|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
18-307 |
4.17e-62 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 214.43 E-value: 4.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 18 IPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELLKCGVNL 97
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 98 EHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGlQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVW 177
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 178 AARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1149123004 258 DAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 307
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
16-274 |
5.55e-59 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 205.57 E-value: 5.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 16 ENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELLKCGV 95
Cdd:COG0666 32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 96 NLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGlQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPL 175
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 176 VWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQD 255
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
250
....*....|....*....
gi 1149123004 256 LLDAGTYVNIPDRSGDTVL 274
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
105-373 |
7.83e-58 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 202.11 E-value: 7.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 105 WTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHL 184
Cdd:COG0666 21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 185 ECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVN 264
Cdd:COG0666 101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 265 IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKAT 344
Cdd:COG0666 181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
|
250 260
....*....|....*....|....*....
gi 1149123004 345 KMRNIEVVELLLDKGAKVSAVDKKGDTPL 373
Cdd:COG0666 261 AAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| KAP_NTPase |
pfam07693 |
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases ... |
441-954 |
8.25e-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: 8.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 441 YDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFagqqieplfqfswlivfltlllcgglgllfaft 520
Cdd:pfam07693 1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 521 vhpnlgiavslsflallyiffiviyfggrregeswnwawvlstrlarhigylelllklmfvnppelpeqttkalPVRFLF 600
Cdd:pfam07693 48 --------------------------------------------------------------------------NEEFII 53
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 601 TDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDTQGKKK--WKKTCCLPSFVIFLFIIGciisgitll 678
Cdd:pfam07693 54 VYFNPWSFSGQDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKigLIFGVAIILALTGLVVAI--------- 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 679 aifrvdpkhltvnavlisiasvvglafvlncrtwwqvldsllnsqrkrlhnaasklhklksEGFMKVLKCEV-ELMARMA 757
Cdd:pfam07693 125 -------------------------------------------------------------EEPMKKLQTEIeELRSDIE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 758 KTIDSftqNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLrdsNINGHDYMRN 837
Cdd:pfam07693 144 STLKD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPNVVFILAADEEILKKALEANYESGL---EIDGQKYLEK 217
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 838 IVHLPVFLNSRGLSNARKFLVTSAtngdvpcsdttgiqedadrrvsQNSLGEMTKLGSKTALnrrdtyrrrqmqrtitrq 917
Cdd:pfam07693 218 IIQVPFTLPPLSLRQLKKFLMLSF----------------------DNSEEGTSSKDRDETL------------------ 257
|
490 500 510
....*....|....*....|....*....|....*..
gi 1149123004 918 MSFDLTKLLVTEDwFSDISPQTMRRLLNIVSVTGRLL 954
Cdd:pfam07693 258 RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
10-241 |
8.68e-57 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 199.02 E-value: 8.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 10 INYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEE 89
Cdd:COG0666 59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 90 LLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGlQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDK 169
Cdd:COG0666 139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123004 170 YGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTAL 241
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
122-394 |
4.37e-56 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 197.10 E-value: 4.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 122 LLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEG 201
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 202 ANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGG 281
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 282 HVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAK 361
Cdd:COG0666 165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
|
250 260 270
....*....|....*....|....*....|...
gi 1149123004 362 VSAVDKKGDTPLHIAIRGRSRKLAELLLRNPKD 394
Cdd:COG0666 245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
151-415 |
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 1149123004 151 ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 230
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 231 NLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWA 310
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 311 VEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLr 390
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL- 239
|
250 260
....*....|....*....|....*
gi 1149123004 391 npKDGRLLYRPNKAGETPYNIDCSH 415
Cdd:COG0666 240 --EAGADLNAKDKDGLTALLLAAAA 262
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
42-133 |
2.02e-27 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 107.51 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 42 LMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELLKCgVNLEHRDMgGWTALMWACYKGRTDVVE 121
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1149123004 122 LLLSHGANPSVT 133
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
49-378 |
1.57e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 114.68 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 49 GNLEIVKELIKNGANC-NLEDLDNWTALISASKEGHVHIVEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHG 127
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCiNISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 128 ANPSVTGLqysvyPIIwaagrgHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmta 207
Cdd:PHA02874 92 VDTSILPI-----PCI------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 208 livavkggytqsvkeilkrnpnVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVR 287
Cdd:PHA02874 150 ----------------------VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 288 ALLQKYADIDIRGQDNKTALYWAVEKGNATMvrDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGAKVSAVD 366
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKD 285
|
330
....*....|..
gi 1149123004 367 KKGDTPLHIAIR 378
Cdd:PHA02874 286 NKGENPIDTAFK 297
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
2-400 |
1.19e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 114.78 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 2 SVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKE 81
Cdd:PHA02876 142 SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 82 GHVHIVEELLKCGVNLEHRDMGGWTALmwacykgrtdvvelllshganpSVTGLQYSVypiiwaagrghadivhLLLQNG 161
Cdd:PHA02876 222 KNIDTIKAIIDNRSNINKNDLSLLKAI----------------------RNEDLETSL----------------LLYDAG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 162 AKVNCSDKYGTTPLVWAARKGHL-ECVKHLLAMGADVDQEGANSMTALIVAVKGGY-TQSVKEILKRNPNVNLTDKDGNT 239
Cdd:PHA02876 264 FSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYIT 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 240 ALMIASK-EGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATM 318
Cdd:PHA02876 344 PLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYM 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 319 -VRDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSrkLAELLLR---NPK 393
Cdd:PHA02876 424 sVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHygaELR 501
|
....*..
