|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
18-306 |
1.27e-63 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 219.06 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 18 IPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCGANL 97
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 98 EHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWA 177
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 178 ARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLD 257
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720373277 258 AGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 306
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
16-273 |
3.08e-61 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 212.12 E-value: 3.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 16 ENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCGA 95
Cdd:COG0666 32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 96 NLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLV 175
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 176 WAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDL 255
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
250
....*....|....*...
gi 1720373277 256 LDAGTYVNIPDRSGDTVL 273
Cdd:COG0666 272 LLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
84-372 |
2.88e-59 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 206.34 E-value: 2.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 84 IHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKV 163
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 164 NCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIA 243
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 244 SKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQ 323
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720373277 324 CNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPL 372
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
10-240 |
8.87e-59 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 204.80 E-value: 8.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 10 INYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEE 89
Cdd:COG0666 59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 90 LLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKY 169
Cdd:COG0666 139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720373277 170 GTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTAL 240
Cdd:COG0666 219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| KAP_NTPase |
pfam07693 |
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases ... |
440-953 |
2.13e-57 |
|
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases are sporadically distributed across a wide phylogenetic range in bacteria and in animals. Many of the prokaryotic KAP NTPases are encoded in plasmids and tend to undergo disruption to form pseudogenes. A unique feature of all eukaryotic and certain bacterial KAP NTPases is the presence of two or four transmembrane helices inserted into the P-loop NTPase domain. These transmembrane helices anchor KAP NTPases in the membrane such that the P-loop domain is located on the intracellular side.
Pssm-ID: 462231 Cd Length: 293 Bit Score: 201.07 E-value: 2.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 440 YDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFagqqieplfqfswlivflilllcgglglvfaft 519
Cdd:pfam07693 1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 520 vdtnlaiavslsflallyiffiviyfggrqegeswnwawalstrlarhigylellfklmfvnppelpeqttkalPVRFLF 599
Cdd:pfam07693 48 --------------------------------------------------------------------------NEEFII 53
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 600 TDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDSQGKKK--WKKTCCLPSFIIFLFIVGciiagitll 677
Cdd:pfam07693 54 VYFNPWSFSGQDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKigLIFGVAIILALTGLVVAI--------- 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 678 aifrvdpkhltvnailisiasivglafvlncrtwwqvldsllnsqrkrlhsaasklhklksEGFMKVLKCEV-ELMARMA 756
Cdd:pfam07693 125 -------------------------------------------------------------EEPMKKLQTEIeELRSDIE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 757 KTIDSftqNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLrdsNINGHDYMRN 836
Cdd:pfam07693 144 STLKD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPNVVFILAADEEILKKALEANYESGL---EIDGQKYLEK 217
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 837 IVHLPVFLNSRGLSNARKFLVTSAtngdiscseatgvqedadrrvsQNSLGEMTKLGSKTALnrrdtyrrrqmqrtitrq 916
Cdd:pfam07693 218 IIQVPFTLPPLSLRQLKKFLMLSF----------------------DNSEEGTSSKDRDETL------------------ 257
|
490 500 510
....*....|....*....|....*....|....*..
gi 1720373277 917 MSFDLTKLLVTEDwFSDISPQTMRRLLNIVSVTGRLL 953
Cdd:pfam07693 258 RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
140-393 |
1.13e-55 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 195.94 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 140 PIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSV 219
Cdd:COG0666 24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 220 KEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRG 299
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 300 QDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGR 379
Cdd:COG0666 184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
|
250
....*....|....
gi 1720373277 380 SRRLAELLLRNPKD 393
Cdd:COG0666 264 AALIVKLLLLALLL 277
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
150-414 |
5.23e-53 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 188.24 E-value: 5.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 150 ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 229
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 230 NLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWA 309
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 310 VEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLLr 389
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL- 239
|
250 260
....*....|....*....|....*
gi 1720373277 390 npKDGRLLYRPNKAGETPYNIDCSH 414
Cdd:COG0666 240 --EAGADLNAKDKDGLTALLLAAAA 262
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
42-133 |
2.66e-27 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 107.12 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 42 LMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCgANLEHRDMgGWTALMWACYKGRTDVVE 121
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1720373277 122 LLLSHGANPSVT 133
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
49-377 |
2.78e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 116.99 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 49 GNVEIVKELIKNGANC-NLEDLDNWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHG 127
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCiNISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 128 ANPSVTGLysvyPIIwaagrgHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmtal 207
Cdd:PHA02874 92 VDTSILPI----PCI------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 208 ivavkggytqsvkeilkrnpnVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRA 287
Cdd:PHA02874 150 ---------------------VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 288 LLQKYADIDIRGQDNKTALYWAVEKGNATMvrDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGARVSAVDK 366
Cdd:PHA02874 209 LIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDN 286
|
330
....*....|.
gi 1720373277 367 KGDTPLHVAIR 377
Cdd:PHA02874 287 KGENPIDTAFK 297
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
43-361 |
6.83e-26 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 113.58 E-value: 6.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 43 MIAAEQGNVEIVKELIKNGANCNLEDLDNWTAL---ISASKEGHIHIVEELLKCGANLEHRDMGGWTAL-MWACYKGRTD 118
Cdd:PHA03095 19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 119 VVELLLSHGANPSVTGLYSVYPI-IWAAG-RGHADIVHLLLQNGAKVNCSDKYGTTPL-VWAARKG-HLECVKHLLAMGA 194
Cdd:PHA03095 99 VIKLLIKAGADVNAKDKVGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNaNVELLRLLIDAGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 195 DVDQEGANSMTAL---IVAVKgGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIE--IVQDLLDAGTYVNIPDRSG 269
Cdd:PHA03095 179 DVYAVDDRFRSLLhhhLQSFK-PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 270 DTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTE-------ICTKDGETPLIKA 342
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAEtvaatlnTASVAGGDIPSDA 337
|
330
....*....|....*....
