGAVRGGHV-------------EIVRALLQ--------------KYADIDIRGQD 302
Cdd:PHA02798 178 nnkekydtlhcyfkyniDRIDADILKLFVDNGFIinkenkshkkkfmEYLNSLLYdnkrfkknildfifSYIDINQVDEL 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 884884283 303 NKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDK 358
Cdd:PHA02798 258 GFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK 313
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
204-411 |
8.85e-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: 70.04 E-value: 8.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 204 SMTALIVAVKGGYTQSVKEILKrNPNVNLTDKD--GNTALMIASKEGHTEIVQDLLDAG-TYVNIPDRS----GDTVLIG 276
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLK-CPSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApELVNEPMTSdlyqGETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 277 AVRGGHVEIVRALLQKYADID---------IRGQDNKtaLYWavekgnatmvrdilqcnpdteictkdGETPLIKATKMR 347
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVspratgtffRPGPKNL--IYY--------------------------GEHPLSFAACVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 884884283 348 NIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLA----ELLLRNPKDGRL--LYR-PNKAGETPYNI 411
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpLDLvPNNQGLTPFKL 218
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
432-988 |
1.00e-11 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 68.78 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 432 TETDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGqqieplfqfswlivfltlllcg 511
Cdd:COG4928 1 NETEEDLLGRKKYAESLANLIKSSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 512 avglvftftldlslgvavalsclalvyifLVVIYFggrregeswnwawvlstrlarhigylellfklmfvNPpelpeqtt 591
Cdd:COG4928 59 -----------------------------VIVVYF-----------------------------------NA-------- 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 592 kalpvrFLFTDYNRLssvggetsLAEMIATLSDACEREfgflatrlfrvfKTEESQGKKKWKKtcclpsfiiflfllgcI 671
Cdd:COG4928 67 ------WLYDGEEDL--------LAALLSEIAAELEKK------------KKKDKKAAKKLKK----------------Y 104
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 672 VAGITLLAVfrvdsrhltvnavlisMASVVGLafvlncrtWWQVLDSLLNSQRKRLHHAASR-LHKLKSEgFMKVLKwev 750
Cdd:COG4928 105 AKRLSKLAL----------------KAGLLGG--------PAEAVAEALKALLKKEYKSKKKsIEAFREE-LEELLK--- 156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 751 ELMAKmaktidsftqnqtRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLssvlrDSNIN 830
Cdd:COG4928 157 ELKGK-------------RLVVFIDDLDRCEPDEAIEVLELIKLFFDFPNVVFVLAFDREILEHALKERY-----GEDID 218
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 831 GHDYMRNIVHLPVFLNSRGLGGARRFLvtsatNGDIACSDAPGLQEDADRRVSQNSLGELTKLGSRTALNRRDTYRRRQM 910
Cdd:COG4928 219 AREYLEKIIQVPFRLPPLSNELLILEL-----DRLLELLLSALLEALLALLLLRALAESISSLRAEFLLLLLLLKLELLL 293
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 884884283 911 QRTITRQMSFDLTKLLVTEDW-FSDISPQTMRRLLNIVSVTGRLLRANQITFNWDRLASWINLTEQWPYRTSWLILYLE 988
Cdd:COG4928 294 ALLVLLLKLELLLENLLLAALlLLLDELELKKLLREDVASRASLYFINAELANLSLKLLKISSELLTLELKLEEERELS 372
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
173-358 |
2.81e-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: 68.50 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 173 TPLVWAARKGHLECVKHLLAM-GADVDQEGANSMTALIVAVKGGYTQSVKEILKRNP---NVNLTDK--DGNTALMIASK 246
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvNEPMTSDlyQGETALHIAVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 247 EGHTEIVQDLLDAGTYVNIPdRS---------------GDTVLIGAVRGGHVEIVRALLQKYADIdiRGQDN--KTALYW 309
Cdd:cd22192 99 NQNLNLVRELIARGADVVSP-RAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADI--RAQDSlgNTVLHI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 884884283 310 AVEKGNAT----MVRDILQCNP-DTEIC-----TKDGETPLIKATKMRNIEVVELLLDK 358
Cdd:cd22192 176 LVLQPNKTfacqMYDLILSYDKeDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
142-297 |
4.73e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.97 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 142 IIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYtQSVK 221
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH-HKIF 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 222 EILKR-----NPNVnltdkdGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADI 296
Cdd:PLN03192 608 RILYHfasisDPHA------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
.