gi 1149123004 394 DGRLLYR 400
Cdd:PHA02876 502 DSRVLHK 508
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
153-403 |
1.79e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 108.60 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 153 IVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQS-VKEI----LKRN 227
Cdd:PHA03100 17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdVKEIvkllLEYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 228 PNVNLTDKDGNTALMIAS--KEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHV--EIVRALLQKYADIDIrgqdn 303
Cdd:PHA03100 97 ANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 304 KTALYWAVEKGNATMVRDILqcnpdteictkdGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRK 383
Cdd:PHA03100 172 KNRVNYLLSYGVPINIKDVY------------GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
250 260
....*....|....*....|....*
gi 1149123004 384 LAELLLRN-----PKDGRLLYRPNK 403
Cdd:PHA03100 240 IFKLLLNNgpsikTIIETLLYFKDK 264
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
43-330 |
3.30e-23 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 105.49 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 43 MIAAEQGNLEIVKELIKNGANCNLEDLDNWTAL---ISASKEGHVHIVEELLKCGVNLEHRDMGGWTAL-MWACYKGRTD 118
Cdd:PHA03095 19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 119 VVELLLSHGANPSVTGLqYSVYPI-IWAAG-RGHADIVHLLLQNGAKVNCSDKYGTTPL-VWAARKG-HLECVKHLLAMG 194
Cdd:PHA03095 99 VIKLLIKAGADVNAKDK-VGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNaNVELLRLLIDAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 195 ADVDQEGANSMTAL---IVAVKgGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTE--IVQDLLDAGTYVNIPDRS 269
Cdd:PHA03095 178 ADVYAVDDRFRSLLhhhLQSFK-PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRY 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123004 270 GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTE 330
Cdd:PHA03095 257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
9-279 |
3.49e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 101.58 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 9 VINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCN---LEDLDNWTalisaskeghvh 85
Cdd:PHA02874 39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpIPCIEKDM------------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 86 iVEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQySVYPIIWAAGRGHADIVHLLLQNGAKVN 165
Cdd:PHA02874 107 -IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 166 CSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKggYTQSVKEILKRNPNVNLTDKDGNTALMIA- 244
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAi 262
|
250 260 270
....*....|....*....|....*....|....*
gi 1149123004 245 SKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVR 279
Cdd:PHA02874 263 NPPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
175-267 |
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 1149123004 175 LVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKrNPNVNLTDkDGNTALMIASKEGHTEIVQ 254
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1149123004 255 DLLDAGTYVNIPD 267
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
113-411 |
1.07e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 100.04 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 113 YKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLA 192
Cdd:PHA02874 10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 193 MGADVDqegansmtalIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDT 272
Cdd:PHA02874 90 NGVDTS----------ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 273 VLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATkMRNIEVV 352
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 353 ELLLDKgAKVSAVDKKGDTPLHIAIRGR-SRKLAELLLRNPKDgrLLYRPNKaGETPYNI 411
Cdd:PHA02874 239 ELLINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKAD--ISIKDNK-GENPIDT 294
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
108-199 |
3.38e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 89.79 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 108 LMWACYKGRTDVVELLLSHGANPSVTgLQYSVYPIIWAAGRGHADIVHLLLQNgAKVNCSDkYGTTPLVWAARKGHLECV 187
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|..
gi 1149123004 188 KHLLAMGADVDQ 199
Cdd:pfam12796 78 KLLLEKGADINV 89
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
142-234 |
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 1149123004 142 IIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLA-MGADVDQEGansMTALIVAVKGGYTQSV 220
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNG---RTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1149123004 221 KEILKRNPNVNLTD 234
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
12-264 |
1.71e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 96.27 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 12 YVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQG-----NLEIVKELIKNGANCNLEDLDNWTALISAS--KEGHV 84
Cdd:PHA03100 42 AKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 85 HIVEELLKCGVNLEHRDMGGWTALMWA--CYKGRTDVVELLLSHGANPSVTglqysvypiiwaagrghaDIVHLLLQNGA 162
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAK------------------NRVNYLLSYGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 163 KVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN--------LTD 234
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKtiietllyFKD 263
|
250 260 270
....*....|....*....|....*....|
gi 1149123004 235 KDGNTALMIASKEgHTEIVQDLLDAGTYVN 264
Cdd:PHA03100 264 KDLNTITKIKMLK-KSIMYMFLLDPGFYKN 292
|
|
| 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 1149123004 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNgANCNLEDlDNWTALISASKEGHVHIVEELLK 92
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLE 82
|
....*....
gi 1149123004 93 CGVNLEHRD 101
Cdd:pfam12796 83 KGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
208-299 |
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 1149123004 208 LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTyVNIPDrSGDTVLIGAVRGGHVEIVR 287
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1149123004 288 ALLQKYADIDIR 299
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
274-366 |
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 1149123004 274 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRdILQCNPDTEICTkDGETPLIKATKMRNIEVVE 353
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1149123004 354 LLLDKGAKVSAVD 366
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
241-335 |
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 1149123004 241 LMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLqKYADIDIRGqDNKTALYWAVEKGNATMVR 320
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|....*
gi 1149123004 321 DILQCNPDteICTKD 335
Cdd:pfam12796 79 LLLEKGAD--INVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
74-298 |
1.79e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 90.05 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 74 ALISASKEGHVHIVEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTglqysvYPIIW-----AAGR 148
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVK------YPDIEselhdAVEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 149 GHADIVHLLLQNGAKVN-CSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRN 227
Cdd:PHA02875 79 GDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123004 228 PNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGD-TVLIGAVRGGHVEIVRALLQKYADIDI 298
Cdd:PHA02875 159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
220-390 |
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 1149123004 220 VKEILKRNPNVNLTDKDGNTAL---MIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVE-IVRALLQKYAD 295
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 296 IDIRGQDNKTAL--YWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGAKVSAVDKKGDT 371
Cdd:PHA03095 110 VNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRS 189
|
170 180
....*....|....*....|..