gi 1720373277 343 TKmrnIEVVELLLDKGARV 361
Cdd:PHA03095 338 TR---LCVAKVVLRGAFSL 353
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
2-399 |
1.88e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 114.39 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 2 SVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKE 81
Cdd:PHA02876 142 SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 82 GHIHIVEELLKCGANLEHRDMGGWTALmwacykgRTDVVELLLshganpsvtglysvypiiwaagrghadivhLLLQNGA 161
Cdd:PHA02876 222 KNIDTIKAIIDNRSNINKNDLSLLKAI-------RNEDLETSL------------------------------LLYDAGF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 162 KVNCSDKYGTTPLVWAARKGHL-ECVKHLLAMGADVDQEGANSMTALIVAVKGGY-TQSVKEILKRNPNVNLTDKDGNTA 239
Cdd:PHA02876 265 SVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 240 LMIASK-EGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATM- 317
Cdd:PHA02876 345 LHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMs 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 318 VRDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSrrLAELLLR---NPKD 393
Cdd:PHA02876 425 VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHygaELRD 502
|
....*.
gi 1720373277 394 GRLLYR 399
Cdd:PHA02876 503 SRVLHK 508
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
12-297 |
5.33e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 110.14 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 12 YVEEENIPALKALLEKCkDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHI--HIVEe 89
Cdd:PHA03100 10 SRIIKVKNIKYIIMEDD-LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 90 llkcganlehrdmggwtalmwacykgrtdVVELLLSHGANPSVTGLYSVYPIIWAAGR--GHADIVHLLLQNGAKVNCSD 167
Cdd:PHA03100 88 -----------------------------IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 168 KYGTTPLVWAARKGH--LECVKHLLAMGADVDQegansmtalivavkggyTQSVKEILKRNPNVNLTDKDGNTALMIASK 245
Cdd:PHA03100 139 SDGENLLHLYLESNKidLKILKLLIDKGVDINA-----------------KNRVNYLLSYGVPINIKDVYGFTPLHYAVY 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720373277 246 EGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDI 297
Cdd:PHA03100 202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
152-402 |
3.05e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 107.83 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 152 IVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQS-VKEI----LKRN 226
Cdd:PHA03100 17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdVKEIvkllLEYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 227 PNVNLTDKDGNTALMIAS--KEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHV--EIVRALLQKYADIDIrgqdn 302
Cdd:PHA03100 97 ANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 303 KTALYWAVEKGNATMVRDILqcnpdteictkdGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRR 382
Cdd:PHA03100 172 KNRVNYLLSYGVPINIKDVY------------GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
250 260
....*....|....*....|....*
gi 1720373277 383 LAELLLRN-----PKDGRLLYRPNK 402
Cdd:PHA03100 240 IFKLLLNNgpsikTIIETLLYFKDK 264
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
40-278 |
3.76e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 107.74 E-value: 3.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 40 TPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEEL-----------------------LKCGAN 96
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 97 LEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVW 176
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 177 AARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKggYTQSVKEILKRNPNVNLTDKDGNTALMIA-SKEGHIEIVQDL 255
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDIL 274
|
250 260
....*....|....*....|...
gi 1720373277 256 LDAGTYVNIPDRSGDTVLIGAVR 278
Cdd:PHA02874 275 LYHKADISIKDNKGENPIDTAFK 297
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
174-266 |
2.10e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 93.26 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 174 LVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKrNPNVNLTDkDGNTALMIASKEGHIEIVQ 253
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1720373277 254 DLLDAGTYVNIPD 266
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
108-198 |
2.62e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.87 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 108 LMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNgAKVNCSDkYGTTPLVWAARKGHLECVK 187
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|.
gi 1720373277 188 HLLAMGADVDQ 198
Cdd:pfam12796 79 LLLEKGADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
13-101 |
8.62e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.63 E-value: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNgANCNLEDlDNWTALISASKEGHIHIVEELLK 92
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 1720373277 93 CGANLEHRD 101
Cdd:pfam12796 83 KGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
207-298 |
4.38e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 207 LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTyVNIPDrSGDTVLIGAVRGGHVEIVR 286
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1720373277 287 ALLQKYADIDIR 298
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
18-306 |
5.24e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 92.40 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 18 IPALKALLEKCKDVDERNECGQTPLMI--AAEQGNVEIVKELIKNGANCNLEDLDNWT---ALISaSKEGHIHIVEELLK 92
Cdd:PHA03095 97 LDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLK-SRNANVELLRLLID 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 93 CGANLEHRDMGGWTALMWAC--YKGRTDVVELLLSHGANPSVTGLYSVYPIIWAA--GRGHADIVHLLLQNGAKVNCSDK 168
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 169 YGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKdgntALMIASKEGH 248
Cdd:PHA03095 256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGG 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720373277 249 IEIVQDLLDAGTYVNIpdRSGDTVLIGAVRGGHVEIVRALLQKYADI-DIRGQDNKTAL 306
Cdd:PHA03095 332 DIPSDATRLCVAKVVL--RGAFSLLPEPIRAYHADFIRECEAEIAVMrTTRIGTGVSLL 388
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
74-297 |
8.09e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 91.21 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 74 ALISASKEGHIHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIV 153
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 154 HLLLQNGAKVN-CSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLT 232
Cdd:PHA02875 85 EELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720373277 233 DKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGD-TVLIGAVRGGHVEIVRALLQKYADIDI 297
Cdd:PHA02875 165 DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
273-365 |
8.43e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.86 E-value: 8.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 273 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRdILQCNPDTEICTkDGETPLIKATKMRNIEVVE 352
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1720373277 353 LLLDKGARVSAVD 365
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
240-334 |
1.31e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.09 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 240 LMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLqKYADIDIRGqDNKTALYWAVEKGNATMVR 319
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|....*
gi 1720373277 320 DILQCNPDteICTKD 334
Cdd:pfam12796 79 LLLEKGAD--INVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
181-398 |
2.37e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 89.67 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 181 GHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRN--PNVNLTDKDgnTALMIASKEGHIEIVQDLLDA 258
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGaiPDVKYPDIE--SELHDAVEEGDVKAVEELLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 259 GTYVN-IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGET 337
Cdd:PHA02875 91 GKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720373277 338 PLIKATKMRNIEVVELLLDKGARVSAVDKKGD-TPLHVAIRGRSRRLAELLLRNPKDGRLLY 398
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1-197 |
2.90e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 86.26 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 1 MSVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQ--GNVEIVKELIKNGANCNLEDLDNWTALISA 78
Cdd:PHA03100 69 STPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 79 SKEGHI--HIVEELLKCGANLEhrdmggwtalmwacykgRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLL 156
Cdd:PHA03100 149 LESNKIdlKILKLLIDKGVDIN-----------------AKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720373277 157 LQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVD 197
Cdd:PHA03100 212 LDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
13-246 |
8.06e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 85.70 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANC---------------------------- 64
Cdd:PHA02878 45 VEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCsvfytlvaikdafnnrnveifkiiltnr 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 65 --NLEDLDNwTALISASKEGHI--HIVEELLKCGANLEHRDM-GGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVY 139
Cdd:PHA02878 125 ykNIQTIDL-VYIDKKSKDDIIeaEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 140 PIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWA-ARKGHLECVKHLLAMGADVD-QEGANSMTALIVAVKGgyTQ 217
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNaKSYILGLTALHSSIKS--ER 281
|
250 260
....*....|....*....|....*....