gi 884884283 297 D 297
Cdd:PLN03192 682 D 682
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
9-257 |
7.95e-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: 67.03 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 9 VINYVEEENIPALKALLEKCK--DVDERNECGQTPLMIAAEQGNLEIVKELIKSgANCNLEDLDnwtALISASKEGHVHI 86
Cdd:TIGR00870 21 FLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLN-LSCRGAVGD---TLLHAISLEYVDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 87 VEELL-------RCGVNVEH---RDMG----GWTALMWACYKGRTDVVELLLSHGAN-------------PSVTGLQYSV 139
Cdd:TIGR00870 97 VEAILlhllaafRKSGPLELandQYTSeftpGITALHLAAHRQNYEIVKLLLERGASvparacgdffvksQGVDSFYHGE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 140 YPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTplvwaarkghlecVKHLLAMGADVDQEG---ANSMTALIVAVKGG- 215
Cdd:TIGR00870 177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNT-------------LLHLLVMENEFKAEYeelSCQMYNFALSLLDKl 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 884884283 216 -YTQSVKEILKRnpnvnltdkDGNTALMIASKEGHTEIVQDLL 257
Cdd:TIGR00870 244 rDSKELEVILNH---------QGLTPLKLAAKEGRIVLFRLKL 277
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
194-366 |
8.56e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.20 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 194 GADVDQEGANSmtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTV 273
Cdd:PLN03192 518 GEHDDPNMASN---LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 274 LIGAVRGGHVEIVRALLQkYADIdirgQDNKTA---LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIE 350
Cdd:PLN03192 595 LWNAISAKHHKIFRILYH-FASI----SDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669
|
170
....*....|....*.
gi 884884283 351 VVELLLDKGAKVSAVD 366
Cdd:PLN03192 670 MVRLLIMNGADVDKAN 685
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
3-170 |
1.45e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 66.43 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 3 VLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEG 82
Cdd:PLN03192 523 PNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 83 HVHIVEELLRCGvNVEHRDMGGwTALMWACYKGRTDVVELLLSHGAN------PSVTGLQYsvypiiwAAGRGHADIVHL 156
Cdd:PLN03192 603 HHKIFRILYHFA-SISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNvdsedhQGATALQV-------AMAEDHVDMVRL 673
|
170
....*....|....
gi 884884283 157 LLQNGAKVNCSDKY 170
Cdd:PLN03192 674 LIMNGADVDKANTD 687
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
141-191 |
2.04e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.67 E-value: 2.04e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 884884283 141 PIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLL 191
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
98-263 |
3.88e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.89 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 98 EHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVW 177
Cdd:PLN03192 519 EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRT-PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWN 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 178 AARKGHLECVKHLLAMGADVDQEGANSMtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:PLN03192 598 AISAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
....*.