gi 1149123004 372 PLHI---AIRGRSRKLAELLLR 390
Cdd:PHA03095 190 LLHHhlqSFKPRARIVRELIRA 211
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
182-399 |
3.69e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 88.89 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 182 GHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRN--PNVNLTDKDgnTALMIASKEGHTEIVQDLLDA 259
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGaiPDVKYPDIE--SELHDAVEEGDVKAVEELLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 260 GTYVN-IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGET 338
Cdd:PHA02875 91 GKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123004 339 PLIKATKMRNIEVVELLLDKGAKVSAVDKKGD-TPLHIAIRGRSRKLAELLLRNPKDGRLLY 399
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
18-307 |
2.73e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 87.00 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 18 IPALKALLEKCKDVDERNECGQTPLMI--AAEQGNLEIVKELIKNGANCNLEDLDNWT---ALISaSKEGHVHIVEELLK 92
Cdd:PHA03095 97 LDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLK-SRNANVELLRLLID 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 93 CGVNLEHRDMGGWTALMWAC--YKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHL-LLQNGAKVNCSDK 169
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLpLLIAGISINARNR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 170 YGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKdgntALMIASKEGH 249
Cdd:PHA03095 256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGG 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123004 250 TEIVQDLLDAGTYVNIpdRSGDTVLIGAVRGGHVEIVRALLQKYADI-DIRGQDNKTAL 307
Cdd:PHA03095 332 DIPSDATRLCVAKVVL--RGAFSLLPEPIRAYHADFIRECEAEIAVMrTTRIGTGVSLL 388
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
21-292 |
6.98e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.85 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 21 LKALLEKCKDVDERNECGQTPLMIAAEQGN-LEIVKELIKNGANCNLEDLDNWTAL--ISASKEGHVHIVEELLKCGVNL 97
Cdd:PHA03095 66 VRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 98 EHRDMGGWTALmwACYKGRTDV----VELLLSHGANPSVTGL-------QYSVYPiiwaagRGHADIVHLLLQNGAKVNC 166
Cdd:PHA03095 146 NALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVYAVDDrfrsllhHHLQSF------KPRARIVRELIRAGCDPAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 167 SDKYGTTPLvwaarkghlecvkHLLAMGAdvdqeganSMTALIVAvkggytqsvkEILKRNPNVNLTDKDGNTALMIASK 246
Cdd:PHA03095 218 TDMLGNTPL-------------HSMATGS--------SCKRSLVL----------PLLIAGISINARNRYGQTPLHYAAV 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1149123004 247 EGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQK 292
Cdd:PHA03095 267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
151-376 |
9.11e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.46 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 151 ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEIL-KR 226
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 227 NPNVNLTDKDGNTALMI--ASKEGHTEIVQDLLDAGTYVNIPDRSGDT---VLIGAvRGGHVEIVRALLQKYADI---DI 298
Cdd:PHA03095 107 GADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKS-RNANVELLRLLIDAGADVyavDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 299 RGQdnkTALYWAVE--KGNATMVRDILQCNPDTEICTKDGETPLIKA---TKMRNIeVVELLLDKGAKVSAVDKKGDTPL 373
Cdd:PHA03095 186 RFR---SLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRS-LVLPLLIAGISINARNRYGQTPL 261
|
...
gi 1149123004 374 HIA 376
Cdd:PHA03095 262 HYA 264
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
204-436 |
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 1149123004 204 SMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAG---TYVNIPDRSGDTVligavrg 280
Cdd:PHA02874 35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtSILPIPCIEKDMI------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 281 ghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGA 360
Cdd:PHA02874 108 ------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123004 361 KVSAVDKKGDTPLHIAIRGRSRKLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSILTQIFGARHLSPTETDG 436
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDH---GNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDG 254
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
307-394 |
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 1149123004 307 LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAkvSAVDKKGDTPLHIAIRGRSRKLAE 386
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
....*...
gi 1149123004 387 LLLRNPKD 394
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
31-257 |
4.03e-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: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 31 VDERNECGQ-----TPLMIAAEQGNLEIVKELIKNgancnlEDLDNW-------TALISASKEGHVHIVEELLKCGVNLE 98
Cdd:cd22192 5 LDELHLLQQkriseSPLLLAAKENDVQAIKKLLKC------PSCDLFqrgalgeTALHVAALYDNLEAAVVLMEAAPELV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 99 HRDMG-----GWTALMWACYKGRTDVVELLLSHGA---NPSVTG----------LQYSVYPIIWAAGRGHADIVHLLLQN 160
Cdd:cd22192 79 NEPMTsdlyqGETALHIAVVNQNLNLVRELIARGAdvvSPRATGtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 161 GAKVNCSDKYGTTPLvwaarkghlecvkHLLAMGAdvDQEGANSMTALIVA-VKGGYTQSVKEIlkrnPNvnltdKDGNT 239
Cdd:cd22192 159 GADIRAQDSLGNTVL-------------HILVLQP--NKTFACQMYDLILSyDKEDDLQPLDLV----PN-----NQGLT 214
|
250
....*....|....*...
gi 1149123004 240 ALMIASKEGHTEIVQDLL 257
Cdd:cd22192 215 PFKLAAKEGNIVMFQHLV 232
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
13-230 |
5.61e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 76.18 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 13 VEEENIPALKALLEKCKDVDER-NECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELL 91
Cdd:PHA02875 76 VEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 92 KCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVN----CS 167
Cdd:PHA02875 156 DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNimfmIE 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123004 168 DKYGTTplvwaarkghLECVKHllaMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 230
Cdd:PHA02875 236 GEECTI----------LDMICN---MCTNLESEAIDALIADIAIRIHKKTIRRDEGFKNNMST 285
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
220-419 |
5.13e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 73.38 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 220 VKEILKRNPNVNLTDKDGNTAL--------MIASKEGHTEIVQDLLdAGTYVNIPDrsgdtvligAVRGGHVEIVRALLQ 291
Cdd:PHA02878 53 VKSLLTRGHNVNQPDHRDLTPLhiickepnKLGMKEMIRSINKCSV-FYTLVAIKD---------AFNNRNVEIFKIILT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 292 KYA----DIDIRGQDNKTAlywaVEKGNATMVRDILQCNPDTEICTKD-GETPLIKATKMRNIEVVELLLDKGAKVSAVD 366
Cdd:PHA02878 123 NRYkniqTIDLVYIDKKSK----DDIIEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1149123004 367 KKGDTPLHIAIRGRSRKLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSI 419
Cdd:PHA02878 199 KTNNSPLHHAVKHYNKPIVHILLEN---GASTDARDKCGNTPLHISVGYCKDY 248
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
41-352 |
8.21e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.99 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 41 PLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTAL----ISASKEGHVHIVEELLKCGVNLEHRdmggwtALMWACYKGR 116
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLhiicKEPNKLGMKEMIRSINKCSVFYTLV------AIKDAFNNRN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 117 TDVVE-LLLSHGANPSVTGLQY----SVYPIIwaagrgHADIVHLLLQNGAKVNCSDKY-GTTPLVWAARKGHLECVKHL 190
Cdd:PHA02878 114 VEIFKiILTNRYKNIQTIDLVYidkkSKDDII------EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 191 LAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKE-GHTEIVQDLLDAGTYVNIPDR- 268
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYi 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 269 SGDTVLIGAVRGGHVeiVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNpdteICTKDGETPLIKATK--M 346
Cdd:PHA02878 268 LGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN----ICLLKRIKPDIKNSEgfI 341
|
....*.