gi 1720373277 218 SVKEILKRNPNVNLTDKDGNTALMIASKE 246
Cdd:PHA02878 282 KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
219-389 |
1.05e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.08 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 219 VKEILKRNPNVNLTDKDGNTAL---MIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVE-IVRALLQKYAD 294
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 295 IDIRGQDNKTAL--YWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGARVSAVDKKGDT 370
Cdd:PHA03095 110 VNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRS 189
|
170 180
....*....|....*....|..
gi 1720373277 371 PLH---VAIRGRSRRLAELLLR 389
Cdd:PHA03095 190 LLHhhlQSFKPRARIVRELIRA 211
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-231 |
2.27e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 83.50 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 38 GQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCGA---NLEHRDmgGWTALMWACYK 114
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATIL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 115 GRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGA 194
Cdd:PHA02875 113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720373277 195 DVDQEGAN-SMTALIVAVKGGYTQSVKEILKRNPNVNL 231
Cdd:PHA02875 193 NIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
203-435 |
4.82e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 82.70 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 203 SMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAG---TYVNIPDRSGDTVligavrg 279
Cdd:PHA02874 35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtSILPIPCIEKDMI------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 280 ghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGA 359
Cdd:PHA02874 108 ------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720373277 360 RVSAVDKKGDTPLHVAIRGRSRRLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSILTQIFGARHLSPTETDG 435
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDH---GNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDG 254
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
306-393 |
7.76e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.38 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 306 LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGArvSAVDKKGDTPLHVAIRGRSRRLAE 385
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
....*...
gi 1720373277 386 LLLRNPKD 393
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
31-256 |
9.67e-15 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 79.67 E-value: 9.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 31 VDERNECGQ-----TPLMIAAEQGNVEIVKELIKNgancnlEDLDNW-------TALISASKEGHIHIVEELLKCGANLE 98
Cdd:cd22192 5 LDELHLLQQkriseSPLLLAAKENDVQAIKKLLKC------PSCDLFqrgalgeTALHVAALYDNLEAAVVLMEAAPELV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 99 HRDMG-----GWTALMWACYKGRTDVVELLLSHGA---NPSVTGLYSV-----------YPIIWAAGRGHADIVHLLLQN 159
Cdd:cd22192 79 NEPMTsdlyqGETALHIAVVNQNLNLVRELIARGAdvvSPRATGTFFRpgpknliyygeHPLSFAACVGNEEIVRLLIEH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 160 GAKVNCSDKYGTTPLvwaarkghlecvkHLLAMGAdvDQEGANSMTALIVA-VKGGYTQSVKEIlkrnPNvnltdKDGNT 238
Cdd:cd22192 159 GADIRAQDSLGNTVL-------------HILVLQP--NKTFACQMYDLILSyDKEDDLQPLDLV----PN-----NQGLT 214
|
250
....*....|....*...
gi 1720373277 239 ALMIASKEGHIEIVQDLL 256
Cdd:cd22192 215 PFKLAAKEGNIVMFQHLV 232
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
13-229 |
2.52e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.26 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 13 VEEENIPALKALLEKCKDVDER-NECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELL 91
Cdd:PHA02875 76 VEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 92 KCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLY-SVYPIIWAAGRGHADIVHLLLQNGAKVN----CS 166
Cdd:PHA02875 156 DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNimfmIE 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720373277 167 DKYGTTplvwaarkghLECVKHllaMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 229
Cdd:PHA02875 236 GEECTI----------LDMICN---MCTNLESEAIDALIADIAIRIHKKTIRRDEGFKNNMST 285
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
41-351 |
1.68e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 71.83 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 41 PLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLkcgANLEHRDMG-GWTALMWACYKGRTDV 119
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFyTLVAIKDAFNNRNVEI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 120 VELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKY-GTTPLVWAARKGHLECVKHLLAMGADVDQ 198
Cdd:PHA02878 117 FKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 199 EGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKE-GHIEIVQDLLDAGTYVNIPDR-SGDTVLIGA 276
Cdd:PHA02878 197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSS 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720373277 277 VRGGHVeiVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNpdteICTKDGETPLIKATK--MRNIEVV 351
Cdd:PHA02878 277 IKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN----ICLLKRIKPDIKNSEgfIDNMDCI 347
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
151-319 |
2.12e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 72.21 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 151 DIVHLLLQNGAKVNcsDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN 230
Cdd:PLN03192 508 NVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 231 LTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNiPDRSGDtVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAV 310
Cdd:PLN03192 586 IRDANGNTALWNAISAKHHKIFRILYHFASISD-PHAAGD-LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
|
....*....
gi 1720373277 311 EKGNATMVR 319
Cdd:PLN03192 664 AEDHVDMVR 672
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
219-418 |
3.28e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 71.06 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 219 VKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLD-------AGTYVNIPDrsgdtvligAVRGGHVEIVRALLQK 291
Cdd:PHA02878 53 VKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvFYTLVAIKD---------AFNNRNVEIFKIILTN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 292 YA----DIDIRGQDNKTAlywaVEKGNATMVRDILQCNPDTEICTKD-GETPLIKATKMRNIEVVELLLDKGARVSAVDK 366
Cdd:PHA02878 124 RYkniqTIDLVYIDKKSK----DDIIEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720373277 367 KGDTPLHVAIRGRSRRLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSI 418
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLEN---GASTDARDKCGNTPLHISVGYCKDY 248
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
172-357 |
7.32e-12 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 70.43 E-value: 7.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 172 TPLVWAARKGHLECVKHLLAM-GADVDQEGANSMTALIVAVKGGYTQSVKEILKRNP---NVNLTDK--DGNTALMIASK 245
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvNEPMTSDlyQGETALHIAVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 246 EGHIEIVQDLLDAGTYVNIPdRS---------------GDTVLIGAVRGGHVEIVRALLQKYADIdiRGQDN--KTALYW 308
Cdd:cd22192 99 NQNLNLVRELIARGADVVSP-RAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADI--RAQDSlgNTVLHI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720373277 309 AVEKGNAT----MVRDILQCNP-DTEIC-----TKDGETPLIKATKMRNIEVVELLLDK 357
Cdd:cd22192 176 LVLQPNKTfacqMYDLILSYDKeDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
3-169 |
7.73e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 70.67 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 3 VLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEG 82
Cdd:PLN03192 523 PNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 83 HIHIVEELLKCgANLEHRDMGGwTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAK 162
Cdd:PLN03192 603 HHKIFRILYHF-ASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
|
....*..
