|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
18-306 |
2.05e-63 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 218.28 E-value: 2.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 18 IPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELLKCGVNL 97
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 98 EHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWA 177
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 178 ARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLD 257
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1149123006 258 AGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 306
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
16-273 |
2.94e-60 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 209.04 E-value: 2.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 16 ENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELLKCGV 95
Cdd:COG0666 32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 96 NLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLV 175
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 176 WAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDL 255
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
250
....*....|....*...
gi 1149123006 256 LDAGTYVNIPDRSGDTVL 273
Cdd:COG0666 272 LLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
86-372 |
4.89e-59 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 205.57 E-value: 4.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 86 IVEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNC 165
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 166 SDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASK 245
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 246 EGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCN 325
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1149123006 326 PDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPL 372
Cdd:COG0666 243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
10-240 |
5.98e-58 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 202.49 E-value: 5.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 10 INYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEE 89
Cdd:COG0666 59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 90 LLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKY 169
Cdd:COG0666 139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123006 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 |
8.32e-58 |
|
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: 202.23 E-value: 8.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 440 YDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFagqqieplfqfswlivfltlllcgglgllfaft 519
Cdd:pfam07693 1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 520 vhpnlgiavslsflallyiffiviyfggrregeswnwawvlstrlarhigylelllklmfvnppelpeqttkalPVRFLF 599
Cdd:pfam07693 48 --------------------------------------------------------------------------NEEFII 53
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 600 TDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDTQGKKK--WKKTCCLPSFVIFLFIIGciisgitll 677
Cdd:pfam07693 54 VYFNPWSFSGQDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKigLIFGVAIILALTGLVVAI--------- 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 678 aifrvdpkhltvnavlisiasvvglafvlncrtwwqvldsllnsqrkrlhnaasklhklksEGFMKVLKCEV-ELMARMA 756
Cdd:pfam07693 125 -------------------------------------------------------------EEPMKKLQTEIeELRSDIE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 757 KTIDSftqNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLrdsNINGHDYMRN 836
Cdd:pfam07693 144 STLKD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPNVVFILAADEEILKKALEANYESGL---EIDGQKYLEK 217
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 837 IVHLPVFLNSRGLSNARKFLVTSAtngdvpcsdttgiqedadrrvsQNSLGEMTKLGSKTALnrrdtyrrrqmqrtitrq 916
Cdd:pfam07693 218 IIQVPFTLPPLSLRQLKKFLMLSF----------------------DNSEEGTSSKDRDETL------------------ 257
|
490 500 510
....*....|....*....|....*....|....*..
gi 1149123006 917 MSFDLTKLLVTEDwFSDISPQTMRRLLNIVSVTGRLL 953
Cdd:pfam07693 258 RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
140-393 |
5.40e-56 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 196.71 E-value: 5.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 140 PIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSV 219
Cdd:COG0666 24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 220 KEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRG 299
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 300 QDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGR 379
Cdd:COG0666 184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
|
250
....*....|....
gi 1149123006 380 SRKLAELLLRNPKD 393
Cdd:COG0666 264 AALIVKLLLLALLL 277
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
150-414 |
1.43e-53 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 189.78 E-value: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 150 ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 229
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 230 NLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWA 309
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 310 VEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLr 389
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL- 239
|
250 260
....*....|....*....|....*
gi 1149123006 390 npKDGRLLYRPNKAGETPYNIDCSH 414
Cdd:COG0666 240 --EAGADLNAKDKDGLTALLLAAAA 262
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
42-133 |
2.01e-27 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 107.51 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 42 LMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELLKCgVNLEHRDMgGWTALMWACYKGRTDVVE 121
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1149123006 122 LLLSHGANPSVT 133
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
49-377 |
1.17e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 115.06 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 49 GNLEIVKELIKNGANC-NLEDLDNWTALISASKEGHVHIVEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHG 127
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCiNISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 128 ANPSVTGLysvyPIIwaagrgHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmtal 207
Cdd:PHA02874 92 VDTSILPI----PCI------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 208 ivavkggytqsvkeilkrnpnVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRA 287
Cdd:PHA02874 150 ---------------------VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 288 LLQKYADIDIRGQDNKTALYWAVEKGNATMvrDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGAKVSAVDK 366
Cdd:PHA02874 209 LIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDN 286
|
330
....*....|.
gi 1149123006 367 KGDTPLHIAIR 377
Cdd:PHA02874 287 KGENPIDTAFK 297
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
2-399 |
2.54e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 113.62 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 2 SVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKE 81
Cdd:PHA02876 142 SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 82 GHVHIVEELLKCGVNLEHRDMGGWTALmwacykgRTDVVELLLshganpsvtglysvypiiwaagrghadivhLLLQNGA 161
Cdd:PHA02876 222 KNIDTIKAIIDNRSNINKNDLSLLKAI-------RNEDLETSL------------------------------LLYDAGF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 162 KVNCSDKYGTTPLVWAARKGHL-ECVKHLLAMGADVDQEGANSMTALIVAVKGGY-TQSVKEILKRNPNVNLTDKDGNTA 239
Cdd:PHA02876 265 SVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 240 LMIASK-EGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATM- 317
Cdd:PHA02876 345 LHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMs 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 318 VRDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSrkLAELLLR---NPKD 393
Cdd:PHA02876 425 VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHygaELRD 502
|
....*.