gi 884884283 258 DAGTYV 263
Cdd:PLN03192 676 MNGADV 681
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
40-91 |
1.82e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 1.82e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 884884283 40 TPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEGHVHIVEELL 91
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
39-232 |
8.83e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 59.62 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 39 QTPLMIAAEQGNLEIVKELIKSGANCNledldnwtalisaskeghvhiveellrcgvNVEHRDmgGWTALMWACYKGRTD 118
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFAD------------------------------DVFYKD--GMTPLHLATILKKLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 119 VVELLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVD 198
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFS-PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
|
170 180 190
....*....|....*....|....*....|....*
gi 884884283 199 QEGAN-SMTALIVAVKGGYTQSVKEILKRNPNVNL 232
Cdd:PHA02875 196 YFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
283-391 |
2.04e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 58.88 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 283 VEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATmVRDILQC------NPDT-EICtkdGETPLIkaTKMRN---IEVV 352
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEK-VKDIVRLlleagaDVNApERC---GFTPLH--LYLYNattLDVI 100
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 884884283 353 ELLLDKGAKVSAVDKKGDTPLHIAIRGRS--RKLAELLLRN 391
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRK 141
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
314-390 |
2.27e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.14 E-value: 2.27e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 884884283 314 GNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLR 390
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
24-78 |
3.06e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 51.58 E-value: 3.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 884884283 24 LLEKC-KDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISA 78
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
237-290 |
3.98e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 3.98e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 884884283 237 GNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALL 290
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
13-58 |
4.52e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 4.52e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 884884283 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELI 58
Cdd:pfam13637 9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
71-124 |
5.95e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 5.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 884884283 71 NWTALISASKEGHVHIVEELLRCGVNVEHRDMGGWTALMWACYKGRTDVVELLL 124
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
338-389 |
7.83e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 7.83e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 884884283 338 TPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLL 389
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
205-257 |
1.07e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 1.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 884884283 205 MTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
104-158 |
1.48e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.58 E-value: 1.48e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 884884283 104 GWTALMWACYKGRTDVVELLLSHGANPSVTGLQySVYPIIWAAGRGHADIVHLLL 158
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
6-175 |
2.71e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 54.97 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 6 SQSVINY-VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEGHV 84
Cdd:PHA02874 124 LKTFLHYaIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 85 HIVEELLRCGVNVEHRDMGGWTALMWACYKGRTdVVELLLShgaNPSV--------TGLQYSV-YPIiwaagrgHADIVH 155
Cdd:PHA02874 204 ACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLIN---NASIndqdidgsTPLHHAInPPC-------DIDIID 272
|
170 180
....*....|....*....|
gi 884884283 156 LLLQNGAKVNCSDKYGTTPL 175
Cdd:PHA02874 273 ILLYHKADISIKDNKGENPI 292
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
157-211 |
3.84e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.50 E-value: 3.84e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 884884283 157 LLQNG-AKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVA 211
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
171-221 |
4.75e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.04 E-value: 4.75e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 884884283 171 GTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVK 221
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1-129 |
8.69e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.52 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 1 MSVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQ--GNLEIVKELIKSGAN--------------- 63
Cdd:PHA03100 69 STPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANvniknsdgenllhly 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 64 --CNLEDLD----------------------------------NWTALISASKEGHVHIVEELLRCGVNVEHRDMGGWTA 107
Cdd:PHA03100 149 leSNKIDLKilkllidkgvdinaknrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
|
170 180
....*....|....*....|..
gi 884884283 108 LMWACYKGRTDVVELLLSHGAN 129
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLNNGPS 250
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
146-257 |
1.14e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 146 AGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmtalivavkggytqsvkeilk 225
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD----------------------------- 140
|
90 100 110
....*....|....*....|....*....|..
gi 884884283 226 rnpnVNLTDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:PTZ00322 141 ----PTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
38-66 |
1.53e-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: 46.04 E-value: 1.53e-06
10 20
....*....|....*....|....*....