gi 1720373277 163 VNCSDKY 169
Cdd:PLN03192 681 VDKANTD 687
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
431-844 |
8.56e-12 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 69.17 E-value: 8.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 431 TETDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGqqieplfqfswlivflilllcg 510
Cdd:COG4928 1 NETEEDLLGRKKYAESLANLIKSSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 511 glglvfaftvdtnlaiavslsflallyifFIVIYFggrqegeswnwawalstrlarhigylellfklmfvNPpelpeqtt 590
Cdd:COG4928 59 -----------------------------VIVVYF-----------------------------------NA-------- 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 591 kalpvrFLFTDYNRLssvggetsLAEMIATLSDACEREfgflatrlfrvfKTEDSQGKKKWKKtcclpsfiiflfivgcI 670
Cdd:COG4928 67 ------WLYDGEEDL--------LAALLSEIAAELEKK------------KKKDKKAAKKLKK----------------Y 104
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 671 IAGITLLAIfrvdpkhltvnailisIASIVGLafvlncrtWWQVLDSLLNSQRKRLHSAASK-LHKLKSEgFMKVLKcev 749
Cdd:COG4928 105 AKRLSKLAL----------------KAGLLGG--------PAEAVAEALKALLKKEYKSKKKsIEAFREE-LEELLK--- 156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 750 ELMARmaktidsftqnqtRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNsvlrdSNIN 829
Cdd:COG4928 157 ELKGK-------------RLVVFIDDLDRCEPDEAIEVLELIKLFFDFPNVVFVLAFDREILEHALKERYG-----EDID 218
|
410
....*....|....*
gi 1720373277 830 GHDYMRNIVHLPVFL 844
Cdd:COG4928 219 AREYLEKIIQVPFRL 233
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
173-376 |
1.14e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.14 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 173 PLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKrnpnVNLTDKDGNTALMI--ASKEGHIE 250
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTLVAIkdAFNNRNVE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 251 IVQDLLdAGTYVNIpdRSGDTVLIGAVRGGHV---EIVRALLQKYADIDIRGQDN-KTALYWAVEKGNATMVRDILQCNP 326
Cdd:PHA02878 116 IFKIIL-TNRYKNI--QTIDLVYIDKKSKDDIieaEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720373277 327 DTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAI 376
Cdd:PHA02878 193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
141-296 |
2.16e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 69.13 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 141 IIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYtQSVK 220
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH-HKIF 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 221 EILKR-----NPNVnltdkdGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADI 295
Cdd:PLN03192 608 RILYHfasisDPHA------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
.
gi 1720373277 296 D 296
Cdd:PLN03192 682 D 682
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
151-380 |
4.08e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 67.60 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 151 DIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLA--MGADVDQEGANSMTA------------LIVAVKGGYT 216
Cdd:PHA02878 51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsiNKCSVFYTLVAIKDAfnnrnveifkiiLTNRYKNIQT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 217 QSVKEILKRNPN-----------------VNLTDKD-GNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVR 278
Cdd:PHA02878 131 IDLVYIDKKSKDdiieaeitklllsygadINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 279 GGHVEIVRALLQKYADIDIRGQDNKTALYWAVEK-GNATMVRDILQCNPDTEI-CTKDGETPLIKAtkMRNIEVVELLLD 356
Cdd:PHA02878 211 HYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSS--IKSERKLKLLLE 288
|
250 260
....*....|....*....|....
gi 1720373277 357 KGARVSAVDKKGDTPLHVAIRGRS 380
Cdd:PHA02878 289 YGADINSLNSYKLTPLSSAVKQYL 312
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
117-357 |
4.88e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 67.17 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 117 TDVVELLLSHGANpsVTGLYSVYPIIWAA------GRGHA-DIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECV 186
Cdd:PHA02798 51 TDIVKLFINLGAN--VNGLDNEYSTPLCTilsnikDYKHMlDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 187 KHLLAMGADVDQEGANSMTALIVAVKGGYT---QSVKEILKRNPNVNL-TDKDGNTALMIASKEG----HIEIVQDLLDA 258
Cdd:PHA02798 129 LFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 259 GTYVNIPDRSGDTVLIGAV-------RGGHVEIVRALLqKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEIC 331
Cdd:PHA02798 209 GFIINKENKSHKKKFMEYLnsllydnKRFKKNILDFIF-SYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINII 287
|
250 260
....*....|....*....|....*.
gi 1720373277 332 TKDGETPLIKATKMRNIEVVELLLDK 357
Cdd:PHA02798 288 TELGNTCLFTAFENESKFIFNSILNK 313
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
98-262 |
6.03e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.59 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 98 EHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWA 177
Cdd:PLN03192 519 EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 178 ARKGHLECVKHLLAMGADVDQEGANSMtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLD 257
Cdd:PLN03192 599 ISAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
|
....*
gi 1720373277 258 AGTYV 262
Cdd:PLN03192 677 NGADV 681
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
203-410 |
7.08e-11 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 66.96 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 203 SMTALIVAVKGGYTQSVKEILKrNPNVNLTDKD--GNTALMIASKEGHIEIVQDLLDAG-TYVNIPDRS----GDTVLIG 275
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLK-CPSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApELVNEPMTSdlyqGETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 276 AVRGGHVEIVRALLQKYADID---------IRGQDNKtaLYWavekgnatmvrdilqcnpdteictkdGETPLIKATKMR 346
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVspratgtffRPGPKNL--IYY--------------------------GEHPLSFAACVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720373277 347 NIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLA----ELLLRNPKDGRL--LYR-PNKAGETPYNI 410
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpLDLvPNNQGLTPFKL 218
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
140-190 |
1.58e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.05 E-value: 1.58e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720373277 140 PIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLL 190
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
193-365 |
2.14e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 66.04 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 193 GADVDQEGANSmtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTV 272
Cdd:PLN03192 518 GEHDDPNMASN---LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 273 LIGAVRGGHVEIVRALLQkYADIdirgQDNKTA---LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIE 349
Cdd:PLN03192 595 LWNAISAKHHKIFRILYH-FASI----SDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669
|
170
....*....|....*.