gi 1149123006 394 GRLLYR 399
Cdd:PHA02876 503 SRVLHK 508
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
43-329 |
1.02e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 110.11 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 43 MIAAEQGNLEIVKELIKNGANCNLEDLDNWTAL---ISASKEGHVHIVEELLKCGVNLEHRDMGGWTAL-MWACYKGRTD 118
Cdd:PHA03095 19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 119 VVELLLSHGANPSVTGLYSVYPI-IWAAG-RGHADIVHLLLQNGAKVNCSDKYGTTPL-VWAARKG-HLECVKHLLAMGA 194
Cdd:PHA03095 99 VIKLLIKAGADVNAKDKVGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNaNVELLRLLIDAGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 195 DVDQEGANSMTAL---IVAVKgGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTE--IVQDLLDAGTYVNIPDRSG 269
Cdd:PHA03095 179 DVYAVDDRFRSLLhhhLQSFK-PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYG 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 270 DTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTE 329
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
152-402 |
1.89e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 108.21 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 152 IVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQS-VKEI----LKRN 226
Cdd:PHA03100 17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdVKEIvkllLEYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 227 PNVNLTDKDGNTALMIAS--KEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHV--EIVRALLQKYADIDIrgqdn 302
Cdd:PHA03100 97 ANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 303 KTALYWAVEKGNATMVRDILqcnpdteictkdGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRK 382
Cdd:PHA03100 172 KNRVNYLLSYGVPINIKDVY------------GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
250 260
....*....|....*....|....*
gi 1149123006 383 LAELLLRN-----PKDGRLLYRPNK 402
Cdd:PHA03100 240 IFKLLLNNgpsikTIIETLLYFKDK 264
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
12-297 |
3.46e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 107.44 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 12 YVEEENIPALKALLEKCkDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVhiveelL 91
Cdd:PHA03100 10 SRIIKVKNIKYIIMEDD-LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYN------L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 92 KCGVNlehrdmggwtalmwacykgrtdVVELLLSHGANPSVTGLYSVYPIIWAAGR--GHADIVHLLLQNGAKVNCSDKY 169
Cdd:PHA03100 83 TDVKE----------------------IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 170 GTTPLVWAARKGH--LECVKHLLAMGADVDQegansmtalivavkggyTQSVKEILKRNPNVNLTDKDGNTALMIASKEG 247
Cdd:PHA03100 141 GENLLHLYLESNKidLKILKLLIDKGVDINA-----------------KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1149123006 248 HTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDI 297
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
40-278 |
1.27e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 106.20 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 40 TPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEEL-----------------------LKCGVN 96
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 97 LEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVW 176
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 177 AARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKggYTQSVKEILKRNPNVNLTDKDGNTALMIA-SKEGHTEIVQDL 255
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDIL 274
|
250 260
....*....|....*....|...
gi 1149123006 256 LDAGTYVNIPDRSGDTVLIGAVR 278
Cdd:PHA02874 275 LYHKADISIKDNKGENPIDTAFK 297
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
108-198 |
2.56e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.87 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 108 LMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNgAKVNCSDkYGTTPLVWAARKGHLECVK 187
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|.
gi 1149123006 188 HLLAMGADVDQ 198
Cdd:pfam12796 79 LLLEKGADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
174-266 |
4.51e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.10 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 174 LVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKrNPNVNLTDkDGNTALMIASKEGHTEIVQ 253
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1149123006 254 DLLDAGTYVNIPD 266
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
141-233 |
8.93e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.25 E-value: 8.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 141 IIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLA-MGADVDQEGansMTALIVAVKGGYTQSV 219
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNG---RTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1149123006 220 KEILKRNPNVNLTD 233
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
13-101 |
2.48e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.09 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNgANCNLEDlDNWTALISASKEGHVHIVEELLK 92
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 1149123006 93 CGVNLEHRD 101
Cdd:pfam12796 83 KGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
207-298 |
3.42e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.71 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 207 LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTyVNIPDrSGDTVLIGAVRGGHVEIVR 286
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1149123006 287 ALLQKYADIDIR 298
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
74-297 |
3.68e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 91.98 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 74 ALISASKEGHVHIVEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIV 153
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 154 HLLLQNGAKVN-CSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLT 232
Cdd:PHA02875 85 EELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123006 233 DKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGD-TVLIGAVRGGHVEIVRALLQKYADIDI 297
Cdd:PHA02875 165 DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
273-365 |
5.75e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.24 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 273 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRdILQCNPDTEICTkDGETPLIKATKMRNIEVVE 352
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1149123006 353 LLLDKGAKVSAVD 365
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
240-334 |
1.42e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.09 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 240 LMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLqKYADIDIRGqDNKTALYWAVEKGNATMVR 319
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|....*
gi 1149123006 320 DILQCNPDteICTKD 334
Cdd:pfam12796 79 LLLEKGAD--INVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
219-389 |
3.08e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 90.08 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 219 VKEILKRNPNVNLTDKDGNTAL---MIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVE-IVRALLQKYAD 294
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 295 IDIRGQDNKTAL--YWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGAKVSAVDKKGDT 370
Cdd:PHA03095 110 VNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRS 189
|
170 180
....*....|....*....|..
gi 1149123006 371 PLHI---AIRGRSRKLAELLLR 389
Cdd:PHA03095 190 LLHHhlqSFKPRARIVRELIRA 211
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
21-291 |
3.74e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 89.70 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 21 LKALLEKCKDVDERNECGQTPL---MIAAEQGNLEIVKELIKNGANCNLEDLDNWTALI----SASKEGhvhIVEELLKC 93
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlylyNATTLD---VIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 94 GVNLEHRDMGGWTALMwACYKG---RTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADI--VHLLLQNGAKVNCSDK 168
Cdd:PHA03095 107 GADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 169 YGTTPLvwaarKGHLE-------CVKHLLAMGADVDQEGANSMTALIVAVKGGYTQS--VKEILKRNPNVNLTDKDGNTA 239
Cdd:PHA03095 186 RFRSLL-----HHHLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTP 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1149123006 240 LMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQK 291
Cdd:PHA03095 261 LHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
181-398 |
3.86e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 88.89 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 181 GHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRN--PNVNLTDKDgnTALMIASKEGHTEIVQDLLDA 258
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGaiPDVKYPDIE--SELHDAVEEGDVKAVEELLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 259 GTYVN-IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGET 337
Cdd:PHA02875 91 GKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123006 338 PLIKATKMRNIEVVELLLDKGAKVSAVDKKGD-TPLHIAIRGRSRKLAELLLRNPKDGRLLY 398
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
18-306 |
6.84e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 88.93 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 18 IPALKALLEKCKDVDERNECGQTPLMI--AAEQGNLEIVKELIKNGANCNLEDLDNWT---ALISaSKEGHVHIVEELLK 92
Cdd:PHA03095 97 LDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLK-SRNANVELLRLLID 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 93 CGVNLEHRDMGGWTALMWAC--YKGRTDVVELLLSHGANPSVTGLYSVYPIIWAA--GRGHADIVHLLLQNGAKVNCSDK 168
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 169 YGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKdgntALMIASKEGH 248
Cdd:PHA03095 256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGG 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123006 249 TEIVQDLLDAGTYVNIpdRSGDTVLIGAVRGGHVEIVRALLQKYADI-DIRGQDNKTAL 306
Cdd:PHA03095 332 DIPSDATRLCVAKVVL--RGAFSLLPEPIRAYHADFIRECEAEIAVMrTTRIGTGVSLL 388
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1-197 |
1.94e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 87.03 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 1 MSVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQ--GNLEIVKELIKNGANCNLEDLDNWTALISA 78
Cdd:PHA03100 69 STPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 79 SKEGHV--HIVEELLKCGVNLEhrdmggwtalmwacykgRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLL 156
Cdd:PHA03100 149 LESNKIdlKILKLLIDKGVDIN-----------------AKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1149123006 157 LQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVD 197
Cdd:PHA03100 212 LDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
150-375 |
9.10e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.46 E-value: 9.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 150 ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEIL-KR 225
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 226 NPNVNLTDKDGNTALMI--ASKEGHTEIVQDLLDAGTYVNIPDRSGDT---VLIGAvRGGHVEIVRALLQKYADI---DI 297
Cdd:PHA03095 107 GADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKS-RNANVELLRLLIDAGADVyavDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 298 RGQdnkTALYWAVE--KGNATMVRDILQCNPDTEICTKDGETPLIKA---TKMRNIeVVELLLDKGAKVSAVDKKGDTPL 372
Cdd:PHA03095 186 RFR---SLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRS-LVLPLLIAGISINARNRYGQTPL 261
|
...
