|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
85-385 |
5.88e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 147.02 E-value: 5.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 85 LLMIINESAKEGINALDSQGNTPLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGTTDI 164
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 165 NLEGDLGNTPVMQACYKDNHEALILLLSRGAKLCKKNKLGCYPIHMTAFMGSLKCMDIVLNKGEEsgctidhqINFTNNE 244
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD--------VNAQDND 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 245 KSSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGATEIVKFMVSsyNGDNkiVDLPDGNDETPLHKSVL 324
Cdd:COG0666 153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE--AGAD--VNAKDNDGKTALDLAAE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1951993450 325 FDHVELAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLLAKGADVKLKDNFGRNFL 385
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
32-352 |
5.37e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 141.24 E-value: 5.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 32 LDENPSLIFKLIAEGNICRVRNFVLKNPGSLAARDDSEATPLHHAAKLGSMDLLLMIINESAKEGINALDSQGNTPLHWA 111
Cdd:COG0666 15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 112 VEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGtTDINLEGDLGNTPVMQACYKDNHEALILLL 191
Cdd:COG0666 95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 192 SRGAKlckknklgcypihmtafmgslkcmdivlnkgeesgctidhqINFTNNEKSSPLHLAVQNGNIDVVKACISYGAKI 271
Cdd:COG0666 174 EAGAD-----------------------------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 272 DLRQSDNATALHFAATQGATEIVKFMVSSYNGDNKIvdlpDGNDETPLHKSVLFDHVELAEYLISAGANINSEDKESRTP 351
Cdd:COG0666 213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK----DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
.
gi 1951993450 352 L 352
Cdd:COG0666 289 L 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
6-282 |
5.13e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 138.55 E-value: 5.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 6 RRMLSSKGKKSNVYDGIFLQDESCSSLDENPSLIFKLIAEGNICRVRNFVLKNPGSLAARDDSEATPLHHAAKLGSMDLL 85
Cdd:COG0666 24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 86 LMIINESAKegINALDSQGNTPLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGtTDIN 165
Cdd:COG0666 104 KLLLEAGAD--VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 166 LEGDLGNTPVMQACYKDNHEALILLLSRGAKLCKKNKLGCYPIHMTAFMGSLKCMDIVLNKGEesgctidhQINFTNNEK 245
Cdd:COG0666 181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA--------DLNAKDKDG 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 1951993450 246 SSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATAL 282
Cdd:COG0666 253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
156-442 |
3.44e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 136.24 E-value: 3.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 156 LILHGTTDINLEGDLGNTPVMQACYKDNHEALILLLSRGAKLCKKNKLGCYPIHMTAFMGSLKCMDIVLNKGEEsgctid 235
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 236 hqINFTNNEKSSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGATEIVKFMVSsyNGDNkiVDLPDGND 315
Cdd:COG0666 80 --INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE--AGAD--VNAQDNDG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 316 ETPLHKSVLFDHVELAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLLAKGADVKLKDNFGRNFLHLMVlqpggL 395
Cdd:COG0666 154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA-----E 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1951993450 396 KNLNNDFLQMENIKQLVTDEDCEGCTPLHYACRHGVPNSVNNLLGLN 442
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
238-557 |
7.99e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 117.75 E-value: 7.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 238 INFTNNEKSSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGATEIVKFMvssyNGDNKIVDLPDGNDET 317
Cdd:COG0666 14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLL----LAAGADINAKDDGGNT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 318 PLHKSVLFDHVELAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLLAKGADVKLKDNFGRnflhlmvlqpgglkn 397
Cdd:COG0666 90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN--------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 398 lnndflqmenikqlvtdedcegcTPLHYACRHGVPNSVNNLLGLNMSLYSKSKNKRSPLHFAACYGRFNTCQRLLRFMSD 477
Cdd:COG0666 155 -----------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 478 arlLNDGDEKGLTPLHLAAENGHEKIVFL-LLKKGALLLSDHHGWTALHYAALNGYTRTIRTLLETSIGLIDKTDKENNT 556
Cdd:COG0666 212 ---VNAKDNDGKTALDLAAENGNLEIVKLlLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
.
gi 1951993450 557 A 557
Cdd:COG0666 289 L 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
328-606 |
6.18e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 103.50 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 328 VELAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLLAKGADVKLKDNFGRNFLHLMVLqpgglKNLNNDFLQMEN 407
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAAL-----AGDLLVALLLLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 408 IKQLVTDEDCEGCTPLHYACRHGVPNSVNNLLGLNMSLYSKSKNKRSPLHFAACYGRFNTCQRLLRFMSDarlLNDGDEK 487
Cdd:COG0666 76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDND 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 488 GLTPLHLAAENGHEKIV-FLLLKKGALLLSDHHGWTALHYAALNGYTRTIRTLLETSIgLIDKTDKENNTAIHLAGREGH 566
Cdd:COG0666 153 GNTPLHLAAANGNLEIVkLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGN 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1951993450 567 AKAVSLLLENGASIML-NANGASFIHEAIRYGKKDAVLASI 606
Cdd:COG0666 232 LEIVKLLLEAGADLNAkDKDGLTALLLAAAAGAALIVKLLL 272
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
249-345 |
1.14e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.78 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 249 LHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGATEIVKFMVSSYNGDNKivdlpdGNDETPLHKSVLFDHV 328
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK------DNGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 1951993450 329 ELAEYLISAGANINSED 345
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
81-355 |
7.20e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 91.24 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 81 SMDLLLMIINESAkeGINALDSQGNTPLHWAVEKNKVDCLKV---LLCRGADPNIPNYYRLTPLHLAIQlFHNT--IVET 155
Cdd:PHA03095 26 TVEEVRRLLAAGA--DVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLY-NATTldVIKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 156 LILHGTtDINLEGDLGNTPvMQACYKD---NHEALILLLSRGAKLCKKNKLGCYPIHmtAFMGSLKC-MDIV---LNKGE 228
Cdd:PHA03095 103 LIKAGA-DVNAKDKVGRTP-LHVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSRNAnVELLrllIDAGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 229 EsgctidhqINFTNNEKSSPLHLAVQN--GNIDVVKACISYGAKIDLRQSDNATALHFAATQG---ATEIVKFMVssyng 303
Cdd:PHA03095 179 D--------VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLI----- 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1951993450 304 DNKIVDLPDGNDETPLHKSVLFDHVELAEYLISAGANINSEDKESRTPLLLA 355
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
50-480 |
1.48e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 88.20 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 50 RVRNFVLKNPGSLAARDDSEATPLHHAAKLGSMDLLLMIINESAKEGINALDsqGNTPLHWAVEKNKVDCLK-------- 121