gi 1720373277 350 VVELLLDKGARVSAVD 365
Cdd:PLN03192 670 MVRLLIMNGADVDKAN 685
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
9-256 |
5.57e-10 |
|
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: 64.33 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 9 VINYVEEENIPALKALLEKCK--DVDERNECGQTPLMIAAEQGNVEIVKELIKNgANCNLEDLDnwTALISASKEGHiHI 86
Cdd:TIGR00870 21 FLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLN-LSCRGAVGD--TLLHAISLEYV-DA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 87 VEELL-------KCGANLEH---RDMG----GWTALMWACYKGRTDVVELLLSHGAN-------------PSVTGLY-SV 138
Cdd:TIGR00870 97 VEAILlhllaafRKSGPLELandQYTSeftpGITALHLAAHRQNYEIVKLLLERGASvparacgdffvksQGVDSFYhGE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 139 YPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTplvwaarkghlecVKHLLAMGADVDQEG---ANSMTALIVAVKGG- 214
Cdd:TIGR00870 177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNT-------------LLHLLVMENEFKAEYeelSCQMYNFALSLLDKl 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720373277 215 -YTQSVKEILKRnpnvnltdkDGNTALMIASKEGHIEIVQDLL 256
Cdd:TIGR00870 244 rDSKELEVILNH---------QGLTPLKLAAKEGRIVLFRLKL 277
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
40-91 |
2.01e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 2.01e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720373277 40 TPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELL 91
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
104-157 |
3.84e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 3.84e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1720373277 104 GWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLL 157
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
24-78 |
7.70e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 53.12 E-value: 7.70e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720373277 24 LLEKC-KDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISA 78
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
71-124 |
9.53e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.05 E-value: 9.53e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1720373277 71 NWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLL 124
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
282-390 |
1.31e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 59.65 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 282 VEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATmVRDILQC------NPDT-EICtkdGETPLIkaTKMRN---IEVV 351
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEK-VKDIVRLlleagaDVNApERC---GFTPLH--LYLYNattLDVI 100
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720373277 352 ELLLDKGARVSAVDKKGDTPLHVAIRGRSRR--LAELLLRN 390
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRK 141
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
236-289 |
2.26e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 2.26e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1720373277 236 GNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALL 289
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
313-389 |
2.40e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.14 E-value: 2.40e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720373277 313 GNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLLR 389
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
13-58 |
2.74e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 2.74e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720373277 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELI 58
Cdd:pfam13637 9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
204-256 |
5.29e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 5.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720373277 204 MTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLL 256
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
87-282 |
5.41e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 57.37 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 87 VEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADI--VHLLLQNGAKVN 164
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 165 CS-DKYGTTPLVwAARKGHLECVKHLLAMGAD---VDQEGANSMTALIVAvKGGYTQSVKEILKRNPNVNLTDKDGNTAL 240
Cdd:PHA02946 135 NSvDEEGCGPLL-ACTDPSERVFKKIMSIGFEariVDKFGKNHIHRHLMS-DNPKASTISWMMKLGISPSKPDHDGNTPL 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720373277 241 MIASKE--GHIEIVqDLLDAGTYVNIPDRSGD---TVLIGAVRGGHV 282
Cdd:PHA02946 213 HIVCSKtvKNVDII-NLLLPSTDVNKQNKFGDsplTLLIKTLSPAHL 258
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
337-388 |
9.25e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 9.25e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720373277 337 TPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLL 388
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
10-290 |
1.19e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 56.29 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 10 INYVEEENIPALKALLEKCKDVDErnEC-GQTPLMIAAEQGNV--EIVKELIKNGANCNLEDLDNwTALISASKEGHI-- 84
Cdd:PHA02989 8 ILYSDTVDKNALEFLLRTGFDVNE--EYrGNSILLLYLKRKDVkiKIVKLLIDNGADVNYKGYIE-TPLCAVLRNREIts 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 85 ----HIVEELLKCGANLEHRDMGGWTALMWACYK---GRTDVVELLLSHGAN-PSVTGL--YSVYPIIWAAGRGHADIVH 154
Cdd:PHA02989 85 nkikKIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFLLSKGINvNDVKNSrgYNLLHMYLESFSVKKDVIK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 155 LLLQNGakVNCSDK---YGTTPLVWAARKG----HLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKE------ 221
Cdd:PHA02989 165 ILLSFG--VNLFEKtslYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNNGSESVLESFLDNNKILSKKEfkvlnf 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720373277 222 ILKRnPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQ 290
Cdd:PHA02989 243 ILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
12-173 |
2.39e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 53.28 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 12 YVEEENIPALKALLekcKDVDERNECGQTPLMIAAEQGNV--EIVKELIKNGANCNLEDLD-NWTAL---ISASKEGHIH 85
Cdd:PHA02859 28 YVEKDDIEGVKKWI---KFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALhhyLSFNKNVEPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 86 IVEELLKCGANLEHRDMGGWTAL-MWAC-YKGRTDVVELLLSHGANP------SVTGLYSVYPIiwaagRGHADIVHLLL 157
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLhMYMCnFNVRINVIKLLIDSGVSFlnkdfdNNNILYSYILF-----HSDKKIFDFLT 179
|
170
....*....|....*.
gi 1720373277 158 QNGAKVNCSDKYGTTP 173
Cdd:PHA02859 180 SLGIDINETNKSGYNC 195
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
156-210 |
2.57e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 2.57e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720373277 156 LLQNG-AKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVA 210
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
170-220 |
3.95e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 3.95e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720373277 170 GTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVK 220
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
51-327 |
5.39e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 54.46 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 51 VEIVKELIKNGANCNLEDLDNWTALISaskeghihIVEELLKcganlehrdmggwtalmwacYKGRTDVVELLLSHGANP 130
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCT--------ILSNIKD--------------------YKHMLDIVKILIENGADI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 131 SVTGLYSVYPIIWAAGRGH---ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECVKHLLAMGADVDQ----EG 200
Cdd:PHA02798 103 NKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThnnkEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 201 ANSMTALIvavKGGYTQSVKEILKRNPNVNLTDKDGNTAlmiaSKEGHIEIVQDLLDAG------------TYVNIPDRS 268
Cdd:PHA02798 183 YDTLHCYF---KYNIDRIDADILKLFVDNGFIINKENKS----HKKKFMEYLNSLLYDNkrfkknildfifSYIDINQVD 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720373277 269 --GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPD 327
Cdd:PHA02798 256 elGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
38-66 |
1.18e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 46.43 E-value: 1.18e-06
10 20
....*....|....*....|....*....