gi 884884283 38 GQTPLMIAAEQGNLEIVKELIKSGANCNL 66
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
178-423 |
1.92e-06 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 52.78 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 178 AARKGHLECVKHLLAMGADVDQEGANSM--TALIVAVKGGYTQSVKEILKRNPNVNLTdkdGNTALMIASKEGHtEIVQD 255
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPKKLNINCPDRLgrSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISLEYV-DAVEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 256 LL--------DAGTYVNIPDRSGD------TVLIGAVRGGHVEIVRALLQKYADIDIRGqdnktalywaveKGNATMVRD 321
Cdd:TIGR00870 100 ILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARA------------CGDFFVKSQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 322 ILQcnpdteiCTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAI-----RGRSRKLA----ELLLR-- 390
Cdd:TIGR00870 168 GVD-------SFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefKAEYEELScqmyNFALSll 240
|
250 260 270
....*....|....*....|....*....|....*
gi 884884283 391 -NPKDGRLLYR-PNKAGETPYNIDCSHQKSILTQI 423
Cdd:TIGR00870 241 dKLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRL 275
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
52-235 |
2.02e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 52.44 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 52 EIVKELIKSGANCNLEDLDNWTAL---ISASKEGHVHIVEELLRCGVNV-EHRDMGGWTAL-MW-ACYKGRTDVVELLLS 125
Cdd:PHA02989 89 KIVKLLLKFGADINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVnDVKNSRGYNLLhMYlESFSVKKDVIKILLS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 126 HGANPSVTGLQYSVYPI-IWAagRGHADIVHL-----LLQNGA------------------------------------- 162
Cdd:PHA02989 169 FGVNLFEKTSLYGLTPMnIYL--RNDIDVISIkvikyLIKKGVnietnnngsesvlesfldnnkilskkefkvlnfilky 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 884884283 163 -KVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDK 235
Cdd:PHA02989 247 iKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLKPGKYLIKK 320
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
226-277 |
2.40e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 2.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 884884283 226 RNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGA 277
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
52-291 |
3.69e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 51.67 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 52 EIVKELIKSGANCNLED---------LDNWTalISASKegHVHIVEELLRCGVNVEHRDMGGWTALMWACYK---GRTDV 119
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGyietplcavLRNRE--ITSNK--IKKIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 120 VELLLSHGAN-PSVTGLQ-YSVYPIIWAAGRGHADIVHLLLQNGakVNCSDK---YGTTPLVWAARKG----HLECVKHL 190
Cdd:PHA02989 127 LRFLLSKGINvNDVKNSRgYNLLHMYLESFSVKKDVIKILLSFG--VNLFEKtslYGLTPMNIYLRNDidviSIKVIKYL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 191 LAMGADVDQEGANSMTALIVAVKGGYTQSVKE------ILKRnPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVN 264
Cdd:PHA02989 205 IKKGVNIETNNNGSESVLESFLDNNKILSKKEfkvlnfILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIY 283
|
250 260
....*....|....*....|....*..
gi 884884283 265 IPDRSGDTVLIGAVRGGHVEIVRALLQ 291
Cdd:PHA02989 284 NVSKDGDTVLTYAIKHGNIDMLNRILQ 310
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
5-231 |
3.77e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 51.76 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 5 ISQSVINYVEEENIpaLKALLEKCKDVDERNECGQTPLMIAAEQG---NLEIVKELIKSGANCNLEDLDNWTALISASKE 81
Cdd:PHA02798 78 ILSNIKDYKHMLDI--VKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 82 GH---VHIVEELLRCGVNV-EHRDMGGWTALmwACY------KGRTDVVELLLSHG------ANPSVTGLQYSVYPIIWA 145
Cdd:PHA02798 156 NHhidIEIIKLLLEKGVDInTHNNKEKYDTL--HCYfkynidRIDADILKLFVDNGfiinkeNKSHKKKFMEYLNSLLYD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 146 AGRGHADIVHLLLQNgAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILK 225
Cdd:PHA02798 234 NKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILN 312
|
....*.
gi 884884283 226 RNPNVN 231
Cdd:PHA02798 313 KKPNKN 318
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
38-68 |
3.78e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 44.97 E-value: 3.78e-06
10 20 30
....*....|....*....|....*....|..
gi 884884283 38 GQTPLMIAAEQ-GNLEIVKELIKSGANCNLED 68
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-133 |
6.42e-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: 44.20 E-value: 6.42e-06
10 20 30
....*....|....*....|....*....|.