Cdd:PHA02876 159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD--DLSVLECAVDSKNIDTIKaiidnrsn 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 122 ---------------------VLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGTTDINLEGDLGNTPV-MQAC 179
Cdd:PHA02876 237 inkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLyLMAK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 180 YKDNHEALILLLSRGAKLCKKNKLGCYPIHMTAFMGSLKcmDIVLNKGEesgctIDHQINFTNNEKSSPLHLAVQNGNID 259
Cdd:PHA02876 317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLE-----LGANVNARDYCDKTPIHYAAVRNNVV 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 260 VVKACISYGAKIDLRQSDNATALHFA--ATQGATEIVKFMVSSYNGDNKIVDLpdgndETPLHKSVLFD-HVELAEYLIS 336
Cdd:PHA02876 390 IINTLLDYGADIEALSQKIGTALHFAlcGTNPYMSVKTLIDRGANVNSKNKDL-----STPLHYACKKNcKLDVIEMLLD 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 337 AGANINSEDKESRTPLLLATSCSAwkSVNLLLAKGADvkLKDNfgrNFLHlmvlqpgglKNLNNDFLQMENIKQLVTDED 416
Cdd:PHA02876 465 NGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAE--LRDS---RVLH---------KSLNDNMFSFRYIIAHICIQD 528
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1951993450 417 cegctplhyACRHGVPNSVNNLLGLNMSLYSKSKNKRSPLHFAACYGR-FNTCQRLLRFMSDARL 480
Cdd:PHA02876 529 ---------FIRHDIRNEVNPLKRVPTRFTSLRESFKEIIQSDDTFKRiWLRCKEELKDISKIRI 584
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
43-385 |
2.86e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 82.70 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 43 IAEGNICRVRNFVLKNPGSLAARDDSEATPLHHAAKLGSMDLLLMIINESAKegINALDSQGNTPLHWAVEKNKVDCLKV 122
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGAD--INHINTKIPHPLLTAIKIGAHDIIKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 123 LLCRGADPNIpnyyrltplhLAIQLFHNTIVETlILHGTTDINLEGDLGNTPVMQACYKDNHEALILLLSRGAKLCKKNK 202
Cdd:PHA02874 87 LIDNGVDTSI----------LPIPCIEKDMIKT-ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 203 LGCYPIHMTAFMGSLKCMDIVLNKGEesgctidhQINFTNNEKSSPLHLAVQNGNIDVVKACISYGAKIdlrqsdnatal 282
Cdd:PHA02874 156 NGCYPIHIAIKHNFFDIIKLLLEKGA--------YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI----------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 283 hfaatqgateivkfMVSSYNGdnkivdlpdgndETPLHKSVLFDHvELAEYLISaGANINSEDKESRTPLLLATS--CSA 360
Cdd:PHA02874 217 --------------MNKCKNG------------FTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAINppCDI 268
|
330 340
....*....|....*....|....*
gi 1951993450 361 wKSVNLLLAKGADVKLKDNFGRNFL 385
Cdd:PHA02874 269 -DIIDILLYHKADISIKDNKGENPI 292
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
315-597 |
8.15e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 81.61 E-value: 8.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 315 DETPLHKSVLFDHVELAE---YLISAGANINSEDKESRTPL-LLATSCSAWKSVNLLLAKGADVKLKDNFGRNFLHLMvl 390
Cdd:PHA03095 47 GKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVY-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 391 qpggLKNLNNDFlqmENIKQL------VTDEDCEGCTPLH-YACRHGV-PNSVNNLLGLNMSLYSKSKNKRSPLHFAACY 462
Cdd:PHA03095 125 ----LSGFNINP---KVIRLLlrkgadVNALDLYGMTPLAvLLKSRNAnVELLRLLIDAGADVYAVDDRFRSLLHHHLQS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 463 GRFNTC--QRLLRFMSDARLLNDGdekGLTPLHLAAENGHEK---IVFLLLKKGALLLSDHHGWTALHYAALNGYTRTIR 537
Cdd:PHA03095 198 FKPRARivRELIRAGCDPAATDML---GNTPLHSMATGSSCKrslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACR 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1951993450 538 TLLE--TSIGLIDKTdkeNNTAIHLAGREGHAKAVSLLL-----------------ENGASIMLNANGASFIHEAIRYG 597
Cdd:PHA03095 275 RLIAlgADINAVSSD---GNTPLSLMVRNNNGRAVRAALaknpsaetvaatlntasVAGGDIPSDATRLCVAKVVLRGA 350
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
71-309 |
8.88e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 81.25 E-value: 8.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 71 TPLHHAAKLGSMDLLLMIINESAKEGINALDSQGNTPLH---WAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQ- 146
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISk 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 147 -LFHNTIVETLILHGTtDINLEGDLGNTPVMQA--CYKDNHEALILLLSRGAKLCKKNKLgcypihmtafmgslkcmDIV 223
Cdd:PHA03100 117 kSNSYSIVEYLLDNGA-NVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRV-----------------NYL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 224 LNKGeesgctidHQINFTNNEKSSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGATEIVKFMVSSYNG 303
Cdd:PHA03100 179 LSYG--------VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
....*.
gi 1951993450 304 DNKIVD 309
Cdd:PHA03100 251 IKTIIE 256
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
108-201 |
2.36e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.46 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 108 LHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGTTDINlegDLGNTPVMQACYKDNHEAL 187
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1951993450 188 ILLLSRGAKLCKKN 201
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
238-527 |
5.16e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.85 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 238 INFTNNEKSSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGATEIVKFMVSsyNG-DNKIVDLPDGNDE 316
Cdd:PHA02874 28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID--NGvDTSILPIPCIEKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 317 TplhksvlfdhvelAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLLAKGADVKLKDNfgrnflhlmvlqpgglk 396
Cdd:PHA02874 106 M-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD----------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 397 nlnndflqmenikqlvtdedcEGCTPLHYACRHGVPNSVNNLLGLNMSLYSKSKNKRSPLHFAACYGRFNTCQRLLRFMS 476
Cdd:PHA02874 156 ---------------------NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1951993450 477 DarlLNDGDEKGLTPLHLAAENgHEKIVFLLLKKGALLLSDHHGWTALHYA 527
Cdd:PHA02874 215 H---IMNKCKNGFTPLHNAIIH-NRSAIELLINNASINDQDIDGSTPLHHA 261
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
113-504 |
7.38e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 78.53 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 113 EKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHntivetlilhgttdinlegdlgntpvmqacyKDNHEALILLLS 192
Cdd:PHA03095 23 SNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSS-------------------------------EKVKDIVRLLLE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 193 RGAklckknklgcypihmtafmgslkcmdiVLNKGEESGCTidhqinftnnekssPLHLAVQNGN-IDVVKACISYGAKI 271
Cdd:PHA03095 72 AGA---------------------------DVNAPERCGFT--------------PLHLYLYNATtLDVIKLLIKAGADV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 272 DLRqsdnatalhfaatqgateivkfmvssyngdnkivdlpDGNDETPLHK--SVLFDHVELAEYLISAGANINSEDKESR 349
Cdd:PHA03095 111 NAK-------------------------------------DKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGM 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 350 TPL---LLATSCSAwKSVNLLLAKGADVKLKDNFGRNFLHLMvlqpggLKNLNNDFLQMENIKQLVTD---EDCEGCTPL 423
Cdd:PHA03095 154 TPLavlLKSRNANV-ELLRLLIDAGADVYAVDDRFRSLLHHH------LQSFKPRARIVRELIRAGCDpaaTDMLGNTPL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 424 HYA-----CRHGVpnsVNNLLGLNMSLYSKSKNKRSPLHFAACYGRFNTCQRLLRFMSDARLLndgDEKGLTPLHLAAEN 498
Cdd:PHA03095 227 HSMatgssCKRSL---VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV---SSDGNTPLSLMVRN 300
|
....*.