gi 1149123006 373 HIA 375
Cdd:PHA03095 262 HYA 264
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
203-435 |
1.22e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 84.63 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 203 SMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAG---TYVNIPDRSGDTVligavrg 279
Cdd:PHA02874 35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtSILPIPCIEKDMI------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 280 ghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGA 359
Cdd:PHA02874 108 ------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123006 360 KVSAVDKKGDTPLHIAIRGRSRKLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSILTQIFGARHLSPTETDG 435
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDH---GNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDG 254
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
306-393 |
1.26e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.69 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 306 LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAkvSAVDKKGDTPLHIAIRGRSRKLAE 385
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
....*...
gi 1149123006 386 LLLRNPKD 393
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
13-246 |
3.64e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 83.39 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANC---------------------------- 64
Cdd:PHA02878 45 VEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCsvfytlvaikdafnnrnveifkiiltnr 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 65 --NLEDLDN-WTALISASKEGHVHIVEELLKCG--VNLEHRDMGGwTALMWACYKGRTDVVELLLSHGANPSVTGLYSVY 139
Cdd:PHA02878 125 ykNIQTIDLvYIDKKSKDDIIEAEITKLLLSYGadINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 140 PIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWA-ARKGHLECVKHLLAMGADVD-QEGANSMTALIVAVKGgyTQ 217
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNaKSYILGLTALHSSIKS--ER 281
|
250 260
....*....|....*....|....*....
gi 1149123006 218 SVKEILKRNPNVNLTDKDGNTALMIASKE 246
Cdd:PHA02878 282 KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
31-256 |
3.69e-14 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 77.75 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 31 VDERNECGQ-----TPLMIAAEQGNLEIVKELIKNgancnlEDLDNW-------TALISASKEGHVHIVEELLKCGVNLE 98
Cdd:cd22192 5 LDELHLLQQkriseSPLLLAAKENDVQAIKKLLKC------PSCDLFqrgalgeTALHVAALYDNLEAAVVLMEAAPELV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 99 HRDMG-----GWTALMWACYKGRTDVVELLLSHGA---NPSVTGLYSV-----------YPIIWAAGRGHADIVHLLLQN 159
Cdd:cd22192 79 NEPMTsdlyqGETALHIAVVNQNLNLVRELIARGAdvvSPRATGTFFRpgpknliyygeHPLSFAACVGNEEIVRLLIEH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 160 GAKVNCSDKYGTTPLvwaarkghlecvkHLLAMGAdvDQEGANSMTALIVA-VKGGYTQSVKEIlkrnPNvnltdKDGNT 238
Cdd:cd22192 159 GADIRAQDSLGNTVL-------------HILVLQP--NKTFACQMYDLILSyDKEDDLQPLDLV----PN-----NQGLT 214
|
250
....*....|....*...
gi 1149123006 239 ALMIASKEGHTEIVQDLL 256
Cdd:cd22192 215 PFKLAAKEGNIVMFQHLV 232
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
219-418 |
5.08e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 73.38 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 219 VKEILKRNPNVNLTDKDGNTAL--------MIASKEGHTEIVQDLLdAGTYVNIPDrsgdtvligAVRGGHVEIVRALLQ 290
Cdd:PHA02878 53 VKSLLTRGHNVNQPDHRDLTPLhiickepnKLGMKEMIRSINKCSV-FYTLVAIKD---------AFNNRNVEIFKIILT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 291 KYA----DIDIRGQDNKTAlywaVEKGNATMVRDILQCNPDTEICTKD-GETPLIKATKMRNIEVVELLLDKGAKVSAVD 365
Cdd:PHA02878 123 NRYkniqTIDLVYIDKKSK----DDIIEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1149123006 366 KKGDTPLHIAIRGRSRKLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSI 418
Cdd:PHA02878 199 KTNNSPLHHAVKHYNKPIVHILLEN---GASTDARDKCGNTPLHISVGYCKDY 248
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
41-351 |
8.06e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.99 E-value: 8.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 41 PLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTAL----ISASKEGHVHIVEELLKCGVNLEHRdmggwtALMWACYKGR 116
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLhiicKEPNKLGMKEMIRSINKCSVFYTLV------AIKDAFNNRN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 117 TDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKY-GTTPLVWAARKGHLECVKHLLAMGAD 195
Cdd:PHA02878 114 VEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 196 VDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKE-GHTEIVQDLLDAGTYVNIPDR-SGDTVL 273
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 274 IGAVRGGHVeiVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNpdteICTKDGETPLIKATK--MRNIEVV 351
Cdd:PHA02878 274 HSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN----ICLLKRIKPDIKNSEgfIDNMDCI 347
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
431-987 |
1.22e-12 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 71.87 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 431 TETDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGqqieplfqfswlivfltlllcg 510
Cdd:COG4928 1 NETEEDLLGRKKYAESLANLIKSSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 511 glgllfaftvhpnlgiavslsflallyifFIVIYFggrregeswnwawvlstrlarhigylelllklmfvNPpelpeqtt 590
Cdd:COG4928 59 -----------------------------VIVVYF-----------------------------------NA-------- 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 591 kalpvrFLFTDYNRLssvggetsLAEMIATLSDACEREfgflatrlfrvfKTEDTQGKKKWKKtcclpsfviflfiigcI 670
Cdd:COG4928 67 ------WLYDGEEDL--------LAALLSEIAAELEKK------------KKKDKKAAKKLKK----------------Y 104
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 671 ISGITLLAIfrvdpkhltvnavlisIASVVGLafvlncrtWWQVLDSLLNSQRKRLHNAASK-LHKLKSEgFMKVLKcev 749
Cdd:COG4928 105 AKRLSKLAL----------------KAGLLGG--------PAEAVAEALKALLKKEYKSKKKsIEAFREE-LEELLK--- 156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 750 ELMARmaktidsftqnqtRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNsvlrdSNIN 829
Cdd:COG4928 157 ELKGK-------------RLVVFIDDLDRCEPDEAIEVLELIKLFFDFPNVVFVLAFDREILEHALKERYG-----EDID 218