gi 884884283 104 GWTALMWACYK-GRTDVVELLLSHGANPSVT 133
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
51-328 |
6.48e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 50.99 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 51 LEIVKELIKSganCNLEDLDNWTALISA---SKEGHVHIVEELLRCGVNVEHRDMGGWTALmwaC--------YKGRTDV 119
Cdd:PHA02798 18 LSTVKLLIKS---CNPNEIVNEYSIFQKylqRDSPSTDIVKLFINLGANVNGLDNEYSTPL---CtilsnikdYKHMLDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 120 VELLLSHGANPSVTGL--QYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECVKHLLAMG 194
Cdd:PHA02798 92 VKILIENGADINKKNSdgETPLYCLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 195 ADVDQ----EGANSMTALIvavKGGYTQSVKEILKRNPN----VNLTDKDGNTALM-------IASKEGHTEIVQDLLda 259
Cdd:PHA02798 172 VDINThnnkEKYDTLHCYF---KYNIDRIDADILKLFVDngfiINKENKSHKKKFMeylnsllYDNKRFKKNILDFIF-- 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 884884283 260 gTYVNIPDRS--GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPD 328
Cdd:PHA02798 247 -SYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
104-132 |
6.92e-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: 6.92e-06
10 20
....*....|....*....|....*....
gi 884884283 104 GWTALMWACYKGRTDVVELLLSHGANPSV 132
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
12-174 |
7.13e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 49.05 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 12 YVEEENIPALKALLekcKDVDERNECGQTPLMIAAEQ--GNLEIVKELIKSGANCNLEDLD-NWTAL---ISASKEGHVH 85
Cdd:PHA02859 28 YVEKDDIEGVKKWI---KFVNDCNDLYETPIFSCLEKdkVNVEILKFLIENGADVNFKTRDnNLSALhhyLSFNKNVEPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 86 IVEELLRCGVNVEHRDMGGWTAL-MWAC-YKGRTDVVELLLSHGANPsvTGLQYSVYPIIWAAGRGHAD--IVHLLLQNG 161
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLhMYMCnFNVRINVIKLLIDSGVSF--LNKDFDNNNILYSYILFHSDkkIFDFLTSLG 182
|
170
....*....|...
gi 884884283 162 AKVNCSDKYGTTP 174
Cdd:PHA02859 183 IDINETNKSGYNC 195
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
54-126 |
9.98e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.28 E-value: 9.98e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 884884283 54 VKELIKSGANCNLEDLDNWTALISASKEGHVHIVEELLRCGVNVEHRDMGGWTALMWACYKGRTDVVELLLSH 126
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
211-411 |
1.28e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 49.67 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 211 AVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVL--IGAVRGGHVEIVRA 288
Cdd:PHA02946 46 GIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 289 LLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGAKVSAVD 366
Cdd:PHA02946 126 LVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 884884283 367 KKGDTPLHIAIRGRSRKLAELLLRNPKDGrlLYRPNKAGETPYNI 411
Cdd:PHA02946 206 HDGNTPLHIVCSKTVKNVDIINLLLPSTD--VNKQNKFGDSPLTL 248
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
37-65 |
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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 43.40 E-value: 1.36e-05
10 20
....*....|....*....|....*....
gi 884884283 37 CGQTPLMIAAEQGNLEIVKELIKSGANCN 65
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
236-268 |
1.43e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 43.43 E-value: 1.43e-05
10 20 30
....*....|....*....|....*....|....
gi 884884283 236 DGNTALMIAS-KEGHTEIVQDLLDAGTYVNIPDR 268
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
123-175 |
2.02e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 2.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 884884283 123 LLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPL 175
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
349-413 |
2.31e-05 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 46.41 E-value: 2.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 884884283 349 IEVVELLLDKGAKVSAVDKK-GDTPLHIAIRGRSRKLAELLLRNPKDGRLLYrpNKAGETPYNIDC 413
Cdd:PHA02736 71 QEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEIL--NYAFKTPYYVAC 134
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
170-198 |
3.46e-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: 3.46e-05
10 20
....*....|....*....|....*....
gi 884884283 170 YGTTPLVWAARKGHLECVKHLLAMGADVD 198
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-132 |
6.06e-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: 6.06e-05
10 20
....*....|....*....|....*....