gi 1951993450 499 GHEKIV 504
Cdd:PHA03095 301 NNGRAV 306
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
71-205 |
8.03e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.11 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 71 TPLHHAAKLGSMDLLLMIInESAKEGINALDSQGNTPLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHN 150
Cdd:PHA02875 70 SELHDAVEEGDVKAVEELL-DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1951993450 151 TIVETLILHGTTdINLEGDLGNTPVMQACYKDNHEALILLLSRGAKLCKKNKLGC 205
Cdd:PHA02875 149 KGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
107-355 |
3.55e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 76.46 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 107 PLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAI----------------------------QLFHNTIVETLIL 158
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikDAFNNRNVEIFKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 159 HGTTDINLEGDLGNTPVMQACYKDNHEALI--LLLSRGAKLCKKNK-LGCYPIHMTAFMGSLKCMDIVLNKGEEsgctid 235
Cdd:PHA02878 120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEItkLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGAN------ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 236 hqINFTNNEKSSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGAT-EIVKFMV---SSYNGDNKIVDLp 311
Cdd:PHA02878 194 --VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLehgVDVNAKSYILGL- 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1951993450 312 dgndeTPLHKSVLFDHVelAEYLISAGANINSEDKESRTPLLLA 355
Cdd:PHA02878 271 -----TALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
456-541 |
4.26e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.99 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 456 LHFAACYGRFNTCQRLLRFMSDARLLndgDEKGLTPLHLAAENGHEKIVfLLLKKGALLLSDHHGWTALHYAALNGYTRT 535
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQ---DKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKDNGRTALHYAARSGHLEI 76
|
....*.
gi 1951993450 536 IRTLLE 541
Cdd:pfam12796 77 VKLLLE 82
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
423-504 |
8.60e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.83 E-value: 8.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 423 LHYACRHGVPNSVNNLLGLNMSLYSKSKNKRSPLHFAACYGRFNTCQRLLRFMSdarllNDGDEKGLTPLHLAAENGHEK 502
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-----VNLKDNGRTALHYAARSGHLE 75
|
..
gi 1951993450 503 IV 504
Cdd:pfam12796 76 IV 77
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
492-583 |
8.85e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.83 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 492 LHLAAENGHEKIV-FLLLKKGALLLSDHHGWTALHYAALNGYTRTIRTLLETSIGlidKTDKENNTAIHLAGREGHAKAV 570
Cdd:pfam12796 1 LHLAAKNGNLELVkLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|...
gi 1951993450 571 SLLLENGASIMLN 583
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
222-460 |
1.19e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 74.32 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 222 IVLNKGEESGCTIDHQINFTNNEKSSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGAT-----EIVKf 296
Cdd:PHA03100 12 IIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVK- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 297 mVSSYNGDNkiVDLPDGNDETPLH--KSVLFDHVELAEYLISAGANINSEDKESRTPLLLATSCSAWKS--VNLLLAKGA 372
Cdd:PHA03100 91 -LLLEYGAN--VNAPDNNGITPLLyaISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 373 DVKLKDNFgrnflhlmvlqpgglknlnnDFLQMENIKQLVTDEdcEGCTPLHYACRHGVPNSVNNLLGLNMSLYSKSKNK 452
Cdd:PHA03100 168 DINAKNRV--------------------NYLLSYGVPINIKDV--YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225
|
....*...
gi 1951993450 453 RSPLHFAA 460
Cdd:PHA03100 226 DTPLHIAI 233
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
73-166 |
2.49e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 66.68 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 73 LHHAAKLGSMDLLLMIINESAkeGINALDSQGNTPLHWAVEKNKVDCLKvLLCRGADPNIPNYYRlTPLHLAIQLFHNTI 152
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGA--DANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDNGR-TALHYAARSGHLEI 76
|
90
....*....|....
gi 1951993450 153 VETLILHGtTDINL 166
Cdd:pfam12796 77 VKLLLEKG-ADINV 89
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
115-380 |
3.07e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 70.08 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 115 NKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGT-TDINLEGDLGNTP---VMQACYKDNHEALILL 190
Cdd:PHA03100 13 IKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGAdINSSTKNNSTPLHylsNIKYNLTDVKEIVKLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 191 LSRGAKLCKKNKLGCYPIH--MTAFMGSLKCMDIVLNKGEEsgctidhqINFTNNEKSSPLHLAVQNGNID--VVKACIS 266
Cdd:PHA03100 93 LEYGANVNAPDNNGITPLLyaISKKSNSYSIVEYLLDNGAN--------VNIKNSDGENLLHLYLESNKIDlkILKLLID 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 267 YGAKIDlrqsdnatalhfaatqGATEIVKFMVSSYNgdnkiVDLPDGNDETPLHKSVLFDHVELAEYLISAGANINSEDK 346
Cdd:PHA03100 165 KGVDIN----------------AKNRVNYLLSYGVP-----INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
|
250 260 270
....*....|....*....|....*....|....
gi 1951993450 347 ESRTPLLLATSCSAWKSVNLLLAKGADVKLKDNF 380
Cdd:PHA03100 224 YGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
247-649 |
4.77e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 70.09 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 247 SPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGATEIVKFMVSSYNGDNKivdlpdgnDETPLHKSVLFD 326
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK--------NDLSLLKAIRNE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 327 HVELAEYLISAGANINSEDKESRTPLLLATSC-SAWKSVNLLLAKGADVKLKDNFGRNFLHLMVlqpgglknlNNDFlQM 405
Cdd:PHA02876 252 DLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMA---------KNGY-DT 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 406 ENIKQL------VTDEDCEGCTPLHYACR-HGVPNSVNNLLGLNMSLYSKSKNKRSPLHFAACYGRFNTCQRLLRFMSDA 478
Cdd:PHA02876 322 ENIRTLimlgadVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 479 RLLNdgdEKGLTPLHLA--AENGHEKIVFLLLKKGALLLSDHHGWTALHYAALNGYTRTIRTLLETSIGLIDKTDKENNT 556
Cdd:PHA02876 402 EALS---QKIGTALHFAlcGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 557 AIHLAgrEGHAKAVSLLLENGASIM--------LNANGASFIHEAIRYGKKDAVLASIQSDRwEEVLQTFSHTSSYKCAI 628
Cdd:PHA02876 479 PLLIA--LEYHGIVNILLHYGAELRdsrvlhksLNDNMFSFRYIIAHICIQDFIRHDIRNEV-NPLKRVPTRFTSLRESF 555
|
410 420
....*....|....*....|.