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 830 GHDYMRNIVHLPVFLNSRGLSNARKFLVTSATNGDVPcsdttGIQEDADRRVSQNSLGEMTKLGSKTALNRRDTYRRRQM 909
Cdd:COG4928 219 AREYLEKIIQVPFRLPPLSNELLILELDRLLELLLSA-----LLEALLALLLLRALAESISSLRAEFLLLLLLLKLELLL 293
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123006 910 QRTITRQMSFDLTKLLVTEDW-FSDISPQTMRRLLNIVSVTGRLLRANQISFNWDRLASWINLTEQWPYRTSWLILYLE 987
Cdd:COG4928 294 ALLVLLLKLELLLENLLLAALlLLLDELELKKLLREDVASRASLYFINAELANLSLKLLKISSELLTLELKLEEERELS 372
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
151-319 |
1.26e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 72.98 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 151 DIVHLLLQNGAKVNcsDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN 230
Cdd:PLN03192 508 NVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 231 LTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNiPDRSGDtVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAV 310
Cdd:PLN03192 586 IRDANGNTALWNAISAKHHKIFRILYHFASISD-PHAAGD-LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
|
....*....
gi 1149123006 311 EKGNATMVR 319
Cdd:PLN03192 664 AEDHVDMVR 672
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
13-229 |
1.30e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.95 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 13 VEEENIPALKALLEKCKDVDER-NECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELL 91
Cdd:PHA02875 76 VEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 92 KCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLY-SVYPIIWAAGRGHADIVHLLLQNGAKVN----CS 166
Cdd:PHA02875 156 DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNimfmIE 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123006 167 DKYGTTplvwaarkghLECVKHllaMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 229
Cdd:PHA02875 236 GEECTI----------LDMICN---MCTNLESEAIDALIADIAIRIHKKTIRRDEGFKNNMST 285
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
203-410 |
8.82e-12 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 70.04 E-value: 8.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 203 SMTALIVAVKGGYTQSVKEILKrNPNVNLTDKD--GNTALMIASKEGHTEIVQDLLDAG-TYVNIPDRS----GDTVLIG 275
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLK-CPSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApELVNEPMTSdlyqGETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 276 AVRGGHVEIVRALLQKYADID---------IRGQDNKtaLYWavekgnatmvrdilqcnpdteictkdGETPLIKATKMR 346
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVspratgtffRPGPKNL--IYY--------------------------GEHPLSFAACVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123006 347 NIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLA----ELLLRNPKDGRL--LYR-PNKAGETPYNI 410
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpLDLvPNNQGLTPFKL 218
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
172-357 |
2.80e-11 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 68.50 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 172 TPLVWAARKGHLECVKHLLAM-GADVDQEGANSMTALIVAVKGGYTQSVKEILKRNP---NVNLTDK--DGNTALMIASK 245
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvNEPMTSDlyQGETALHIAVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 246 EGHTEIVQDLLDAGTYVNIPdRS---------------GDTVLIGAVRGGHVEIVRALLQKYADIdiRGQDN--KTALYW 308
Cdd:cd22192 99 NQNLNLVRELIARGADVVSP-RAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADI--RAQDSlgNTVLHI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123006 309 AVEKGNAT----MVRDILQCNP-DTEIC-----TKDGETPLIKATKMRNIEVVELLLDK 357
Cdd:cd22192 176 LVLQPNKTfacqMYDLILSYDKeDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
3-169 |
3.27e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 68.36 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 3 VLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEG 82
Cdd:PLN03192 523 PNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 83 HVHIVEELLKCGvNLEHRDMGGwTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAK 162
Cdd:PLN03192 603 HHKIFRILYHFA-SISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
|
....*..
gi 1149123006 163 VNCSDKY 169
Cdd:PLN03192 681 VDKANTD 687
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
98-262 |
4.01e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 68.36 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 98 EHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWA 177
Cdd:PLN03192 519 EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 178 ARKGHLECVKHLLAMGADVDQEGANSMtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLD 257
Cdd:PLN03192 599 ISAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
|
....*
gi 1149123006 258 AGTYV 262
Cdd:PLN03192 677 NGADV 681
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
141-302 |
4.71e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.97 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 141 IIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYtQSVK 220
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH-HKIF 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 221 EILKR-----NPNVnltdkdGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADI 295
Cdd:PLN03192 608 RILYHfasisDPHA------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
....*..
gi 1149123006 296 DIRGQDN 302
Cdd:PLN03192 682 DKANTDD 688
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
117-357 |
7.02e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 66.78 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 117 TDVVELLLSHGANpsVTGLYSVYPIIWAA------GRGHA-DIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECV 186
Cdd:PHA02798 51 TDIVKLFINLGAN--VNGLDNEYSTPLCTilsnikDYKHMlDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 187 KHLLAMGADVDQEGANSMTALIVAVKGGYT---QSVKEILKRNPNVNL-TDKDGNTALMIASKEGHTEIVQDLL----DA 258
Cdd:PHA02798 129 LFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNIDRIDADILklfvDN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 259 GTYVNIPDRSGDTVLIGAV-------RGGHVEIVRALLqKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEIC 331
Cdd:PHA02798 209 GFIINKENKSHKKKFMEYLnsllydnKRFKKNILDFIF-SYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINII 287
|
250 260
....*....|....*....|....*.