gi 1149123004 347 RNIEVV 352
Cdd:PHA02878 342 DNMDCI 347
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
432-988 |
1.15e-12 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 71.87 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 432 TETDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGqqieplfqfswlivfltlllcg 511
Cdd:COG4928 1 NETEEDLLGRKKYAESLANLIKSSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 512 glgllfaftvhpnlgiavslsflallyifFIVIYFggrregeswnwawvlstrlarhigylelllklmfvNPpelpeqtt 591
Cdd:COG4928 59 -----------------------------VIVVYF-----------------------------------NA-------- 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 592 kalpvrFLFTDYNRLssvggetsLAEMIATLSDACEREfgflatrlfrvfKTEDTQGKKKWKKtcclpsfviflfiigcI 671
Cdd:COG4928 67 ------WLYDGEEDL--------LAALLSEIAAELEKK------------KKKDKKAAKKLKK----------------Y 104
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 672 ISGITLLAIfrvdpkhltvnavlisIASVVGLafvlncrtWWQVLDSLLNSQRKRLHNAASK-LHKLKSEgFMKVLKcev 750
Cdd:COG4928 105 AKRLSKLAL----------------KAGLLGG--------PAEAVAEALKALLKKEYKSKKKsIEAFREE-LEELLK--- 156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 751 ELMARmaktidsftqnqtRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNsvlrdSNIN 830
Cdd:COG4928 157 ELKGK-------------RLVVFIDDLDRCEPDEAIEVLELIKLFFDFPNVVFVLAFDREILEHALKERYG-----EDID 218
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 831 GHDYMRNIVHLPVFLNSRGLSNARKFLVTSATNGDVPcsdttGIQEDADRRVSQNSLGEMTKLGSKTALNRRDTYRRRQM 910
Cdd:COG4928 219 AREYLEKIIQVPFRLPPLSNELLILELDRLLELLLSA-----LLEALLALLLLRALAESISSLRAEFLLLLLLLKLELLL 293
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123004 911 QRTITRQMSFDLTKLLVTEDW-FSDISPQTMRRLLNIVSVTGRLLRANQISFNWDRLASWINLTEQWPYRTSWLILYLE 988
Cdd:COG4928 294 ALLVLLLKLELLLENLLLAALlLLLDELELKKLLREDVASRASLYFINAELANLSLKLLKISSELLTLELKLEEERELS 372
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
152-320 |
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 1149123004 152 DIVHLLLQNGAKVNcsDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN 231
Cdd:PLN03192 508 NVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 232 LTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNiPDRSGDtVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAV 311
Cdd:PLN03192 586 IRDANGNTALWNAISAKHHKIFRILYHFASISD-PHAAGD-LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
|
....*....
gi 1149123004 312 EKGNATMVR 320
Cdd:PLN03192 664 AEDHVDMVR 672
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
13-308 |
5.78e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 70.29 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLedLDNWTALISASKEGHVHIVEELLk 92
Cdd:PHA02878 45 VEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSV--FYTLVAIKDAFNNRNVEIFKIIL- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 93 cgvnLEHRDMGGWTALMWACYKGRTDVVE-----LLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCS 167
Cdd:PHA02878 122 ----TNRYKNIQTIDLVYIDKKSKDDIIEaeitkLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 168 DKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVkgGYTQS---VKEILKRNPNVNLTDK-DGNTALMI 243
Cdd:PHA02878 198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKDydiLKLLLEHGVDVNAKSYiLGLTALHS 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123004 244 ASKEghTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRG------GHVEIVRALLQKYADIDIRG----QDNKTALY 308
Cdd:PHA02878 276 SIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQylciniGRILISNICLLKRIKPDIKNsegfIDNMDCIT 348
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
204-411 |
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 1149123004 204 SMTALIVAVKGGYTQSVKEILKrNPNVNLTDKD--GNTALMIASKEGHTEIVQDLLDAG-TYVNIPDRS----GDTVLIG 276
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLK-CPSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApELVNEPMTSdlyqGETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 277 AVRGGHVEIVRALLQKYADID---------IRGQDNKtaLYWavekgnatmvrdilqcnpdteictkdGETPLIKATKMR 347
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVspratgtffRPGPKNL--IYY--------------------------GEHPLSFAACVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123004 348 NIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLA----ELLLRNPKDGRL--LYR-PNKAGETPYNI 411
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpLDLvPNNQGLTPFKL 218
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
118-358 |
1.26e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 69.09 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 118 DVVELLLShGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLV-----WAARKGHLECVKHLLA 192
Cdd:PHA02798 19 STVKLLIK-SCNPNEIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 193 MGADVDQEGANSMTALIVAVKGGYTQSVKEIL---KRNPNVNLTDKDGNTALMIASKEGHT---EIVQDLLDAGTYVNIP 266
Cdd:PHA02798 98 NGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 267 -----------------DRSGDTVLIGAVRGGHV-------------EIVRALLQ--------------KYADIDIRGQD 302
Cdd:PHA02798 178 nnkekydtlhcyfkyniDRIDADILKLFVDNGFIinkenkshkkkfmEYLNSLLYdnkrfkknildfifSYIDINQVDEL 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123004 303 NKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDK 358
Cdd:PHA02798 258 GFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK 313
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
9-257 |
2.47e-11 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 68.95 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 9 VINYVEEENIPALKALLEKCK--DVDERNECGQTPLMIAAEQGNLEIVKELIKNgANCNLEDLDnwtALISASKEGHVHI 86
Cdd:TIGR00870 21 FLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLN-LSCRGAVGD---TLLHAISLEYVDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 87 VEELL-------KCGVNLEH---RDMG----GWTALMWACYKGRTDVVELLLSHGAN-------------PSVTGLQYSV 139
Cdd:TIGR00870 97 VEAILlhllaafRKSGPLELandQYTSeftpGITALHLAAHRQNYEIVKLLLERGASvparacgdffvksQGVDSFYHGE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 140 YPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTplvwaarkghlecVKHLLAMGADVDQEG---ANSMTALIVAVKGG- 215
Cdd:TIGR00870 177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNT-------------LLHLLVMENEFKAEYeelSCQMYNFALSLLDKl 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1149123004 216 -YTQSVKEILKRnpnvnltdkDGNTALMIASKEGHTEIVQDLL 257
Cdd:TIGR00870 244 rDSKELEVILNH---------QGLTPLKLAAKEGRIVLFRLKL 277
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
173-358 |
2.81e-11 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 68.50 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 173 TPLVWAARKGHLECVKHLLAM-GADVDQEGANSMTALIVAVKGGYTQSVKEILKRNP---NVNLTDK--DGNTALMIASK 246
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvNEPMTSDlyQGETALHIAVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 247 EGHTEIVQDLLDAGTYVNIPdRS---------------GDTVLIGAVRGGHVEIVRALLQKYADIdiRGQDN--KTALYW 309
Cdd:cd22192 99 NQNLNLVRELIARGADVVSP-RAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADI--RAQDSlgNTVLHI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123004 310 AVEKGNAT----MVRDILQCNP-DTEIC-----TKDGETPLIKATKMRNIEVVELLLDK 358
Cdd:cd22192 176 LVLQPNKTfacqMYDLILSYDKeDDLQPldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
142-303 |
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 1149123004 142 IIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYtQSVK 221
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH-HKIF 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 222 EILKR-----NPNVnltdkdGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADI 296
Cdd:PLN03192 608 RILYHfasisDPHA------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
....*..