gi 1951993450 629 LEMIyHLPETFKTLLDKCMTE 649
Cdd:PHA02876 556 KEII-QSDDTFKRIWLRCKEE 575
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
147-373 |
8.96e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.48 E-value: 8.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 147 LFHNTIVETLILHGTTDINLEGDLGNTPVMQACYKDNHEALILLLSRGAKLCKKNKLGCYPIHMTAFMGSLKCMDIVLnk 226
Cdd:PHA02875 11 LFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 227 geESGCTIDHQINFTNNeksSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGATEIVKFMVSSyngdNK 306
Cdd:PHA02875 89 --DLGKFADDVFYKDGM---TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH----KA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1951993450 307 IVDLPDGNDETPLHKSVLFDHVELAEYLISAGANINSEDKESRTPLLlatsCSAWKS-----VNLLLAKGAD 373
Cdd:PHA02875 160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL----CYAIENnkidiVRLFIKRGAD 227
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
106-390 |
2.23e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 67.38 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 106 TPLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHNTivetlilhgttdinlegdlgntpvmqacyKDNHE 185
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNL-----------------------------TDVKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 186 ALILLLSRGAklckknklgcypihmtafmgslkcmdivlnkgeesgctidhQINFTNNEKSSPLHLAVQN--GNIDVVKA 263
Cdd:PHA03100 88 IVKLLLEYGA-----------------------------------------NVNAPDNNGITPLLYAISKksNSYSIVEY 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 264 CISYGAKIDLRQSDNATALHFAATQGA--TEIVKFMVSS---YNGDNKIvdlpdgndetplhksvlfdhvelaEYLISAG 338
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKgvdINAKNRV------------------------NYLLSYG 182
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1951993450 339 ANINSEDKESRTPLLLATSCSAWKSVNLLLAKGADVKLKDNFGRNFLHLMVL 390
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
43-134 |
4.36e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.13 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 43 IAEGNICRVRNFvLKNPGSLAARDDSEATPLHHAAKLGSMDLLLMIINESAKEginaLDSQGNTPLHWAVEKNKVDCLKV 122
Cdd:pfam12796 5 AKNGNLELVKLL-LENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN----LKDNGRTALHYAARSGHLEIVKL 79
|
90
....*....|..
gi 1951993450 123 LLCRGADPNIPN 134
Cdd:pfam12796 80 LLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
176-274 |
5.35e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.13 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 176 MQACYKDNHEALILLLSRGAKLCKKNKLGCYPIHMTAFMGSLKCMDIVLNKGeesgctidhQINFTNNEKsSPLHLAVQN 255
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA---------DVNLKDNGR-TALHYAARS 71
|
90
....*....|....*....
gi 1951993450 256 GNIDVVKACISYGAKIDLR 274
Cdd:pfam12796 72 GHLEIVKLLLEKGADINVK 90
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
364-601 |
1.47e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 65.05 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 364 VNLLLAKGADVKLKDNFGRNFLHLMVLQPGGLKNLNNDFLqMENIKQLVTDEDCeGCTPLH-YACRHGVPNSVNNLLGLN 442
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLL-LEAGADVNAPERC-GFTPLHlYLYNATTLDVIKLLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 443 MSLYSKSKNKRSPLHfaACYGRFNTCQRLLRFMSDARL-LNDGDEKGLTPLHLAAENGH---EKIVFLLLKKGALLLSDH 518
Cdd:PHA03095 108 ADVNAKDKVGRTPLH--VYLSGFNINPKVIRLLLRKGAdVNALDLYGMTPLAVLLKSRNanvELLRLLIDAGADVYAVDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 519 HGWTALHYAALN--GYTRTIRTLLETSIGLIdKTDKENNTAIHLAGREGHAKA--VSLLLENGASI-MLNANGASFIHEA 593
Cdd:PHA03095 186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPA-ATDMLGNTPLHSMATGSSCKRslVLPLLIAGISInARNRYGQTPLHYA 264
|
....*...
gi 1951993450 594 IRYGKKDA 601
Cdd:PHA03095 265 AVFNNPRA 272
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
326-580 |
2.19e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.08 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 326 DHVELAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLLAKGADVKLKDNFGRNFLHLMVLQPG---------GLK 396
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNidtikaiidNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 397 NLNNDFLQMENIkqlVTDEDCEGCTPLHYAcrhgvpnsvnnllglNMSLYSKSKNKRSPLHFAAcygRFNTCQRLL-RFM 475
Cdd:PHA02876 236 NINKNDLSLLKA---IRNEDLETSLLLYDA---------------GFSVNSIDDCKNTPLHHAS---QAPSLSRLVpKLL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 476 SDARLLNDGDEKGLTPLHLAAENGH--EKIVFLLLKKGALLLSDHHGWTALHYAA-LNGYTRTIRTLLETSIGlIDKTDK 552
Cdd:PHA02876 295 ERGADVNAKNIKGETPLYLMAKNGYdtENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGAN-VNARDY 373
|
250 260
....*....|....*....|....*...
gi 1951993450 553 ENNTAIHLAGREGHAKAVSLLLENGASI 580
Cdd:PHA02876 374 CDKTPIHYAAVRNNVVIINTLLDYGADI 401
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
103-253 |
2.53e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 64.13 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 103 QGNTPLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGTTdINLEGDLGNTPV-MQACYK 181
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS-TDARDKCGNTPLhISVGYC 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1951993450 182 DNHEALILLLSRGAKL-CKKNKLGCYPIHMTafMGSLKCMDIVLNKGEEsgctidhqINFTNNEKSSPLHLAV 253
Cdd:PHA02878 246 KDYDILKLLLEHGVDVnAKSYILGLTALHSS--IKSERKLKLLLEYGAD--------INSLNSYKLTPLSSAV 308
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
65-334 |
2.95e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.83 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 65 RDDSEATPLHHAAKLGSMDLLLMIINESAKegINALDSQGNTPLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLA 144
Cdd:PHA02874 120 KDAELKTFLHYAIKKGDLESIKMLFEYGAD--VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 145 IQLfhntivetlilhgttdinleGDLgntpvmqACYKdnhealiLLLSRGAKLCKKNKLGCYPIHmTAFMGSLKCMDIVL 224
Cdd:PHA02874 198 AEY--------------------GDY-------ACIK-------LLIDHGNHIMNKCKNGFTPLH-NAIIHNRSAIELLI 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 225 NkgeesgctiDHQINFTNNEKSSPLHLAVQNG-NIDVVKACISYGAKIDLRQSDNATALHFAATQ-GATEIVKFMVSSYN 302
Cdd:PHA02874 243 N---------NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAV 313
|
250 260 270
....*....|....*....|....*....|..