gi 1149123006 332 TKDGETPLIKATKMRNIEVVELLLDK 357
Cdd:PHA02798 288 TELGNTCLFTAFENESKFIFNSILNK 313
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
193-365 |
8.31e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.20 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 193 GADVDQEGANSmtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTV 272
Cdd:PLN03192 518 GEHDDPNMASN---LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 273 LIGAVRGGHVEIVRALLQkYADIdirgQDNKTA---LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIE 349
Cdd:PLN03192 595 LWNAISAKHHKIFRILYH-FASI----SDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669
|
170
....*....|....*.
gi 1149123006 350 VVELLLDKGAKVSAVD 365
Cdd:PLN03192 670 MVRLLIMNGADVDKAN 685
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
140-190 |
1.54e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.05 E-value: 1.54e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1149123006 140 PIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLL 190
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
9-256 |
2.44e-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: 65.49 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 9 VINYVEEENIPALKALLEKCK--DVDERNECGQTPLMIAAEQGNLEIVKELIKNgANCNLEDLDnwtALISASKEGHVHI 86
Cdd:TIGR00870 21 FLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLN-LSCRGAVGD---TLLHAISLEYVDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 87 VEELL-------KCGVNLEH---RDMG----GWTALMWACYKGRTDVVELLLSHGAN-------------PSVTGLY-SV 138
Cdd:TIGR00870 97 VEAILlhllaafRKSGPLELandQYTSeftpGITALHLAAHRQNYEIVKLLLERGASvparacgdffvksQGVDSFYhGE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 139 YPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTplvwaarkghlecVKHLLAMGADVDQEG---ANSMTALIVAVKGG- 214
Cdd:TIGR00870 177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNT-------------LLHLLVMENEFKAEYeelSCQMYNFALSLLDKl 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1149123006 215 -YTQSVKEILKRnpnvnltdkDGNTALMIASKEGHTEIVQDLL 256
Cdd:TIGR00870 244 rDSKELEVILNH---------QGLTPLKLAAKEGRIVLFRLKL 277
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
40-91 |
7.24e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 7.24e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1149123006 40 TPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELL 91
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
24-78 |
2.64e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 54.66 E-value: 2.64e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123006 24 LLEKC-KDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISA 78
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
104-157 |
3.75e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 3.75e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1149123006 104 GWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLL 157
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
71-124 |
1.10e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 1.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1149123006 71 NWTALISASKEGHVHIVEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLL 124
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
282-390 |
2.03e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 58.88 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 282 VEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATmVRDILQC------NPDT-EICtkdGETPLIkaTKMRN---IEVV 351
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEK-VKDIVRLlleagaDVNApERC---GFTPLH--LYLYNattLDVI 100
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1149123006 352 ELLLDKGAKVSAVDKKGDTPLHIAIRGRS--RKLAELLLRN 390
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRK 141
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
313-389 |
2.22e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.14 E-value: 2.22e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123006 313 GNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLR 389
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
87-282 |
3.22e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 58.14 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 87 VEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADI--VHLLLQNGAKVN 164
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 165 CS-DKYGTTPLVwAARKGHLECVKHLLAMGAD---VDQEGANSMTALIVAvKGGYTQSVKEILKRNPNVNLTDKDGNTAL 240
Cdd:PHA02946 135 NSvDEEGCGPLL-ACTDPSERVFKKIMSIGFEariVDKFGKNHIHRHLMS-DNPKASTISWMMKLGISPSKPDHDGNTPL 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1149123006 241 -MIASKEGHTEIVQDLLDAGTYVNIPDRSGD---TVLIGAVRGGHV 282
Cdd:PHA02946 213 hIVCSKTVKNVDIINLLLPSTDVNKQNKFGDsplTLLIKTLSPAHL 258
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
236-289 |
3.26e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 3.26e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1149123006 236 GNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALL 289
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
13-58 |
3.56e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 3.56e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1149123006 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELI 58
Cdd:pfam13637 9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
337-388 |
6.41e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 6.41e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1149123006 337 TPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLL 388
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
39-195 |
6.93e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.92 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 39 QTPLMIAAEQGNLEIVKELIKNGANCNleDL---DNWTALISASKEGHVHIVEELLKCGVNLEHRDMGGWTALMWACYKG 115
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 116 RTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYG-TTPLVWAARKGHLECVKHLLAMGA 194
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGA 226
|
.
gi 1149123006 195 D 195
Cdd:PHA02875 227 D 227
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
204-256 |
9.31e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 9.31e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1149123006 204 MTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLL 256
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
156-210 |
2.53e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 2.53e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123006 156 LLQNG-AKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVA 210
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
170-220 |
3.85e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 3.85e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1149123006 170 GTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVK 220
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
51-327 |
9.50e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.69 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 51 LEIVKELIKNGANCNLEDLDNWTALISaskeghvhIVEELLKcgvnlehrdmggwtalmwacYKGRTDVVELLLSHGANP 130
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCT--------ILSNIKD--------------------YKHMLDIVKILIENGADI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 131 SVTGLYSVYPIIWAAGRGH---ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECVKHLLAMGADVDQ----EG 200
Cdd:PHA02798 103 NKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThnnkEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 201 ANSMTALIvavKGGYTQSVKEILKRNPN----VNLTDKDGNTALM-------IASKEGHTEIVQDLLdagTYVNIPDRS- 268
Cdd:PHA02798 183 YDTLHCYF---KYNIDRIDADILKLFVDngfiINKENKSHKKKFMeylnsllYDNKRFKKNILDFIF---SYIDINQVDe 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 269 -GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPD 327
Cdd:PHA02798 257 lGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
38-66 |
9.72e-07 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 46.43 E-value: 9.72e-07
10 20
....*....|....*....|....*....
gi 1149123006 38 GQTPLMIAAEQGNLEIVKELIKNGANCNL 66
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
145-256 |
1.08e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 145 AGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmtalivavkggytqsvkeilk 224
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD----------------------------- 140
|
90 100 110
....*....|....*....|....*....|..
gi 1149123006 225 rnpnVNLTDKDGNTALMIASKEGHTEIVQDLL 256
Cdd:PTZ00322 141 ----PTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
52-290 |
1.36e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 53.21 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 52 EIVKELIKNGANCNLED---------LDNWTalISASKegHVHIVEELLKCGVNLEHRDMGGWTALMWACYK---GRTDV 119
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGyietplcavLRNRE--ITSNK--IKKIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 120 VELLLSHGAN-PSVTGL--YSVYPIIWAAGRGHADIVHLLLQNGakVNCSDK---YGTTPLVWAARKG----HLECVKHL 189
Cdd:PHA02989 127 LRFLLSKGINvNDVKNSrgYNLLHMYLESFSVKKDVIKILLSFG--VNLFEKtslYGLTPMNIYLRNDidviSIKVIKYL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 190 LAMGADVDQEGANSMTALIVAVKGGYTQSVKE------ILKRnPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVN 263
Cdd:PHA02989 205 IKKGVNIETNNNGSESVLESFLDNNKILSKKEfkvlnfILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIY 283
|
250 260
....*....|....*....|....*..