gi 884884283 104 GWTALMWACYKGRTDVVELLLSHGANPSV 132
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
30-257 |
6.85e-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: 47.57 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 30 DVDERNECGQTPLMIAA---EQGNLEIVKELIKSGancnlEDLDNWTALISASkeghvhIVEELLRcgvnvehrdmgGWT 106
Cdd:cd21882 18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAA-----PDSGNPKELVNAP------CTDEFYQ-----------GQT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 107 ALMWACYKGRTDVVELLLSHGANPSV------------TGLQYSVYPIIWAAGRGHADIVHLLLQNGAK---VNCSDKYG 171
Cdd:cd21882 76 ALHIAIENRNLNLVRLLVENGADVSAratgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 172 TTplvwaarkghlecVKHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrnpnvnlTDKDGNTALMIASK 246
Cdd:cd21882 156 NT-------------VLHALVLQADNTPENSAFVCQmynllLSYGAHLDPTQQLEEI---------PNHQGLTPLKLAAV 213
|
250
....*....|.
gi 884884283 247 EGHTEIVQDLL 257
Cdd:cd21882 214 EGKIVMFQHIL 224
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
170-199 |
7.17e-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: 7.17e-05
10 20 30
....*....|....*....|....*....|.
gi 884884283 170 YGTTPLVWAA-RKGHLECVKHLLAMGADVDQ 199
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
305-356 |
7.60e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 7.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 884884283 305 TALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLL 356
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
117-209 |
7.99e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 46.51 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 117 TDVVELLLSHGANPSV---TGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGT-TPLVWAARKGHLECVKHLLA 192
Cdd:PHA02884 46 TDIIDAILKLGADPEApfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLS 125
|
90
....*....|....*..
gi 884884283 193 MGADVDQEgANSMTALI 209
Cdd:PHA02884 126 YGADINIQ-TNDMVTPI 141
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
284-451 |
8.05e-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: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 284 EIVRALLQ--------------KYADIDIRGQdnkTALYWAVEKGNATMVRDILQCNPDTEICTKD-------------- 335
Cdd:cd22194 111 EIVRILLAfaeengildrfinaEYTEEAYEGQ---TALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyf 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 336 GETPLIKATKMRNIEVVELLLDKGAK-VSAVDKKGDTPLH----IAIRGRSR-----KLAELLLRNPKDGRLLYRPNKAG 405
Cdd:cd22194 188 GETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHalvtVAEDSKTQndfvkRMYDMILLKSENKNLETIRNNEG 267
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 884884283 406 ETPYNIDCSHQK-SILTQIFG-------ARHLSPTETDgdmLGYDLYSSALADI 451
Cdd:cd22194 268 LTPLQLAAKMGKaEILKYILSreikekpNRSLSRKFTD---WAYGPVSSSLYDL 318
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
90-133 |
8.91e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 8.91e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 884884283 90 LLRCG-VNVEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVT 133
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK 45
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
152-257 |
9.87e-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: 47.06 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 152 DIVHLLLQNGAKVNCSDK--------------YGTTPLVWAARKGHLECVKHLLAMGADV----DQEGANSMTALIVAVK 213
Cdd:cd22194 155 DIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKESTDitsqDSRGNTVLHALVTVAE 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 884884283 214 GGYTQ--SVKE----ILKRNPNVNL---TDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:cd22194 235 DSKTQndFVKRmydmILLKSENKNLetiRNNEGLTPLQLAAKMGKAEILKYIL 287
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
95-257 |
1.09e-04 |
|
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: 47.11 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 95 VNVEHRD--MGGWTALMWACYKGRTDVVELLLSHGA-------------NPSVTGLQYSVYPIIWAAGRGHADIVHLLLQ 159
Cdd:cd22196 83 VNAAYTDsyYKGQTALHIAIERRNMHLVELLVQNGAdvharasgeffkkKKGGPGFYFGELPLSLAACTNQLDIVKFLLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 160 N---GAKVNCSDKYGTTplvwaarkghlecVKHLLAMGADVDQEGANSMTALivavkggYTQSVKEILKRNPNVNL---T 233
Cdd:cd22196 163 NphsPADISARDSMGNT-------------VLHALVEVADNTPENTKFVTKM-------YNEILILGAKIRPLLKLeeiT 222
|
170 180
....*....|....*....|....