gi 1149123004 297 DIRGQDN 303
Cdd:PLN03192 682 DKANTDD 688
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
3-170 |
8.11e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.20 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 3 VLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEG 82
Cdd:PLN03192 523 PNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 83 HVHIVEELLKCGvNLEHRDMGGwTALMWACYKGRTDVVELLLSHGAN------PSVTGLQYsvypiiwAAGRGHADIVHL 156
Cdd:PLN03192 603 HHKIFRILYHFA-SISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNvdsedhQGATALQV-------AMAEDHVDMVRL 673
|
170
....*....|....
gi 1149123004 157 LLQNGAKVNCSDKY 170
Cdd:PLN03192 674 LIMNGADVDKANTD 687
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
194-366 |
8.32e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.20 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 194 GADVDQEGANSmtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTV 273
Cdd:PLN03192 518 GEHDDPNMASN---LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 274 LIGAVRGGHVEIVRALLQkYADIdirgQDNKTA---LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIE 350
Cdd:PLN03192 595 LWNAISAKHHKIFRILYH-FASI----SDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669
|
170
....*....|....*.
gi 1149123004 351 VVELLLDKGAKVSAVD 366
Cdd:PLN03192 670 MVRLLIMNGADVDKAN 685
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
141-191 |
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 1149123004 141 PIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLL 191
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
98-263 |
3.77e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.89 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 98 EHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVW 177
Cdd:PLN03192 519 EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRT-PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWN 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 178 AARKGHLECVKHLLAMGADVDQEGANSMtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:PLN03192 598 AISAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
....*.
gi 1149123004 258 DAGTYV 263
Cdd:PLN03192 676 MNGADV 681
|
|
| 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 1149123004 40 TPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELL 91
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
24-78 |
2.62e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 54.66 E-value: 2.62e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123004 24 LLEKC-KDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISA 78
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| 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 1149123004 71 NWTALISASKEGHVHIVEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLL 124
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
283-391 |
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 1149123004 283 VEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATmVRDILQC------NPDT-EICtkdGETPLIkaTKMRN---IEVV 352
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEK-VKDIVRLlleagaDVNApERC---GFTPLH--LYLYNattLDVI 100
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1149123004 353 ELLLDKGAKVSAVDKKGDTPLHIAIRGRS--RKLAELLLRN 391
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRK 141
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
314-390 |
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 1149123004 314 GNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLR 390
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
237-290 |
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 1149123004 237 GNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALL 290
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 1149123004 13 VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELI 58
Cdd:pfam13637 9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
338-389 |
6.42e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 6.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1149123004 338 TPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLL 389
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
205-257 |
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 1149123004 205 MTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
6-175 |
1.11e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 56.51 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 6 SQSVINY-VEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHV 84
Cdd:PHA02874 124 LKTFLHYaIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 85 HIVEELLKCGVNLEHRDMGGWTALMWACYKGRTdVVELLLShgaNPSV--------TGLQYSV-YPIiwaagrgHADIVH 155
Cdd:PHA02874 204 ACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLIN---NASIndqdidgsTPLHHAInPPC-------DIDIID 272
|
170 180
....*....|....*....|
gi 1149123004 156 LLLQNGAKVNCSDKYGTTPL 175
Cdd:PHA02874 273 ILLYHKADISIKDNKGENPI 292
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
104-158 |
1.21e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 1.21e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1149123004 104 GWTALMWACYKGRTDVVELLLSHGANPSVTGLQySVYPIIWAAGRGHADIVHLLL 158
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
157-211 |
2.51e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 2.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123004 157 LLQNG-AKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVA 211
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
171-221 |
3.86e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 3.86e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1149123004 171 GTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVK 221
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1-129 |
9.29e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.52 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 1 MSVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQ--GNLEIVKELIKNGAN--------------- 63
Cdd:PHA03100 69 STPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANvniknsdgenllhly 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 64 --CNLEDLD----------------------------------NWTALISASKEGHVHIVEELLKCGVNLEHRDMGGWTA 107
Cdd:PHA03100 149 leSNKIDLKilkllidkgvdinaknrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
|
170 180
....*....|....*....|..
gi 1149123004 108 LMWACYKGRTDVVELLLSHGAN 129
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLNNGPS 250
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
38-66 |
9.73e-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: 9.73e-07
10 20
....*....|....*....|....*....
gi 1149123004 38 GQTPLMIAAEQGNLEIVKELIKNGANCNL 66
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
52-291 |
9.97e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 53.59 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 52 EIVKELIKNGANCNLED---------LDNWTalISASKegHVHIVEELLKCGVNLEHRDMGGWTALMWACYK---GRTDV 119
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGyietplcavLRNRE--ITSNK--IKKIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 120 VELLLSHGAN-PSVTGLQ-YSVYPIIWAAGRGHADIVHLLLQNGakVNCSDK---YGTTPLVWAARKG----HLECVKHL 190
Cdd:PHA02989 127 LRFLLSKGINvNDVKNSRgYNLLHMYLESFSVKKDVIKILLSFG--VNLFEKtslYGLTPMNIYLRNDidviSIKVIKYL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 191 LAMGADVDQEGANSMTALIVAVKGGYTQSVKE------ILKRnPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVN 264
Cdd:PHA02989 205 IKKGVNIETNNNGSESVLESFLDNNKILSKKEfkvlnfILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIY 283
|
250 260
....*....|....*....|....*..