gi 1951993450 303 GDNKIVDLPdgnDETPLHKSVLFDHVELAEYL 334
Cdd:PHA02874 314 LIKEADKLK---DSDFLEHIEIKDNKEFSDFI 342
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
112-439 |
3.05e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 64.31 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 112 VEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGtTDINLEGDLGNTPVMQACYKDNHEALILLL 191
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG-ADVNIIALDDLSVLECAVDSKNIDTIKAII 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 192 SRGAKLCKKNKLGCYPIHMTAFMGSLKCMDivlnkgeeSGCTidhqINFTNNEKSSPLHLAVQNGNID-VVKACISYGAK 270
Cdd:PHA02876 232 DNRSNINKNDLSLLKAIRNEDLETSLLLYD--------AGFS----VNSIDDCKNTPLHHASQAPSLSrLVPKLLERGAD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 271 IDLRQSDNATALHFAATQG-ATEIVKFMVSSyngdNKIVDLPDGNDETPLHKSVLFD-HVELAEYLISAGANINSEDKES 348
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGyDTENIRTLIML----GADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 349 RTPLLLATSCSAWKSVNLLLAKGADVKLKDNFGRNFLHLMVLQPGGLKNLNNDFLQMENikqlVTDEDCEGCTPLHYACR 428
Cdd:PHA02876 376 KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGAN----VNSKNKDLSTPLHYACK 451
|
330
....*....|.
gi 1951993450 429 HGVPNSVNNLL 439
Cdd:PHA02876 452 KNCKLDVIEML 462
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
76-319 |
1.26e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.93 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 76 AAKLGSMDLLLMIINESAKEGINALDsqGNTPLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVET 155
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYD--GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 156 LILHGTTDINLEGDLGNTPVMQACYKDNHEALILLLSRGAKLCKKNKLGCYPIHMTAFMGSLKCMDIVlnkgeesgctID 235
Cdd:PHA02875 87 LLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL----------ID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 236 HQ--INFTNNEKSSPLHLAVQNGNIDVVKACISYGAKID-LRQSDNATALHFAATQGATEIVKFMVSSyNGDNKIVDLPD 312
Cdd:PHA02875 157 HKacLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKR-GADCNIMFMIE 235
|
....*..
gi 1951993450 313 GNDETPL 319
Cdd:PHA02875 236 GEECTIL 242
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
35-258 |
1.22e-08 |
|
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: 59.26 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 35 NPSLIFKLIAEGNICRVRNFVLKNPGSLAARDDSEATPLHHAAKLGSMDLLLMIInESAKEGIN-ALDS---QGNTPLHW 110
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM-EAAPELVNePMTSdlyQGETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 111 AVEKNKVDCLKVLLCRGAD------------PNIPN--YYRLTPLHLAIQLFHNTIVETLILHGtTDINLEGDLGNTPVm 176
Cdd:cd22192 96 AVVNQNLNLVRELIARGADvvspratgtffrPGPKNliYYGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVL- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 177 qacykdnHealILLLSRGAKLCKknklgcypiHMtafmgslkcMDIVLN-KGEESGCTIDHQinfTNNEKSSPLHLAVQN 255
Cdd:cd22192 174 -------H---ILVLQPNKTFAC---------QM---------YDLILSyDKEDDLQPLDLV---PNNQGLTPFKLAAKE 222
|
...
gi 1951993450 256 GNI 258
Cdd:cd22192 223 GNI 225
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
247-383 |
1.33e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.46 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 247 SPLHLAVQNGNIDVVKACISYGAKI-DLRQSDNATALHFAATQGATEIVKFMVSsYNGDNkivDLPDGNDETPLHKSVLF 325
Cdd:PHA02875 70 SELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIA-RGADP---DIPNTDKFSPLHLAVMM 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1951993450 326 DHVELAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLLAKGADVklkDNFGRN 383
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI---DYFGKN 200
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
818-995 |
3.62e-08 |
|
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.
Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 55.74 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 818 KLAYIFNGSNIIDWSIYISSIVfvssmcstpLVVSHFQWQFGAIAVFASW--VNFLIYLQRFESYGIYIVMFWEILRTLL 895
Cdd:pfam00520 60 KKRYFRSPWNILDFVVVLPSLI---------SLVLSSVGSLSGLRVLRLLrlLRLLRLIRRLEGLRTLVNSLIRSLKSLG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 896 RIVFLFFFLILafglSFYVFLY---------------PQMTFSRPYFALMQSFTMMLGdIDYQEGFLKPLLDDQIQFPFF 960
Cdd:pfam00520 131 NLLLLLLLFLF----IFAIIGYqlfggklktwenpdnGRTNFDNFPNAFLWLFQTMTT-EGWGDIMYDTIDGKGEFWAYI 205
|
170 180 190
....*....|....*....|....*....|....*
gi 1951993450 961 TFIhliMFTLLIPILLMNLLIGLAVGDIAEVQRNA 995
Cdd:pfam00520 206 YFV---SFIILGGFLLLNLFIAVIIDNFQELTERT 237
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
97-144 |
5.13e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.42 E-value: 5.13e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1951993450 97 INALDSQGNTPLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLA 144
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
7-197 |
1.58e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 55.45 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 7 RMLSSKGKKSNVYDGIFLQD-ESCSSLDENPSLIFKLIAEGnicrvrnfvlknpGSLAARDDSEATPLHHAAKLGSMDLL 85
Cdd:PHA02876 325 RTLIMLGADVNAADRLYITPlHQASTLDRNKDIVITLLELG-------------ANVNARDYCDKTPIHYAAVRNNVVII 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 86 LMIINESAKegINALDSQGNTPLHWAV-EKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGTTDI 164
Cdd:PHA02876 392 NTLLDYGAD--IEALSQKIGTALHFALcGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADV 469
|
170 180 190
....*....|....*....|....*....|...