gi 1149123006 264 IPDRSGDTVLIGAVRGGHVEIVRALLQ 290
Cdd:PHA02989 284 NVSKDGDTVLTYAIKHGNIDMLNRILQ 310
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
38-68 |
1.40e-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: 1.40e-06
10 20 30
....*....|....*....|....*....|..
gi 1149123006 38 GQTPLMIAAEQ-GNLEIVKELIKNGANCNLED 68
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
225-276 |
1.73e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.57 E-value: 1.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1149123006 225 RNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGA 276
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
177-422 |
1.91e-06 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 52.78 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 177 AARKGHLECVKHLLAMGADVDQEGANSM--TALIVAVKGGYTQSVKEILKRNPNVNLTdkdGNTALMIASKEGHtEIVQD 254
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPKKLNINCPDRLgrSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISLEYV-DAVEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 255 LL--------DAGTYVNIPDRSGD------TVLIGAVRGGHVEIVRALLQKYADIDIRGqdnktalywaveKGNATMVRD 320
Cdd:TIGR00870 100 ILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARA------------CGDFFVKSQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 321 ILQcnpdteiCTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAI-----RGRSRKLA----ELLLR-- 389
Cdd:TIGR00870 168 GVD-------SFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefKAEYEELScqmyNFALSll 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1149123006 390 -NPKDGRLLYR-PNKAGETPYNIDCSHQKSILTQI 422
Cdd:TIGR00870 241 dKLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRL 275
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
5-230 |
2.49e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 52.14 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 5 ISQSVINYVEEENIpaLKALLEKCKDVDERNECGQTPLMIAAEQG---NLEIVKELIKNGANCNLEDLDNWTALISASKE 81
Cdd:PHA02798 78 ILSNIKDYKHMLDI--VKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 82 GH---VHIVEELLKCGVNL-EHRDMGGWTALmwACY------KGRTDVVELLLSHG-----ANPSV--TGLYSVYPIIWA 144
Cdd:PHA02798 156 NHhidIEIIKLLLEKGVDInTHNNKEKYDTL--HCYfkynidRIDADILKLFVDNGfiinkENKSHkkKFMEYLNSLLYD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 145 AGRGHADIVHLLLQNgAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILK 224
Cdd:PHA02798 234 NKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILN 312
|
....*.
gi 1149123006 225 RNPNVN 230
Cdd:PHA02798 313 KKPNKN 318
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
37-65 |
2.92e-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: 2.92e-06
10 20
....*....|....*....|....*....
gi 1149123006 37 CGQTPLMIAAEQGNLEIVKELIKNGANCN 65
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
12-173 |
2.97e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 49.82 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 12 YVEEENIPALKALLekcKDVDERNECGQTPLMIAAEQ--GNLEIVKELIKNGANCNLEDLD-NWTAL---ISASKEGHVH 85
Cdd:PHA02859 28 YVEKDDIEGVKKWI---KFVNDCNDLYETPIFSCLEKdkVNVEILKFLIENGADVNFKTRDnNLSALhhyLSFNKNVEPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 86 IVEELLKCGVNLEHRDMGGWTAL-MWAC-YKGRTDVVELLLSHGANP------SVTGLYSVYPIiwaagRGHADIVHLLL 157
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLhMYMCnFNVRINVIKLLIDSGVSFlnkdfdNNNILYSYILF-----HSDKKIFDFLT 179
|
170
....*....|....*.
gi 1149123006 158 QNGAKVNCSDKYGTTP 173
Cdd:PHA02859 180 SLGIDINETNKSGYNC 195
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-133 |
5.41e-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: 5.41e-06
10 20 30
....*....|....*....|....*....|.
gi 1149123006 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 |
6.90e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 44.12 E-value: 6.90e-06
10 20
....*....|....*....|....*....
gi 1149123006 104 GWTALMWACYKGRTDVVELLLSHGANPSV 132
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
235-267 |
1.21e-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: 1.21e-05
10 20 30
....*....|....*....|....*....|....
gi 1149123006 235 DGNTALMIAS-KEGHTEIVQDLLDAGTYVNIPDR 267
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
52-234 |
1.33e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 49.74 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 52 EIVKELIKNGANCNLEDLDNWTAL---ISASKEGHVHIVEELLKCGVNL-EHRDMGGWTAL-MW-ACYKGRTDVVELLLS 125
Cdd:PHA02989 89 KIVKLLLKFGADINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVnDVKNSRGYNLLhMYlESFSVKKDVIKILLS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 126 HGANP-SVTGLYSVYPI-IWAagRGHADIVHL-----LLQNGA------------------------------------- 161
Cdd:PHA02989 169 FGVNLfEKTSLYGLTPMnIYL--RNDIDVISIkvikyLIKKGVnietnnngsesvlesfldnnkilskkefkvlnfilky 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123006 162 -KVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDK 234
Cdd:PHA02989 247 iKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLKPGKYLIKK 320
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
123-174 |
1.35e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 1.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1149123006 123 LLSHG-ANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPL 174
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
210-410 |
2.12e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 48.90 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 210 AVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVL--IGAVRGGHVEIVRA 287
Cdd:PHA02946 46 GIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 288 LLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGAKVSAVD 365
Cdd:PHA02946 126 LVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1149123006 366 KKGDTPLHIAIRGRSRKLAELLLRNPKDGrlLYRPNKAGETPYNI 410
Cdd:PHA02946 206 HDGNTPLHIVCSKTVKNVDIINLLLPSTD--VNKQNKFGDSPLTL 248
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
348-412 |
2.65e-05 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 46.02 E-value: 2.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123006 348 IEVVELLLDKGAKVSAVDKK-GDTPLHIAIRGRSRKLAELLLRNPKDGRLLYrpNKAGETPYNIDC 412
Cdd:PHA02736 71 QEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEIL--NYAFKTPYYVAC 134
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
169-197 |
3.45e-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: 3.45e-05
10 20
....*....|....*....|....*....