gi 1720373277 38 GQTPLMIAAEQGNVEIVKELIKNGANCNL 66
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
225-276 |
1.47e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 1.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720373277 225 RNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGA 276
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
38-68 |
1.47e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 46.13 E-value: 1.47e-06
10 20 30
....*....|....*....|....*....|..
gi 1720373277 38 GQTPLMIAAEQ-GNVEIVKELIKNGANCNLED 68
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
145-256 |
2.01e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 145 AGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmtalivavkggytqsvkeilk 224
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD----------------------------- 140
|
90 100 110
....*....|....*....|....*....|..
gi 1720373277 225 rnpnVNLTDKDGNTALMIASKEGHIEIVQDLL 256
Cdd:PTZ00322 141 ----PTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
37-65 |
3.10e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 45.33 E-value: 3.10e-06
10 20
....*....|....*....|....*....
gi 1720373277 37 CGQTPLMIAAEQGNVEIVKELIKNGANCN 65
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-133 |
5.54e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 44.59 E-value: 5.54e-06
10 20 30
....*....|....*....|....*....|.
gi 1720373277 104 GWTALMWACYK-GRTDVVELLLSHGANPSVT 133
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
104-132 |
7.06e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 44.12 E-value: 7.06e-06
10 20
....*....|....*....|....*....
gi 1720373277 104 GWTALMWACYKGRTDVVELLLSHGANPSV 132
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
52-234 |
7.12e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 50.90 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 52 EIVKELIKNGANCNLEDLDNWTALISASKEGHIH---IVEELLKCGANL-EHRDMGGWTAL-MW-ACYKGRTDVVELLLS 125
Cdd:PHA02989 89 KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINncdMLRFLLSKGINVnDVKNSRGYNLLhMYlESFSVKKDVIKILLS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 126 HGANP-SVTGLYSVYPI-IWAagRGHADIVHL-----LLQNGA------------------------------------- 161
Cdd:PHA02989 169 FGVNLfEKTSLYGLTPMnIYL--RNDIDVISIkvikyLIKKGVnietnnngsesvlesfldnnkilskkefkvlnfilky 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720373277 162 -KVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDK 234
Cdd:PHA02989 247 iKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLKPGKYLIKK 320
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
5-230 |
1.15e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 50.22 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 5 ISQSVINYVEEENIpaLKALLEKCKDVDERNECGQTPLMIAAEQG---NVEIVKELIKNGANCNLEDLDNWTALISASKE 81
Cdd:PHA02798 78 ILSNIKDYKHMLDI--VKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 82 GH---IHIVEELLKCGANL-EHRDMGGWTALmwACY------KGRTDVVELLLSHG-----ANPSV--TGLYSVYPIIWA 144
Cdd:PHA02798 156 NHhidIEIIKLLLEKGVDInTHNNKEKYDTL--HCYfkynidRIDADILKLFVDNGfiinkENKSHkkKFMEYLNSLLYD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 145 AGRGHADIVHLLLQNgAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILK 224
Cdd:PHA02798 234 NKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILN 312
|
....*.
gi 1720373277 225 RNPNVN 230
Cdd:PHA02798 313 KKPNKN 318
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
46-126 |
1.25e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.28 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 46 AEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLS 125
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
.
gi 1720373277 126 H 126
Cdd:PTZ00322 170 H 170
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
235-267 |
1.37e-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: 1.37e-05
10 20 30
....*....|....*....|....*....|....
gi 1720373277 235 DGNTALMIAS-KEGHIEIVQDLLDAGTYVNIPDR 267
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
123-174 |
1.38e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 1.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720373277 123 LLSHG-ANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPL 174
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
177-422 |
1.44e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.08 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 177 AARKGHLECVKHLLAMGADVDQEGANSM--TALIVAVKGGYTQSVKEILKRNPNVNLTdkdGNTALMIASKEGHiEIVQD 254
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPKKLNINCPDRLgrSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISLEYV-DAVEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 255 LL--------DAGTYVNIPDRSGD------TVLIGAVRGGHVEIVRALLQKYADIDIRGqdnktalywaveKGNATMVRD 320
Cdd:TIGR00870 100 ILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARA------------CGDFFVKSQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 321 ILQcnpdteiCTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAI---------RGRSRRLAELLLR-- 389
Cdd:TIGR00870 168 GVD-------SFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSll 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1720373277 390 -NPKDGRLLYR-PNKAGETPYNIDCSHQKSILTQI 422
Cdd:TIGR00870 241 dKLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRL 275
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
283-450 |
1.55e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 49.76 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 283 EIVRALLQ--------------KYADIDIRGQdnkTALYWAVEKGNATMVRDILQCNPDTEICTKD-------------- 334
Cdd:cd22194 111 EIVRILLAfaeengildrfinaEYTEEAYEGQ---TALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyf 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 335 GETPLIKATKMRNIEVVELLLDKGAR-VSAVDKKGDTPLH----VAIRGRSR-----RLAELLLRNPKDGRLLYRPNKAG 404
Cdd:cd22194 188 GETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHalvtVAEDSKTQndfvkRMYDMILLKSENKNLETIRNNEG 267
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720373277 405 ETPYNIDCSHQK-SILTQIFG-------ARHLSPTETDgdmLGYDLYSSALADI 450
Cdd:cd22194 268 LTPLQLAAKMGKaEILKYILSreikekpNRSLSRKFTD---WAYGPVSSSLYDL 318
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
169-197 |
3.53e-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: 3.53e-05
10 20
....*....|....*....|....*....