gi 1951993450 165 NLEGDLGNTPVMQACykDNHEALILLLSRGAKL 197
Cdd:PHA02876 470 NAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
67-195 |
1.64e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 55.27 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 67 DSEATPLHHAAKLGSMDLLLMIINESAKegINALDSQGNTPLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIQ 146
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGAN--VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1951993450 147 LFHNTIVETLILHGTTDINLEGDLGNTPVMQACYKDnHEALILLLSRGA 195
Cdd:PHA02878 244 YCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKS-ERKLKLLLEYGA 291
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
51-195 |
1.68e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.03 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 51 VRNFVLKNPGSLAARDDSEATPLH-----HAAKLGSMDLLLmiineSAKEGINALDSQGNTPLHWAVE--KNKVDCLKVL 123
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAvllksRNANVELLRLLI-----DAGADVYAVDDRFRSLLHHHLQsfKPRARIVREL 208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1951993450 124 LCRGADPNIPNYYRLTPLHLA--IQLFHNTIVETLILHGtTDINLEGDLGNTPVMQACYKDNHEALILLLSRGA 195
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPLHSMatGSSCKRSLVLPLLIAG-ISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
69-124 |
2.71e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 2.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1951993450 69 EATPLHHAAKLGSMDLLLMIINESAKegINALDSQGNTPLHWAVEKNKVDCLKVLL 124
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAD--INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
246-298 |
2.76e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 2.76e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1951993450 246 SSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFAATQGATEIVKFMV 298
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
319-448 |
2.89e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 49.34 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 319 LHKSVLFDHVELAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLLAKGAdvklkdnfgrnflhlmvlqpgglknl 398
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-------------------------- 54
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1951993450 399 nndflqmenikqlvTDEDCEGCTPLHYACRHGVPNSVNNLLGLNMSLYSK 448
Cdd:pfam12796 55 --------------VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
520-574 |
3.46e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.04 E-value: 3.46e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1951993450 520 GWTALHYAALNGYTRTIRTLLETSIgLIDKTDKENNTAIHLAGREGHAKAVSLLL 574
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
317-596 |
3.90e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.81 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 317 TPLHKSVLFDHVELAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLLAKGADVKLKDnfgrnflhlmvlqpggLK 396
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILP----------------IP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 397 NLNNDflqmenikqlvtdedcegctplhyacrhgvpnSVNNLLGLNMSLYSKSKNKRSPLHFAACYGRFNTCQRLLRFMS 476
Cdd:PHA02874 101 CIEKD--------------------------------MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 477 DarlLNDGDEKGLTPLHLAAE-NGHEKIVFLLLKKGALLLSDHHGWTALHYAALNGYTRTIRTLLETSIGLIDKTdKENN 555
Cdd:PHA02874 149 D---VNIEDDNGCYPIHIAIKhNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC-KNGF 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1951993450 556 TAIHLAGRegHAKAVSLLLENGASI-MLNANGASFIHEAIRY 596
Cdd:PHA02874 225 TPLHNAII--HNRSAIELLINNASInDQDIDGSTPLHHAINP 264
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
172-392 |
5.49e-07 |
|
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: 53.86 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 172 NTPVMQACYKDNHEAL-ILLLSRGAKLCKKNKLGCYPIHMTAFMGSLKCMDIVLNKGEEsgcTIDHQINFTNNEKSSPLH 250
Cdd:cd22192 18 ESPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE---LVNEPMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 251 LAVQNGNIDVVKACISYGAKIdlrQSDNATALHFaatqgateivkfmvsSYNGDNKIVdlpdgndetplhksvlfdhveL 330
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADV---VSPRATGTFF---------------RPGPKNLIY---------------------Y 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1951993450 331 AEYLISAGANINSEDkesrtplllatscsawkSVNLLLAKGADVKLKDNFGRNFLHLMVLQP 392
Cdd:cd22192 136 GEHPLSFAACVGNEE-----------------IVRLLIEHGADIRAQDSLGNTVLHILVLQP 180
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
104-157 |
6.00e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 6.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1951993450 104 GNTPLHWAVEKNKVDCLKVLLCRGADPNIPNYYRLTPLHLAIqLFHNT-IVETLI 157
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA-SNGNVeVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
7-145 |
6.09e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.49 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 7 RMLSSKGKKSNVYDGIF--LQDESCSSLDENPSLIFKLIAEGniCRVrnfvlknpgslAARDDSEATPLHHAAKLGSMDL 84
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFrsLLHHHLQSFKPRARIVRELIRAG--CDP-----------AATDMLGNTPLHSMATGSSCKR 237
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1951993450 85 LLM---IINESakeGINALDSQGNTPLHWA-VEKNKVDCLKvLLCRGADPNIPNYYRLTPLHLAI 145
Cdd:PHA03095 238 SLVlplLIAGI---SINARNRYGQTPLHYAaVFNNPRACRR-LIALGADINAVSSDGNTPLSLMV 298
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
706-1017 |
8.28e-07 |
|
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: 53.09 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 706 HPVcKEYLLMKWMAYGFKAHLLNLAIYSLGLIPLTLLIINavRPecldiLEKRDHlkqtdfinssVRTECNITRKLEPLR 785
Cdd:cd22192 283 TPV-KELVSLKWKRYGRPYFRILALLYLLYIIIFTLCCVY--RP-----LKPRPE----------NNTDPRDITLYVQKT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 786 LKDT-QYTKVCMSLVFCM-SVFGIIK----EVAQLCQQKLAYIFnGSNIIDWSIYISSIVFVSSMCSTPLV-VSHFQWQ- 857
Cdd:cd22192 345 LQESyVTPKDYLRLVGELiSVLGAIVilllEIPDILRVGVKRYF-GQTVLGGPFHVIIITYACLVLLTLVLrLTSLSGEv 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 858 -FGAIAVFASWVNFLIYLQRFESYGIYIVMFWEIL-RTLLRIVFLFFFLILAFGLSFYVFLYPQMTFSRPYF-----ALM 930
Cdd:cd22192 424 vPMSLALVLGWCNVMYFARGFQMLGPFTIMIQKIIfGDLMKFCWLMFVVILGFSSAFYMIFQTEDPDSLGHFydfpmTLF 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 931 QSFTMMLGDIDyqeGFlkplLDDQIQFPFFTFIHLIMFTLLIPILLMNLLIGLAVGDIAEV--QRNACLKriaMQVSLHT 1008
Cdd:cd22192 504 STFELFLGLID---GP----ANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVahERDELWR---AQVVATT 573
|
330
....*....|..