gi 884884283 234 DKDGNTALMIASKEGHTEIVQDLL 257
Cdd:cd22196 223 NKKGLTPLKLAAKTGKIGIFAYIL 246
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
303-437 |
1.47e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.14 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 303 NKTALYWAVEKGNATMVRDILQC--NPDTEIctKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAI-RG 379
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIgiNPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVeEG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 884884283 380 RSRKLAELLLRNPKDGRLLYrpnKAGETPYNIDCSHQKSILTQIFGARHLSPTETDGD 437
Cdd:PHA02875 80 DVKAVEELLDLGKFADDVFY---KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
274-394 |
1.55e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.14 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 274 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVE 353
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 884884283 354 LLLDKGAKVSAV-DKKGDTPLHIAIRGRSRKLAELLLRNPKD 394
Cdd:PHA02875 86 ELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
270-320 |
1.86e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 1.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 884884283 270 GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVR 320
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
339-424 |
2.35e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 45.64 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 339 PLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLRNPKDGRLLYRPNKAGETPYNIDCSHQKS 418
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
|
....*.
gi 884884283 419 ILTQIF 424
Cdd:PHA02878 120 ILTNRY 125
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
22-103 |
2.36e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 22 KALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKSGANCNLEDLDNWTALISASKEGHVHIVEELLRCgvNVEHRD 101
Cdd:PTZ00322 99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH--SQCHFE 176
|
..
gi 884884283 102 MG 103
Cdd:PTZ00322 177 LG 178
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
269-356 |
2.55e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 269 SGDTVliGAvrgghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN 348
Cdd:PTZ00322 92 SGDAV--GA---------RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
....*...
gi 884884283 349 IEVVELLL 356
Cdd:PTZ00322 161 REVVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
189-290 |
2.82e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.66 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 189 HLLAMGADVDQEGANSMTA-LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPD 267
Cdd:PTZ00322 66 HNLTTEEVIDPVVAHMLTVeLCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
|
90 100
....*....|....*....|...
gi 884884283 268 RSGDTVLIGAVRGGHVEIVRALL 290
Cdd:PTZ00322 146 KDGKTPLELAEENGFREVVQLLS 168
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
191-394 |
3.76e-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: 45.46 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 191 LAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNP--NVNLTDKDGNTALMIASKEGHTEIVQDLLdagTYVNIPDR 268
Cdd:TIGR00870 4 LDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELL---LNLSCRGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 269 SGDTvLIGAVRGGHVEIVRALLQKYADIDiRGQDNktaLYWAVEKGNATMVRDIlqcnpdteictkdgeTPLIKATKMRN 348
Cdd:TIGR00870 81 VGDT-LLHAISLEYVDAVEAILLHLLAAF-RKSGP---LELANDQYTSEFTPGI---------------TALHLAAHRQN 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 349 IEVVELLLDKGAKVSA-------VDKKGDT-------PLHIAIRGRSRKLAELLLRNPKD 394
Cdd:TIGR00870 141 YEIVKLLLERGASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPAD 200
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
335-367 |
4.20e-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: 39.19 E-value: 4.20e-04
10 20 30
....*....|....*....|....*....|....
gi 884884283 335 DGETPLIKA-TKMRNIEVVELLLDKGAKVSAVDK 367
Cdd:pfam00023 1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
95-257 |
4.76e-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: 44.79 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 95 VNVEHRDMG--GWTALMWACYKGRTDVVELLLSHGA-----------NPSV--TGLQYSVYPIIWAAGRGHADIVHLLLQ 159
Cdd:cd22193 65 INAEYTDEYyeGQTALHIAIERRQGDIVALLVENGAdvhahakgrffQPKYqgEGFYFGELPLSLAACTNQPDIVQYLLE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 160 NG---AKVNCSDKYGTTPLvwaarkghlecvkHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrnpnvn 231
Cdd:cd22193 145 NEhqpADIEAQDSRGNTVL-------------HALVTVADNTKENTKFVTRmydmiLIRGAKLCPTVELEEI-------- 203
|
170 180
....*....|....*....|....*.