gi 1149123004 265 IPDRSGDTVLIGAVRGGHVEIVRALLQ 291
Cdd:PHA02989 284 NVSKDGDTVLTYAIKHGNIDMLNRILQ 310
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
146-257 |
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 1149123004 146 AGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmtalivavkggytqsvkeilk 225
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD----------------------------- 140
|
90 100 110
....*....|....*....|....*....|..
gi 1149123004 226 rnpnVNLTDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:PTZ00322 141 ----PTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| 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 1149123004 38 GQTPLMIAAEQ-GNLEIVKELIKNGANCNLED 68
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
226-277 |
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 1149123004 226 RNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGA 277
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
5-231 |
1.91e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 52.53 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 5 ISQSVINYVEEENIpaLKALLEKCKDVDERNECGQTPLMIAAEQG---NLEIVKELIKNGANCNLEDLDNWTALISASKE 81
Cdd:PHA02798 78 ILSNIKDYKHMLDI--VKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 82 GH---VHIVEELLKCGVNL-EHRDMGGWTALmwACY------KGRTDVVELLLSHG------ANPSVTGLQYSVYPIIWA 145
Cdd:PHA02798 156 NHhidIEIIKLLLEKGVDInTHNNKEKYDTL--HCYfkynidRIDADILKLFVDNGfiinkeNKSHKKKFMEYLNSLLYD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 146 AGRGHADIVHLLLQNgAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILK 225
Cdd:PHA02798 234 NKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILN 312
|
....*.
gi 1149123004 226 RNPNVN 231
Cdd:PHA02798 313 KKPNKN 318
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
178-423 |
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 1149123004 178 AARKGHLECVKHLLAMGADVDQEGANSM--TALIVAVKGGYTQSVKEILKRNPNVNLTdkdGNTALMIASKEGHtEIVQD 255
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPKKLNINCPDRLgrSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISLEYV-DAVEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 256 LL--------DAGTYVNIPDRSGD------TVLIGAVRGGHVEIVRALLQKYADIDIRGqdnktalywaveKGNATMVRD 321
Cdd:TIGR00870 100 ILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARA------------CGDFFVKSQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 322 ILQcnpdteiCTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAI-----RGRSRKLA----ELLLR-- 390
Cdd:TIGR00870 168 GVD-------SFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefKAEYEELScqmyNFALSll 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1149123004 391 -NPKDGRLLYR-PNKAGETPYNIDCSHQKSILTQI 423
Cdd:TIGR00870 241 dKLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRL 275
|
|
| 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 1149123004 37 CGQTPLMIAAEQGNLEIVKELIKNGANCN 65
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
51-328 |
4.62e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 51.37 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 51 LEIVKELIKNGANCNLEDLDNWTALISaskeghvhIVEELLKcgvnlehrdmggwtalmwacYKGRTDVVELLLSHGANP 130
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCT--------ILSNIKD--------------------YKHMLDIVKILIENGADI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 131 SVTGL--QYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECVKHLLAMGADVDQ----EG 201
Cdd:PHA02798 103 NKKNSdgETPLYCLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThnnkEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 202 ANSMTALIvavKGGYTQSVKEILKRNPN----VNLTDKDGNTALM-------IASKEGHTEIVQDLLdagTYVNIPDRS- 269
Cdd:PHA02798 183 YDTLHCYF---KYNIDRIDADILKLFVDngfiINKENKSHKKKFMeylnsllYDNKRFKKNILDFIF---SYIDINQVDe 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 270 -GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPD 328
Cdd:PHA02798 257 lGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
12-174 |
5.23e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 49.43 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 12 YVEEENIPALKALLekcKDVDERNECGQTPLMIAAEQ--GNLEIVKELIKNGANCNLEDLD-NWTAL---ISASKEGHVH 85
Cdd:PHA02859 28 YVEKDDIEGVKKWI---KFVNDCNDLYETPIFSCLEKdkVNVEILKFLIENGADVNFKTRDnNLSALhhyLSFNKNVEPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 86 IVEELLKCGVNLEHRDMGGWTAL-MWAC-YKGRTDVVELLLSHGANPsvTGLQYSVYPIIWAAGRGHAD--IVHLLLQNG 161
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLhMYMCnFNVRINVIKLLIDSGVSF--LNKDFDNNNILYSYILFHSDkkIFDFLTSLG 182
|
170
....*....|...
gi 1149123004 162 AKVNCSDKYGTTP 174
Cdd:PHA02859 183 IDINETNKSGYNC 195
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-133 |
5.42e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 44.59 E-value: 5.42e-06
10 20 30
....*....|....*....|....*....|.