gi 1951993450 1009 -SLEKKLP--FW 1017
Cdd:cd22192 574 lMLERRLPrcLW 585
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
520-1021 |
3.27e-06 |
|
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: 51.42 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 520 GWTALHYAALN---GYTRTIRTLLETSIGLIDK--------TDK--ENNTAIHLAGREGHAKAVSLLLENGASIMLNANG 586
Cdd:cd21882 26 GKTCLHKAALNlndGVNEAIMLLLEAAPDSGNPkelvnapcTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 587 ASFI---HEAIRYGKKDAVLASIqSDRWEEVLQTFSHtsSYKCAILEMIYHLPETFKTLL----DKCMTESTGDKKSPNF 659
Cdd:cd21882 106 RFFRkspGNLFYFGELPLSLAAC-TNQEEIVRLLLEN--GAQPAALEAQDSLGNTVLHALvlqaDNTPENSAFVCQMYNL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 660 YIEYNFK--YLQcPLNFRKAHKGeknvhyepLTTLNAMVQHQRIDLLSHPVCKEYL---------LMKWmAYGfkahLLN 728
Cdd:cd21882 183 LLSYGAHldPTQ-QLEEIPNHQG--------LTPLKLAAVEGKIVMFQHILQREFSgpyqplsrkFTEW-TYG----PVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 729 LAIYSLGLIP-------LTLLIINAVRPECLDIL----------EKRDHLKQTDF-INSSVR-------TECNITRKLEP 783
Cdd:cd21882 249 SSLYDLSEIDsweknsvLELIAFSKKREARHQMLvqeplnellqEKWDRYGRPYFcFNFACYllymiifTVCAYYRPLKD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 784 LRLKDTQYTKVCMSLVFCMSVFGIIKEVAQLCQQkLAYIFNGSNIIDWSI---YISSIVFVSSMCSTPLVVSHFQWQFGA 860
Cdd:cd21882 329 RPANQEAKATFGDSIRLVGEILTVLGGVYILLGE-IPYFFRRRLSRWFGFldsYFEILFITQALLVLLSMVLRFMETEGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 861 IA--VFA---SWVNFLIYLQRFESYGIYIVMFWE-ILRTLLRIVFLFFFLILAFGLSFYVFL----YPQM-TFSRPYFAL 929
Cdd:cd21882 408 VVplVFSlvlGWCNVLYYTRGFQMLGIYTVMIQKmILRDLMRFCWVYLVFLFGFASAFVILFqtedPNKLgEFRDYPDAL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 930 MQSFTMMLGDIDYQegflkplLDDQIQFPFFTFIHLIMFTLLIPILLMNLLIGL---AVGDIAEVQRNACLKRIAMQVsl 1006
Cdd:cd21882 488 LELFKFTIGMGDLP-------FNENVDFPFVYLILLLAYVILTYLLLLNMLIALmgeTVNRVAQESDEIWKLQKAITT-- 558
|
570
....*....|....*
gi 1951993450 1007 hTSLEKKLPfWFLKR 1021
Cdd:cd21882 559 -LMLERKYP-RCLRK 571
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
471-580 |
4.52e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.02 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 471 LLRFMSDARLlndGDEKGLTPLHLAAENGHEKIV--------------------------------FLLLKKGALLLSDH 518
Cdd:PLN03192 544 LLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVlvllkhacnvhirdangntalwnaisakhhkiFRILYHFASISDPH 620
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1951993450 519 HGWTALHYAALNGYTRTIRTLLEtsIGL-IDKTDKENNTAIHLAGREGHAKAVSLLLENGASI 580
Cdd:PLN03192 621 AAGDLLCTAAKRNDLTAMKELLK--QGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
103-134 |
5.29e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 44.20 E-value: 5.29e-06
10 20 30
....*....|....*....|....*....|...
gi 1951993450 103 QGNTPLHWAVEK-NKVDCLKVLLCRGADPNIPN 134
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
280-335 |
7.84e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 7.84e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1951993450 280 TALHFAATQGATEIVKFMVSSyngdNKIVDLPDGNDETPLHKSVLFDHVELAEYLI 335
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK----GADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
53-251 |
1.05e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.19 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 53 NFVLKNPGSLAARDDSEATPLHHAAKLGSMDLLLMIINESAKEGINalDSQGNTPLHWAVEKNKVDCLKVLLCRGADPNI 132
Cdd:PHA02874 141 KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK--DNNGESPLHNAAEYGDYACIKLLIDHGNHIMN 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 133 PNYYRLTPLHLAIqLFHNTIVETLILHGT---TDINlegdlGNTPVMQA----CYKDnheALILLLSRGAKLCKKNKLGC 205
Cdd:PHA02874 219 KCKNGFTPLHNAI-IHNRSAIELLINNASindQDID-----GSTPLHHAinppCDID---IIDILLYHKADISIKDNKGE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 206 YPIHmTAF---------------------MGSLKCMDI-------------------------------VLNKGEESGCT 233
Cdd:PHA02874 290 NPID-TAFkyinkdpvikdiianavlikeADKLKDSDFlehieikdnkefsdfikecneeiedmkktkcGCDKNIFDLCL 368
|
250
....*....|....*...
gi 1951993450 234 IDHQINFTNNEKSSPLHL 251
Cdd:PHA02874 369 IRIKHKFDGNEDSIKDYL 386
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
103-132 |
1.78e-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: 42.57 E-value: 1.78e-05
10 20 30
....*....|....*....|....*....|
gi 1951993450 103 QGNTPLHWAVEKNKVDCLKVLLCRGADPNI 132
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
3-205 |
2.34e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 48.34 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 3 YSIRRMLSSKGKKSNVYDgiflqdescsslDENPSLIFKLIAEGNIcRVRNFVLKNPGSLAARDDSEATPLHHA-AKLGS 81
Cdd:PHA02878 181 QRLTELLLSYGANVNIPD------------KTNNSPLHHAVKHYNK-PIVHILLENGASTDARDKCGNTPLHISvGYCKD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 82 MDLLLMIINESAKegINALDS-QGNTPLHWAVEKNKVdcLKVLLCRGADPNIPNYYRLTPLHLAIQLFHN-TIVETLILH 159
Cdd:PHA02878 248 YDILKLLLEHGVD--VNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQYLCiNIGRILISN 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1951993450 160 GTTDINLEGDLGNTpvmqACYKDNHEALilllsRGAKLCKKNKLGC 205
Cdd:PHA02878 324 ICLLKRIKPDIKNS----EGFIDNMDCI-----TSNKRLNQIKDKC 360
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
849-1021 |
4.58e-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: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 849 LVVSHFQWQFG--------AIAVFASWVNFLIYLQRFESYGIYIVMfweILRTLLRIVFLFFFLILAFGLSFYVFLY--- 917
Cdd:cd22194 459 VIVSVFLYLFAykeylaclVLAMALGWANMLYYTRGFQSLGIYSVM---IQKVILNDVLKFLLVYILFLLGFGVALAsli 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 918 ---PQMTFSRPYF----ALMQSF--TMMLGDIDYQEGFLKPLLddqiqfpfFTFIhLIMFTLLIPILLMNLLIGLAVGDI 988
Cdd:cd22194 536 edcPDDSECSSYGsfsdAVLELFklTIGLGDLEIQQNSKYPIL--------FLLL-LITYVILTFVLLLNMLIALMGETV 606
|
170 180 190
....*....|....*....|....*....|....*...
gi 1951993450 989 AEVQRNAclKRI-----AMQVslhTSLEKKLPFWFLKR 1021
Cdd:cd22194 607 ENVSKES--ERIwrlqrARTI---LEFEKSLPEWLRKR 639
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
420-602 |
6.40e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.97 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 420 CTPLHYACRHGVPNSVNNLLGLNMSLYSKSKNKRSPLHFAAcygrfNTCQRLLRFMSDARLL-------NDGDEKGLTPL 492
Cdd:PHA03100 36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLS-----NIKYNLTDVKEIVKLLleyganvNAPDNNGITPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 493 HLAAEN--GHEKIV-FLLLKKGALLLSDHHGWTALHYAALNGY--TRTIRTLLE--------TSIGL-------IDKTDK 552
Cdd:PHA03100 111 LYAISKksNSYSIVeYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDkgvdinakNRVNYllsygvpINIKDV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1951993450 553 ENNTAIHLAGREGHAKAVSLLLENGASI-MLNANGASFIHEAIRYGKKDAV 602
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIF 241
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
83-226 |
6.96e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 47.06 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 83 DLLLMIINESAKEGinalDSQGNTPLHWAVEKNKVDCLKVLLCRGADPNI--------PN------YYRLTPLHLAIQLF 148
Cdd:cd22194 124 GILDRFINAEYTEE----AYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnPKykhegfYFGETPLALAACTN 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 149 HNTIVETLILHGTTDINLEGDLGNTpVMQACYK--DNHEA----------LILLLSRGAKLCK-KNKLGCYPIHMTAFMG 215
Cdd:cd22194 200 QPEIVQLLMEKESTDITSQDSRGNT-VLHALVTvaEDSKTqndfvkrmydMILLKSENKNLETiRNNEGLTPLQLAAKMG 278
|
170
....*....|.