gi 884884283 232 lTDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:cd22193 204 -RNNDGLTPLQLAAKMGKIEILKYIL 228
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
322-376 |
5.66e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 5.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 884884283 322 ILQCNP-DTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIA 376
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
141-169 |
5.99e-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: 5.99e-04
10 20 30
....*....|....*....|....*....|
gi 884884283 141 PIIWAAGR-GHADIVHLLLQNGAKVNCSDK 169
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
70-101 |
1.38e-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: 37.65 E-value: 1.38e-03
10 20 30
....*....|....*....|....*....|...
gi 884884283 70 DNWTAL-ISASKEGHVHIVEELLRCGVNVEHRD 101
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
173-198 |
1.71e-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: 1.71e-03
10 20
....*....|....*....|....*.
gi 884884283 173 TPLVWAARKGHLECVKHLLAMGADVD 198
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
236-265 |
2.50e-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: 36.80 E-value: 2.50e-03
10 20 30
....*....|....*....|....*....|
gi 884884283 236 DGNTALMIASKEGHTEIVQDLLDAGTYVNI 265
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
335-364 |
3.36e-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: 3.36e-03
10 20 30
....*....|....*....|....*....|
gi 884884283 335 DGETPLIKATKMRNIEVVELLLDKGAKVSA 364
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
120-204 |
3.43e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.19 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 120 VELLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQ 199
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRT-PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
|
....*
gi 884884283 200 EGANS 204
Cdd:PTZ00322 177 LGANA 181
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
294-343 |
3.71e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 3.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 884884283 294 ADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKA 343
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
256-307 |
3.82e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 3.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 884884283 256 LLDAGTY-VNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 307
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
32-191 |
4.11e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 41.76 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 32 DERNECGQTPLMIAAEQGNleiVKELIKsgANCNLEDLDNWTALISASKEGHVHIVEELLRCGVNVEHRDMG-------- 103
Cdd:cd22197 60 DGVNACIMPLLEIDKDSGN---PKPLVN--AQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 104 -----GWTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHAD--------IVHL---LLQNGAKVNCS 167
Cdd:cd22197 135 tcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQDSLGNTVLHALVMIADnspensalVIKMydgLLQAGARLCPT 214
|
170 180 190
....*....|....*....|....*....|.
gi 884884283 168 DKY-------GTTPLVWAARKGHLECVKHLL 191
Cdd:cd22197 215 VQLeeisnheGLTPLKLAAKEGKIEIFRHIL 245
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
270-298 |
4.25e-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: 4.25e-03
10 20
....*....|....*....|....*....
gi 884884283 270 GDTVLIGAVRGGHVEIVRALLQKYADIDI 298
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
297-409 |
5.57e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.80 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884283 297 DIRGQdnkTALYWAVEKGNATMVRDILQCNPDTEICtkDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIA 376
Cdd:PHA02791 27 DVHGH---SALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYA 101
|
90 100 110
....*....|....*....|....*....|...
gi 884884283 377 IRGRSRKLAELLLRnpKDGRLLYRPNKAGETPY 409
Cdd:PHA02791 102 VDSGNMQTVKLFVK--KNWRLMFYGKTGWKTSF 132
|
|
| PHA02743 |
PHA02743 |
Viral ankyrin protein; Provisional |
352-411 |
5.64e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 39.41 E-value: 5.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 884884283 352 VELLLDKGAKVSAVDKK-GDTPLHIAIRGRSRKLAELLLRNPkdGRLLYRPNKAGETPYNI 411
Cdd:PHA02743 76 IELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCRQL--GVNLGAINYQHETAYHI 134
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
270-299 |
5.87e-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: 5.87e-03
10 20 30
....*....|....*....|....*....|.
gi 884884283 270 GDTVL-IGAVRGGHVEIVRALLQKYADIDIR 299
Cdd:pfam00023 2 GNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
141-166 |
7.67e-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: 7.67e-03
|
| |