gi 1720373277 169 YGTTPLVWAARKGHLECVKHLLAMGADVD 197
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
32-256 |
5.82e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 47.93 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 32 DERNECGQTPLMIAAEQGNVeivKELIKngANCNLEDLDNWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTAlmwa 111
Cdd:cd22197 60 DGVNACIMPLLEIDKDSGNP---KPLVN--AQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQ---- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 112 cykgrtdvvelllshgANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKvncsdkygttPLVWAARKGHLECVKHLLA 191
Cdd:cd22197 131 ----------------KKQGTCFYFGELPLSLAACTKQWDVVNYLLENPHQ----------PASLQAQDSLGNTVLHALV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373277 192 MGADVDQEGansmTALIVAVkggYTQSVKEILKRNPNVNL---TDKDGNTALMIASKEGHIEIVQDLL 256
Cdd:cd22197 185 MIADNSPEN----SALVIKM---YDGLLQAGARLCPTVQLeeiSNHEGLTPLKLAAKEGKIEIFRHIL 245
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-132 |
6.18e-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: 6.18e-05
10 20
....*....|....*....|....*....
gi 1720373277 104 GWTALMWACYKGRTDVVELLLSHGANPSV 132
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
169-198 |
6.38e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 41.51 E-value: 6.38e-05
10 20 30
....*....|....*....|....*....|.
gi 1720373277 169 YGTTPLVWAA-RKGHLECVKHLLAMGADVDQ 198
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
304-355 |
6.56e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 6.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720373277 304 TALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLL 355
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
90-133 |
7.62e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 7.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1720373277 90 LLKCG-ANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVT 133
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK 45
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
210-410 |
1.02e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.97 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 210 AVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVL--IGAVRGGHVEIVRA 287
Cdd:PHA02946 46 GIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 288 LLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGARVSAVD 365
Cdd:PHA02946 126 LVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720373277 366 KKGDTPLHVAIRGRSRRLAELLLRNPKDGrlLYRPNKAGETPYNI 410
Cdd:PHA02946 206 HDGNTPLHIVCSKTVKNVDIINLLLPSTD--VNKQNKFGDSPLTL 248
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
235-363 |
1.04e-04 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.38 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 235 DGNTALMIASKEGHIEIVQDLLD--AGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYadiDIRGQDNKTALYWAVEK 312
Cdd:TIGR00870 16 DEEKAFLPAAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENENLELTELLLNL---SCRGAVGDTLLHAISLE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720373277 313 G----NATMvRDILQCNPDT-------EICTKD---GETPLIKATKMRNIEVVELLLDKGARVSA 363
Cdd:TIGR00870 93 YvdavEAIL-LHLLAAFRKSgplelanDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
188-289 |
1.23e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 188 HLLAMGADVDQEGANSMTA-LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPD 266
Cdd:PTZ00322 66 HNLTTEEVIDPVVAHMLTVeLCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
|
90 100
....*....|....*....|...
gi 1720373277 267 RSGDTVLIGAVRGGHVEIVRALL 289
Cdd:PTZ00322 146 KDGKTPLELAEENGFREVVQLLS 168
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
117-208 |
1.28e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 46.13 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 117 TDVVELLLSHGANPSVTGLYS----VYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGT-TPLVWAARKGHLECVKHLLA 191
Cdd:PHA02884 46 TDIIDAILKLGADPEAPFPLSenskTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLS 125
|
90
....*....|....*..
gi 1720373277 192 MGADVDQEgANSMTALI 208
Cdd:PHA02884 126 YGADINIQ-TNDMVTPI 141
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
60-256 |
1.43e-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: 46.72 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 60 NGANC------NLEDLDNWTALI---SASKEGHihiveelLKCGANLEHRD--MGGWTALMWACYKGRTDVVELLLSHGA 128
Cdd:cd22196 46 TGKTCllkamlNLHNGQNDTISLlldIAEKTGN-------LKEFVNAAYTDsyYKGQTALHIAIERRNMHLVELLVQNGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 129 -------------NPSVTGLY-SVYPIIWAAGRGHADIVHLLLQN---GAKVNCSDKYGTTplvwaarkghlecVKHLLA 191
Cdd:cd22196 119 dvharasgeffkkKKGGPGFYfGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNT-------------VLHALV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373277 192 MGADVDQEGANSMTALivavkggYTQSVKEILKRNPNVNL---TDKDGNTALMIASKEGHIEIVQDLL 256
Cdd:cd22196 186 EVADNTPENTKFVTKM-------YNEILILGAKIRPLLKLeeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
269-319 |
1.57e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 1.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720373277 269 GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVR 319
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
30-256 |
2.27e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 46.03 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 30 DVDERNECGQTPLMIAAeqgnveivkelikngANCNLEDLDNWTALISASKEGHIhiVEELLKCGANLEHRDmgGWTALM 109
Cdd:cd21882 18 SAYQRGATGKTCLHKAA---------------LNLNDGVNEAIMLLLEAAPDSGN--PKELVNAPCTDEFYQ--GQTALH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 110 WACYKGRTDVVELLLSHGANPSV------------TGLY-SVYPIIWAAGRGHADIVHLLLQNGAK---VNCSDKYGTTp 173
Cdd:cd21882 79 IAIENRNLNLVRLLVENGADVSAratgrffrkspgNLFYfGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNT- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 174 lvwaarkghlecVKHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrnpnvnlTDKDGNTALMIASKEGH 248
Cdd:cd21882 158 ------------VLHALVLQADNTPENSAFVCQmynllLSYGAHLDPTQQLEEI---------PNHQGLTPLKLAAVEGK 216
|
....*...
gi 1720373277 249 IEIVQDLL 256
Cdd:cd21882 217 IVMFQHIL 224
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
13-256 |
2.44e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 45.90 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 13 VEEENIPALKALLEKCKDVDERNECGQTP--LM---IAAEQGNVEIVKELIkngaNCNLEDLDNWTALISASKEGHIhiV 87
Cdd:cd22194 53 VSEAAVEELGELLKELKDLSRRRRKTDVPdfLMhklTASDTGKTCLMKALL----NINENTKEIVRILLAFAEENGI--L 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 88 EELLKcgANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSV-------------TGLY-SVYPIIWAAGRGHADIV 153
Cdd:cd22194 127 DRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpkykhEGFYfGETPLALAACTNQPEIV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 154 HLLLQNGAK-VNCSDKYGTTPLvwaarkghlecvkHLLAMGADvDQEGANSMTalivavkggyTQSVKEILKRNPNVNL- 231
Cdd:cd22194 205 QLLMEKESTdITSQDSRGNTVL-------------HALVTVAE-DSKTQNDFV----------KRMYDMILLKSENKNLe 260
|
250 260
....*....|....*....|....*..