gi 1149123006 169 YGTTPLVWAARKGHLECVKHLLAMGADVD 197
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
54-126 |
4.52e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 4.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123006 54 VKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSH 126
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-132 |
6.03e-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: 6.03e-05
10 20
....*....|....*....|....*....
gi 1149123006 104 GWTALMWACYKGRTDVVELLLSHGANPSV 132
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
169-198 |
6.23e-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: 6.23e-05
10 20 30
....*....|....*....|....*....|.
gi 1149123006 169 YGTTPLVWAA-RKGHLECVKHLLAMGADVDQ 198
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
304-355 |
6.41e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 6.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1149123006 304 TALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLL 355
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
90-133 |
6.75e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 6.75e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1149123006 90 LLKCG-VNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVT 133
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK 45
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
283-450 |
9.59e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 47.45 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 283 EIVRALLQ--------------KYADIDIRGQdnkTALYWAVEKGNATMVRDILQCNPDTEICTKD-------------- 334
Cdd:cd22194 111 EIVRILLAfaeengildrfinaEYTEEAYEGQ---TALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyf 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 335 GETPLIKATKMRNIEVVELLLDKGAK-VSAVDKKGDTPLH----IAIRGRSR-----KLAELLLRNPKDGRLLYRPNKAG 404
Cdd:cd22194 188 GETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHalvtVAEDSKTQndfvkRMYDMILLKSENKNLETIRNNEG 267
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1149123006 405 ETPYNIDCSHQK-SILTQIFG-------ARHLSPTETDgdmLGYDLYSSALADI 450
Cdd:cd22194 268 LTPLQLAAKMGKaEILKYILSreikekpNRSLSRKFTD---WAYGPVSSSLYDL 318
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
151-256 |
1.06e-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: 47.06 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 151 DIVHLLLQNGAKVNCSDK--------------YGTTPLVWAARKGHLECVKHLLAMGADV----DQEGANSMTALIVAVK 212
Cdd:cd22194 155 DIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKESTDitsqDSRGNTVLHALVTVAE 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1149123006 213 GGYTQ--SVKE----ILKRNPNVNL---TDKDGNTALMIASKEGHTEIVQDLL 256
Cdd:cd22194 235 DSKTQndFVKRmydmILLKSENKNLetiRNNEGLTPLQLAAKMGKAEILKYIL 287
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
117-208 |
1.41e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 45.74 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 117 TDVVELLLSHGANPSVTGLYS----VYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGT-TPLVWAARKGHLECVKHLLA 191
Cdd:PHA02884 46 TDIIDAILKLGADPEAPFPLSenskTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLS 125
|
90
....*....|....*..
gi 1149123006 192 MGADVDQEgANSMTALI 208
Cdd:PHA02884 126 YGADINIQ-TNDMVTPI 141
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
269-319 |
1.54e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 1.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1149123006 269 GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVR 319
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
60-256 |
1.57e-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: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 60 NGANC------NLEDLDNWTALI---SASKEGHvhiveelLKCGVNLEHRD--MGGWTALMWACYKGRTDVVELLLSHGA 128
Cdd:cd22196 46 TGKTCllkamlNLHNGQNDTISLlldIAEKTGN-------LKEFVNAAYTDsyYKGQTALHIAIERRNMHLVELLVQNGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 129 -------------NPSVTGLY-SVYPIIWAAGRGHADIVHLLLQN---GAKVNCSDKYGTTplvwaarkghlecVKHLLA 191
Cdd:cd22196 119 dvharasgeffkkKKGGPGFYfGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNT-------------VLHALV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123006 192 MGADVDQEGANSMTALivavkggYTQSVKEILKRNPNVNL---TDKDGNTALMIASKEGHTEIVQDLL 256
Cdd:cd22196 186 EVADNTPENTKFVTKM-------YNEILILGAKIRPLLKLeeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
273-393 |
1.61e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.14 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 273 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVE 352
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1149123006 353 LLLDKGAKVSAV-DKKGDTPLHIAIRGRSRKLAELLLRNPKD 393
Cdd:PHA02875 86 ELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
302-436 |
1.67e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.14 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 302 NKTALYWAVEKGNATMVRDILQC--NPDTEIctKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAI-RG 378
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIgiNPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVeEG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123006 379 RSRKLAELLLRNPKDGRLLYrpnKAGETPYNIDCSHQKSILTQIFGARHLSPTETDGD 436
Cdd:PHA02875 80 DVKAVEELLDLGKFADDVFY---KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
268-355 |
2.41e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 268 SGDTVliGAvrgghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN 347
Cdd:PTZ00322 92 SGDAV--GA---------RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
....*...
gi 1149123006 348 IEVVELLL 355
Cdd:PTZ00322 161 REVVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
188-289 |
2.63e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.66 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 188 HLLAMGADVDQEGANSMTA-LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPD 266
Cdd:PTZ00322 66 HNLTTEEVIDPVVAHMLTVeLCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
|
90 100
....*....|....*....|...
gi 1149123006 267 RSGDTVLIGAVRGGHVEIVRALL 289
Cdd:PTZ00322 146 KDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
57-108 |
3.25e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 3.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1149123006 57 LIKNG-ANCNLEDLDNWTALISASKEGHVHIVEELLKCGVNLEHRDMGGWTAL 108
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
30-256 |
3.44e-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: 45.26 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 30 DVDERNECGQTPLMIAA---EQGNLEIVKELIKNGancnlEDLDNWTALISASkeghvhIVEELLKcgvnlehrdmgGWT 106
Cdd:cd21882 18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAA-----PDSGNPKELVNAP------CTDEFYQ-----------GQT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 107 ALMWACYKGRTDVVELLLSHGANPSV------------TGLY-SVYPIIWAAGRGHADIVHLLLQNGAK---VNCSDKYG 170
Cdd:cd21882 76 ALHIAIENRNLNLVRLLVENGADVSAratgrffrkspgNLFYfGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 171 TTplvwaarkghlecVKHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrnpnvnlTDKDGNTALMIASK 245
Cdd:cd21882 156 NT-------------VLHALVLQADNTPENSAFVCQmynllLSYGAHLDPTQQLEEI---------PNHQGLTPLKLAAV 213
|
250
....*....|.
gi 1149123006 246 EGHTEIVQDLL 256
Cdd:cd21882 214 EGKIVMFQHIL 224
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
334-366 |
3.72e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.58 E-value: 3.72e-04
10 20 30
....*....|....*....|....*....|....