gi 1149123004 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 1149123004 104 GWTALMWACYKGRTDVVELLLSHGANPSV 132
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
236-268 |
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 1149123004 236 DGNTALMIAS-KEGHTEIVQDLLDAGTYVNIPDR 268
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
123-175 |
1.40e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 1.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1149123004 123 LLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPL 175
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
211-411 |
2.14e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 48.90 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 211 AVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVL--IGAVRGGHVEIVRA 288
Cdd:PHA02946 46 GIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 289 LLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGAKVSAVD 366
Cdd:PHA02946 126 LVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1149123004 367 KKGDTPLHIAIRGRSRKLAELLLRNPKDGrlLYRPNKAGETPYNI 411
Cdd:PHA02946 206 HDGNTPLHIVCSKTVKNVDIINLLLPSTD--VNKQNKFGDSPLTL 248
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
52-235 |
2.45e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 48.97 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 52 EIVKELIKNGANCNLEDLDNWTAL---ISASKEGHVHIVEELLKCGVNL-EHRDMGGWTAL-MW-ACYKGRTDVVELLLS 125
Cdd:PHA02989 89 KIVKLLLKFGADINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVnDVKNSRGYNLLhMYlESFSVKKDVIKILLS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 126 HGANPSVTGLQYSVYPI-IWAagRGHADIVHL-----LLQNGA------------------------------------- 162
Cdd:PHA02989 169 FGVNLFEKTSLYGLTPMnIYL--RNDIDVISIkvikyLIKKGVnietnnngsesvlesfldnnkilskkefkvlnfilky 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123004 163 -KVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDK 235
Cdd:PHA02989 247 iKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLKPGKYLIKK 320
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
349-413 |
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 1149123004 349 IEVVELLLDKGAKVSAVDKK-GDTPLHIAIRGRSRKLAELLLRNPKDGRLLYrpNKAGETPYNIDC 413
Cdd:PHA02736 71 QEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEIL--NYAFKTPYYVAC 134
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
170-198 |
3.45e-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 1149123004 170 YGTTPLVWAARKGHLECVKHLLAMGADVD 198
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 1149123004 54 VKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELLKCGVNLEHRDMGGWTALMWACYKGRTDVVELLLSH 126
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
60-257 |
4.98e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 48.26 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 60 NGANC------NLEDLDNWTALI---SASKEGHvhiveelLKCGVNLEHRD--MGGWTALMWACYKGRTDVVELLLSHGA 128
Cdd:cd22196 46 TGKTCllkamlNLHNGQNDTISLlldIAEKTGN-------LKEFVNAAYTDsyYKGQTALHIAIERRNMHLVELLVQNGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 129 -------------NPSVTGLQYSVYPIIWAAGRGHADIVHLLLQN---GAKVNCSDKYGTTplvwaarkghlecVKHLLA 192
Cdd:cd22196 119 dvharasgeffkkKKGGPGFYFGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNT-------------VLHALV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123004 193 MGADVDQEGANSMTALivavkggYTQSVKEILKRNPNVNL---TDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:cd22196 186 EVADNTPENTKFVTKM-------YNEILILGAKIRPLLKLeeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
30-257 |
5.56e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 47.95 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 30 DVDERNECGQTPLMIAA---EQGNLEIVKELIKNGancnlEDLDNWTALISASkeghvhIVEELLKcgvnlehrdmgGWT 106
Cdd:cd21882 18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAA-----PDSGNPKELVNAP------CTDEFYQ-----------GQT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 107 ALMWACYKGRTDVVELLLSHGANPSV------------TGLQYSVYPIIWAAGRGHADIVHLLLQNGAK---VNCSDKYG 171
Cdd:cd21882 76 ALHIAIENRNLNLVRLLVENGADVSAratgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 172 TTplvwaarkghlecVKHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrnpnvnlTDKDGNTALMIASK 246
Cdd:cd21882 156 NT-------------VLHALVLQADNTPENSAFVCQmynllLSYGAHLDPTQQLEEI---------PNHQGLTPLKLAAV 213
|
250
....*....|.
gi 1149123004 247 EGHTEIVQDLL 257
Cdd:cd21882 214 EGKIVMFQHIL 224
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-132 |
6.04e-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: 6.04e-05
10 20
....*....|....*....|....*....
gi 1149123004 104 GWTALMWACYKGRTDVVELLLSHGANPSV 132
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
170-199 |
6.23e-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 1149123004 170 YGTTPLVWAA-RKGHLECVKHLLAMGADVDQ 199
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
305-356 |
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 1149123004 305 TALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLL 356
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 1149123004 90 LLKCG-VNLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVT 133
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK 45
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
117-209 |
8.94e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 46.51 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 117 TDVVELLLSHGANPSV---TGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGT-TPLVWAARKGHLECVKHLLA 192
Cdd:PHA02884 46 TDIIDAILKLGADPEApfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLS 125
|
90
....*....|....*..
gi 1149123004 193 MGADVDQEgANSMTALI 209
Cdd:PHA02884 126 YGADINIQ-TNDMVTPI 141
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
284-451 |
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 1149123004 284 EIVRALLQ--------------KYADIDIRGQdnkTALYWAVEKGNATMVRDILQCNPDTEICTKD-------------- 335
Cdd:cd22194 111 EIVRILLAfaeengildrfinaEYTEEAYEGQ---TALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyf 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 336 GETPLIKATKMRNIEVVELLLDKGAK-VSAVDKKGDTPLH----IAIRGRSR-----KLAELLLRNPKDGRLLYRPNKAG 405
Cdd:cd22194 188 GETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHalvtVAEDSKTQndfvkRMYDMILLKSENKNLETIRNNEG 267
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1149123004 406 ETPYNIDCSHQK-SILTQIFG-------ARHLSPTETDgdmLGYDLYSSALADI 451
Cdd:cd22194 268 LTPLQLAAKMGKaEILKYILSreikekpNRSLSRKFTD---WAYGPVSSSLYDL 318
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
152-257 |
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 1149123004 152 DIVHLLLQNGAKVNCSDK--------------YGTTPLVWAARKGHLECVKHLLAMGADV----DQEGANSMTALIVAVK 213
Cdd:cd22194 155 DIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKESTDitsqDSRGNTVLHALVTVAE 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1149123004 214 GGYTQ--SVKE----ILKRNPNVNL---TDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:cd22194 235 DSKTQndFVKRmydmILLKSENKNLetiRNNEGLTPLQLAAKMGKAEILKYIL 287
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
270-320 |
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 1149123004 270 GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVR 320
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
274-394 |
1.57e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.14 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 274 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVE 353
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1149123004 354 LLLDKGAKVSAV-DKKGDTPLHIAIRGRSRKLAELLLRNPKD 394
Cdd:PHA02875 86 ELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
303-437 |
1.62e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.14 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 303 NKTALYWAVEKGNATMVRDILQC--NPDTEIctKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAI-RG 379
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIgiNPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVeEG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123004 380 RSRKLAELLLRNPKDGRLLYrpnKAGETPYNIDCSHQKSILTQIFGARHLSPTETDGD 437
Cdd:PHA02875 80 DVKAVEELLDLGKFADDVFY---KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
269-356 |
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 1149123004 269 SGDTVliGAvrgghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN 348
Cdd:PTZ00322 92 SGDAV--GA---------RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
....*...