gi 1720373277 232 --TDKDGNTALMIASKEGHIEIVQDLL 256
Cdd:cd22194 261 tiRNNEGLTPLQLAAKMGKAEILKYIL 287
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
268-355 |
2.47e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 268 SGDTVliGAvrgghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN 347
Cdd:PTZ00322 92 SGDAV--GA---------RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
....*...
gi 1720373277 348 IEVVELLL 355
Cdd:PTZ00322 161 REVVQLLS 168
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
273-393 |
2.55e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 45.37 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 273 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVE 352
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1720373277 353 LLLDKGARVSAV-DKKGDTPLHVAIRGRSRRLAELLLRNPKD 393
Cdd:PHA02875 86 ELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
348-412 |
2.56e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 43.33 E-value: 2.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720373277 348 IEVVELLLDKGARVSAVDKK-GDTPLHVAIRGRSRRLAELLLRNPKDGRLLYrpNKAGETPYNIDC 412
Cdd:PHA02736 71 QEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEIL--NYAFKTPYYVAC 134
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
302-436 |
3.66e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.98 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 302 NKTALYWAVEKGNATMVRDILQC--NPDTEIctKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAI-RG 378
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIgiNPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVeEG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373277 379 RSRRLAELLLRNPKDGRLLYrpnKAGETPYNIDCSHQKSILTQIFGARHLSPTETDGD 436
Cdd:PHA02875 80 DVKAVEELLDLGKFADDVFY---KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
104-256 |
3.73e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 45.17 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 104 GWTALMWACYKGRTDVVELLLSHGA-----------NPSVTGLYSVY---PIIWAAGRGHADIVHLLLQNG---AKVNCS 166
Cdd:cd22193 76 GQTALHIAIERRQGDIVALLVENGAdvhahakgrffQPKYQGEGFYFgelPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 167 DKYGTTPLvwaarkghlecvkHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrnpnvnlTDKDGNTALM 241
Cdd:cd22193 156 DSRGNTVL-------------HALVTVADNTKENTKFVTRmydmiLIRGAKLCPTVELEEI---------RNNDGLTPLQ 213
|
170
....*....|....*
gi 1720373277 242 IASKEGHIEIVQDLL 256
Cdd:cd22193 214 LAAKMGKIEILKYIL 228
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
57-108 |
3.82e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 3.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720373277 57 LIKNG-ANCNLEDLDNWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTAL 108
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
90-157 |
4.09e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.27 E-value: 4.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373277 90 LLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLL 157
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
120-203 |
4.64e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 120 VELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQE 199
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
|
....
gi 1720373277 200 GANS 203
Cdd:PTZ00322 178 GANA 181
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
354-410 |
4.79e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 4.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373277 354 LLDKG-ARVSAVDKKGDTPLHVAIRGRSRRLAELLLRNPKDGRLlyrPNKAGETPYNI 410
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL---KDEEGLTALDL 55
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
140-168 |
5.32e-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: 5.32e-04
10 20 30
....*....|....*....|....*....|
gi 1720373277 140 PIIWAAGR-GHADIVHLLLQNGAKVNCSDK 168
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
235-264 |
6.19e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 6.19e-04
10 20 30
....*....|....*....|....*....|
gi 1720373277 235 DGNTALMIASKEGHIEIVQDLLDAGTYVNI 264
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
334-366 |
6.48e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.81 E-value: 6.48e-04
10 20 30
....*....|....*....|....*....|....
gi 1720373277 334 DGETPLIKA-TKMRNIEVVELLLDKGARVSAVDK 366
Cdd:pfam00023 1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
70-101 |
7.51e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.42 E-value: 7.51e-04
10 20 30
....*....|....*....|....*....|...
gi 1720373277 70 DNWTAL-ISASKEGHIHIVEELLKCGANLEHRD 101
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
22-103 |
9.32e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 22 KALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCgaNLEHRD 101
Cdd:PTZ00322 99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH--SQCHFE 176
|
..
gi 1720373277 102 MG 103
Cdd:PTZ00322 177 LG 178
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
338-423 |
1.16e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 43.72 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 338 PLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLLRNPKDGRLLYRPNKAGETPYNIDCSHQKS 417
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
|
....*.
gi 1720373277 418 ILTQIF 423
Cdd:PHA02878 120 ILTNRY 125
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
172-197 |
1.74e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.62 E-value: 1.74e-03
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
321-375 |
1.76e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720373277 321 ILQCNP-DTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVA 375
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
255-306 |
2.87e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 2.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720373277 255 LLDAGTY-VNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 306
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
293-342 |
2.87e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 2.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720373277 293 ADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKA 342
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
269-297 |
4.34e-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: 4.34e-03
10 20
....*....|....*....|....*....
gi 1720373277 269 GDTVLIGAVRGGHVEIVRALLQKYADIDI 297
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
269-298 |
5.27e-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: 5.27e-03
10 20 30
....*....|....*....|....*....|.
gi 1720373277 269 GDTVL-IGAVRGGHVEIVRALLQKYADIDIR 298
Cdd:pfam00023 2 GNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
17-71 |
7.23e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.39 E-value: 7.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720373277 17 NIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDN 71
Cdd:PLN03192 634 DLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
51-297 |
7.58e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 40.97 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 51 VEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELL---KCGANLEHRDMGGWTALMWACYKGRT---DVVELLL 124
Cdd:PHA02798 89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 125 SHGANPSVTGLYSVYP-----IIWAAGRGHADIVHLLLQNGAKVNCSDKYgttplvwaARKGHLECVKHLLAMGADVDQE 199
Cdd:PHA02798 169 EKGVDINTHNNKEKYDtlhcyFKYNIDRIDADILKLFVDNGFIINKENKS--------HKKKFMEYLNSLLYDNKRFKKN 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373277 200 GANSMTALIvavkggytqsvkeilkrnpNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRG 279
Cdd:PHA02798 241 ILDFIFSYI-------------------DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
|
250
....*....|....*...
gi 1720373277 280 GHVEIVRALLQKYADIDI 297
Cdd:PHA02798 302 ESKFIFNSILNKKPNKNT 319
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
70-98 |
7.75e-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: 7.75e-03
10 20
....*....|....*....|....*....
gi 1720373277 70 DNWTALISASKEGHIHIVEELLKCGANLE 98
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
140-165 |
7.82e-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: 7.82e-03
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
334-363 |
9.91e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.26 E-value: 9.91e-03
10 20 30
....*....|....*....|....*....|
gi 1720373277 334 DGETPLIKATKMRNIEVVELLLDKGARVSA 363
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| |