gi 1149123006 334 DGETPLIKA-TKMRNIEVVELLLDKGAKVSAVDK 366
Cdd:pfam00023 1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
190-393 |
3.75e-04 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 45.46 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 190 LAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNP--NVNLTDKDGNTALMIASKEGHTEIVQDLLdagTYVNIPDR 267
Cdd:TIGR00870 4 LDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELL---LNLSCRGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 268 SGDTvLIGAVRGGHVEIVRALLQKYADIDiRGQDNktaLYWAVEKGNATMVRDIlqcnpdteictkdgeTPLIKATKMRN 347
Cdd:TIGR00870 81 VGDT-LLHAISLEYVDAVEAILLHLLAAF-RKSGP---LELANDQYTSEFTPGI---------------TALHLAAHRQN 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 348 IEVVELLLDKGAKVSA-------VDKKGDT-------PLHIAIRGRSRKLAELLLRNPKD 393
Cdd:TIGR00870 141 YEIVKLLLERGASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPAD 200
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
321-375 |
3.85e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 3.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123006 321 ILQCNP-DTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIA 375
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
338-423 |
4.05e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 44.87 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 338 PLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLRNPKDGRLLYRPNKAGETPYNIDCSHQKS 417
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
|
....*.
gi 1149123006 418 ILTQIF 423
Cdd:PHA02878 120 ILTNRY 125
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
120-203 |
4.52e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 120 VELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQE 199
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
|
....
gi 1149123006 200 GANS 203
Cdd:PTZ00322 178 GANA 181
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
140-168 |
5.20e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.81 E-value: 5.20e-04
10 20 30
....*....|....*....|....*....|
gi 1149123006 140 PIIWAAGR-GHADIVHLLLQNGAKVNCSDK 168
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
91-256 |
6.49e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 44.40 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 91 LKCGVNLEHRDMG--GWTALMWACYKGRTDVVELLLSHGA-----------NPSVTGLYSVY---PIIWAAGRGHADIVH 154
Cdd:cd22193 61 LKRFINAEYTDEYyeGQTALHIAIERRQGDIVALLVENGAdvhahakgrffQPKYQGEGFYFgelPLSLAACTNQPDIVQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 155 LLLQNG---AKVNCSDKYGTTPLvwaarkghlecvkHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrn 226
Cdd:cd22193 141 YLLENEhqpADIEAQDSRGNTVL-------------HALVTVADNTKENTKFVTRmydmiLIRGAKLCPTVELEEI---- 203
|
170 180 190
....*....|....*....|....*....|
gi 1149123006 227 pnvnlTDKDGNTALMIASKEGHTEIVQDLL 256
Cdd:cd22193 204 -----RNNDGLTPLQLAAKMGKIEILKYIL 228
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
22-103 |
9.16e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 22 KALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELLKCGVnlEHRD 101
Cdd:PTZ00322 99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ--CHFE 176
|
..
gi 1149123006 102 MG 103
Cdd:PTZ00322 177 LG 178
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
172-197 |
1.70e-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: 1.70e-03
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
90-157 |
2.00e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.96 E-value: 2.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123006 90 LLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLL 157
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
70-101 |
2.32e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.27 E-value: 2.32e-03
10 20 30
....*....|....*....|....*....|...
gi 1149123006 70 DNWTAL-ISASKEGHVHIVEELLKCGVNLEHRD 101
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
235-264 |
2.49e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|
gi 1149123006 235 DGNTALMIASKEGHTEIVQDLLDAGTYVNI 264
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
32-190 |
2.79e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 42.53 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 32 DERNECGQTPLMIAAEQGNleiVKELIKngANCNLEDLDNWTALISASKEGHVHIVEELLKCGVNLEHRDMG-------- 103
Cdd:cd22197 60 DGVNACIMPLLEIDKDSGN---PKPLVN--AQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 104 -----GWTALMWACYKGRTDVVELLLSHGANPSV---------TGLYSVYPIIWAAGRGHADIVHL---LLQNGAKVNCS 166
Cdd:cd22197 135 tcfyfGELPLSLAACTKQWDVVNYLLENPHQPASlqaqdslgnTVLHALVMIADNSPENSALVIKMydgLLQAGARLCPT 214
|
170 180 190
....*....|....*....|....*....|.
gi 1149123006 167 DKY-------GTTPLVWAARKGHLECVKHLL 190
Cdd:cd22197 215 VQLeeisnheGLTPLKLAAKEGKIEIFRHIL 245
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
293-342 |
2.84e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 2.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1149123006 293 ADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKA 342
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
255-306 |
2.84e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 2.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1149123006 255 LLDAGTY-VNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 306
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
334-363 |
3.35e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.41 E-value: 3.35e-03
10 20 30
....*....|....*....|....*....|
gi 1149123006 334 DGETPLIKATKMRNIEVVELLLDKGAKVSA 363
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
269-297 |
4.24e-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: 4.24e-03
10 20
....*....|....*....|....*....
gi 1149123006 269 GDTVLIGAVRGGHVEIVRALLQKYADIDI 297
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
269-298 |
5.15e-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: 5.15e-03
10 20 30
....*....|....*....|....*....|.
gi 1149123006 269 GDTVL-IGAVRGGHVEIVRALLQKYADIDIR 298
Cdd:pfam00023 2 GNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
|
|
| PHA02743 |
PHA02743 |
Viral ankyrin protein; Provisional |
351-410 |
5.56e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 39.41 E-value: 5.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123006 351 VELLLDKGAKVSAVDKK-GDTPLHIAIRGRSRKLAELLLRNPkdGRLLYRPNKAGETPYNI 410
Cdd:PHA02743 76 IELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCRQL--GVNLGAINYQHETAYHI 134
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
140-165 |
7.65e-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: 7.65e-03
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
296-408 |
9.75e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123006 296 DIRGQdnkTALYWAVEKGNATMVRDILQCNPDTEICtkDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIA 375
Cdd:PHA02791 27 DVHGH---SALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYA 101
|
90 100 110
....*....|....*....|....*....|...
gi 1149123006 376 IRGRSRKLAELLLRnpKDGRLLYRPNKAGETPY 408
Cdd:PHA02791 102 VDSGNMQTVKLFVK--KNWRLMFYGKTGWKTSF 132
|
|
| |