gi 1149123004 349 IEVVELLL 356
Cdd:PTZ00322 161 REVVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
189-290 |
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 1149123004 189 HLLAMGADVDQEGANSMTA-LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPD 267
Cdd:PTZ00322 66 HNLTTEEVIDPVVAHMLTVeLCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
|
90 100
....*....|....*....|...
gi 1149123004 268 RSGDTVLIGAVRGGHVEIVRALL 290
Cdd:PTZ00322 146 KDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
57-108 |
3.29e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 3.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1149123004 57 LIKNG-ANCNLEDLDNWTALISASKEGHVHIVEELLKCGVNLEHRDMGGWTAL 108
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
335-367 |
3.73e-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: 3.73e-04
10 20 30
....*....|....*....|....*....|....
gi 1149123004 335 DGETPLIKA-TKMRNIEVVELLLDKGAKVSAVDK 367
Cdd:pfam00023 1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
191-394 |
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 1149123004 191 LAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNP--NVNLTDKDGNTALMIASKEGHTEIVQDLLdagTYVNIPDR 268
Cdd:TIGR00870 4 LDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELL---LNLSCRGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 269 SGDTvLIGAVRGGHVEIVRALLQKYADIDiRGQDNktaLYWAVEKGNATMVRDIlqcnpdteictkdgeTPLIKATKMRN 348
Cdd:TIGR00870 81 VGDT-LLHAISLEYVDAVEAILLHLLAAF-RKSGP---LELANDQYTSEFTPGI---------------TALHLAAHRQN 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 349 IEVVELLLDKGAKVSA-------VDKKGDT-------PLHIAIRGRSRKLAELLLRNPKD 394
Cdd:TIGR00870 141 YEIVKLLLERGASVPAracgdffVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPAD 200
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
322-376 |
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 1149123004 322 ILQCNP-DTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIA 376
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
339-424 |
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 1149123004 339 PLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLRNPKDGRLLYRPNKAGETPYNIDCSHQKS 418
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
|
....*.
gi 1149123004 419 ILTQIF 424
Cdd:PHA02878 120 ILTNRY 125
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
91-257 |
4.95e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 44.79 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 91 LKCGVNLEHRDMG--GWTALMWACYKGRTDVVELLLSHGA-----------NPSV--TGLQYSVYPIIWAAGRGHADIVH 155
Cdd:cd22193 61 LKRFINAEYTDEYyeGQTALHIAIERRQGDIVALLVENGAdvhahakgrffQPKYqgEGFYFGELPLSLAACTNQPDIVQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 156 LLLQNG---AKVNCSDKYGTTPLvwaarkghlecvkHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrn 227
Cdd:cd22193 141 YLLENEhqpADIEAQDSRGNTVL-------------HALVTVADNTKENTKFVTRmydmiLIRGAKLCPTVELEEI---- 203
|
170 180 190
....*....|....*....|....*....|
gi 1149123004 228 pnvnlTDKDGNTALMIASKEGHTEIVQDLL 257
Cdd:cd22193 204 -----RNNDGLTPLQLAAKMGKIEILKYIL 228
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
141-169 |
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 1149123004 141 PIIWAAGR-GHADIVHLLLQNGAKVNCSDK 169
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
22-103 |
9.09e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 22 KALLEKCKDVDERNECGQTPLMIAAEQGNLEIVKELIKNGANCNLEDLDNWTALISASKEGHVHIVEELLKCGVnlEHRD 101
Cdd:PTZ00322 99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ--CHFE 176
|
..
gi 1149123004 102 MG 103
Cdd:PTZ00322 177 LG 178
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
173-198 |
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
|
| 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 1149123004 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 ... |
236-265 |
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 1149123004 236 DGNTALMIASKEGHTEIVQDLLDAGTYVNI 265
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
32-191 |
2.68e-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: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 32 DERNECGQTPLMIAAEQGNleiVKELIKngANCNLEDLDNWTALISASKEGHVHIVEELLKCGVNLEHRDMG-------- 103
Cdd:cd22197 60 DGVNACIMPLLEIDKDSGN---PKPLVN--AQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 104 -----GWTALMWACYKGRTDVVELLLSHGANPSVTGLQYSVYPIIWAAGRGHAD--------IVHL---LLQNGAKVNCS 167
Cdd:cd22197 135 tcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQDSLGNTVLHALVMIADnspensalVIKMydgLLQAGARLCPT 214
|
170 180 190
....*....|....*....|....*....|.
gi 1149123004 168 DKY-------GTTPLVWAARKGHLECVKHLL 191
Cdd:cd22197 215 VQLeeisnheGLTPLKLAAKEGKIEIFRHIL 245
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
294-343 |
2.81e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 2.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1149123004 294 ADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKA 343
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
256-307 |
2.81e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 2.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1149123004 256 LLDAGTY-VNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 307
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
335-364 |
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 1149123004 335 DGETPLIKATKMRNIEVVELLLDKGAKVSA 364
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
120-204 |
3.48e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.19 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 120 VELLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQ 199
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRT-PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
|
....*
gi 1149123004 200 EGANS 204
Cdd:PTZ00322 177 LGANA 181
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
270-298 |
4.24e-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 1149123004 270 GDTVLIGAVRGGHVEIVRALLQKYADIDI 298
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
270-299 |
5.15e-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 1149123004 270 GDTVL-IGAVRGGHVEIVRALLQKYADIDIR 299
Cdd:pfam00023 2 GNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
|
|
| PHA02743 |
PHA02743 |
Viral ankyrin protein; Provisional |
352-411 |
5.57e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 39.41 E-value: 5.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123004 352 VELLLDKGAKVSAVDKK-GDTPLHIAIRGRSRKLAELLLRNPkdGRLLYRPNKAGETPYNI 411
Cdd:PHA02743 76 IELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCRQL--GVNLGAINYQHETAYHI 134
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
141-166 |
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 |
297-409 |
9.76e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123004 297 DIRGQdnkTALYWAVEKGNATMVRDILQCNPDTEICtkDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIA 376
Cdd:PHA02791 27 DVHGH---SALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYA 101
|
90 100 110
....*....|....*....|....*....|...
gi 1149123004 377 IRGRSRKLAELLLRnpKDGRLLYRPNKAGETPY 409
Cdd:PHA02791 102 VDSGNMQTVKLFVK--KNWRLMFYGKTGWKTSF 132
|
|
| |