gi 1951993450 216 SLKCMDIVLNK 226
Cdd:cd22194 279 KAEILKYILSR 289
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
488-540 |
7.01e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 7.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1951993450 488 GLTPLHLAAENGHEKIV-FLLLKKGALLLSDHHGWTALHYAALNGYTRTIRTLL 540
Cdd:pfam13637 1 ELTALHAAAASGHLELLrLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
22-209 |
7.34e-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: 46.80 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 22 IFLQDESCSSLDENPSlIFKLIAEGNICRVRNFVLKNPGSLAArddseATPLHHAAKlgSMDLLLMIINESAkeginaLD 101
Cdd:cd21882 3 ELLGLLECLRWYLTDS-AYQRGATGKTCLHKAALNLNDGVNEA-----IMLLLEAAP--DSGNPKELVNAPC------TD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 102 S--QGNTPLHWAVEKNKVDCLKVLLCRGAD-------------PNIPNYYRLTPLHLAIQLFHNTIVETLILHG--TTDI 164
Cdd:cd21882 69 EfyQGQTALHIAIENRNLNLVRLLVENGADvsaratgrffrksPGNLFYFGELPLSLAACTNQEEIVRLLLENGaqPAAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1951993450 165 NLEGDLGNTP----VMQACYKDNHEALI-----LLLSRGAKLCKKNKLGCYPIH 209
Cdd:cd21882 149 EAQDSLGNTVlhalVLQADNTPENSAFVcqmynLLLSYGAHLDPTQQLEEIPNH 202
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
53-193 |
9.49e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.17 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 53 NFVLKNPGSLAARDDSEATPLHHAAKLGSMDLLLMIINESAKEGINALDSQGNTPLHWAVEKNKVDCLKV--LLCRGADP 130
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISI 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1951993450 131 NIPNYYRLTPLHLAiQLFHNTIV-ETLILHGTtDINLEGDLGNTPVMQACYKDNHEALILLLSR 193
Cdd:PHA03095 251 NARNRYGQTPLHYA-AVFNNPRAcRRLIALGA-DINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
239-595 |
1.21e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 45.82 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 239 NFTNNEKSSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFaatqgateivkfmvssyngdnkivdLPDGNDETp 318
Cdd:PHA02946 66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-------------------------LSGTDDEV- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 319 lhksvlfdhVELAEYLISAGANIN-SEDKESRTPLLLATSCSAwKSVNLLLAKGADVKLKDNFGRNFLHlmvlqpgglKN 397
Cdd:PHA02946 120 ---------IERINLLVQYGAKINnSVDEEGCGPLLACTDPSE-RVFKKIMSIGFEARIVDKFGKNHIH---------RH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 398 LNNDFLQMENIKQLV------TDEDCEGCTPLHYACRHGVPN-SVNNLLGLNMSLYSKSKNKRSPLHFaacygrfntcqr 470
Cdd:PHA02946 181 LMSDNPKASTISWMMklgispSKPDHDGNTPLHIVCSKTVKNvDIINLLLPSTDVNKQNKFGDSPLTL------------ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 471 LLRFMSDARLLNdgdeKGLTPLHLAAENGHEKIVFLLLKKGALLLSD---HHGWTALHYAALNGYTRTIRTLLETSIGLI 547
Cdd:PHA02946 249 LIKTLSPAHLIN----KLLSTSNVITDQTVNICIFYDRDDVLEIINDkgkQYDSTDFKMAVEVGSIRCVKYLLDNDIICE 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1951993450 548 DktdkenntAIHLAGREGHAKAVSLLLENGASIMLNANGASFIHEAIR 595
Cdd:PHA02946 325 D--------AMYYAVLSEYETMVDYLLFNHFSVDSVVNGHTCMSECVR 364
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
842-983 |
1.32e-04 |
|
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: 46.00 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 842 SSMCSTPLVVSHFQWqFGAIAVFA---SWVNFLIYLQRFESYGIYIVMFWE-ILRTLLRIVFLffflilafglsFYVFLY 917
Cdd:cd22197 412 LTVLSQVLYFMGSEW-YLPLLVFSlvlGWLNLLYYTRGFQHTGIYSVMIQKvILRDLLRFLLV-----------YLVFLF 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 918 ----PQMTFSR----------------------------PYFALMQS------FTMMLGDIDYQEgflkpllddQIQFPF 959
Cdd:cd22197 480 gfavALVSLSReapspkapednnstvteqptvgqeeepaPYRSILDAslelfkFTIGMGELAFQE---------QLRFRG 550
|
170 180
....*....|....*....|....
gi 1951993450 960 FTFIHLIMFTLLIPILLMNLLIGL 983
Cdd:cd22197 551 VVLLLLLAYVLLTYVLLLNMLIAL 574
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
232-427 |
2.67e-04 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 45.29 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 232 CTIDHQINFTNNEKSSPLHLAVQNGNI--DVVKACISYGAKIDLRqsdnatalhfaATQGATEIVKFMVSSYNGDNKIVD 309
Cdd:PHA02716 199 CNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMK-----------CVNGMSPIMTYIINIDNINPEITN 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 310 L----PDGNDETPLhKSVLFDHVELAEYL--------ISAGANINSEDKESRTPL---LLATSCSAwKSVNLLLAKGADV 374
Cdd:PHA02716 268 IyiesLDGNKVKNI-PMILHSYITLARNIdisvvysfLQPGVKLHYKDSAGRTCLhqyILRHNIST-DIIKLLHEYGNDL 345
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1951993450 375 KLKDNFGRNFLH--------LMVLQPGGLKNLNNDFLQ-MENIKQLVTDEDCEGCTPL-HYAC 427
Cdd:PHA02716 346 NEPDNIGNTVLHtylsmlsvVNILDPETDNDIRLDVIQcLISLGADITAVNCLGYTPLtSYIC 408
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
453-504 |
2.75e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 2.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1951993450 453 RSPLHFAACYGRFNTCQRLLRFMSDarlLNDGDEKGLTPLHLAAENGHEKIV 504
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVL 50
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
104-132 |
2.98e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.16 E-value: 2.98e-04
10 20
....*....|....*....|....*....
gi 1951993450 104 GNTPLHWAVEKNKVDCLKVLLCRGADPNI 132
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
831-1021 |
3.37e-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: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 831 WSIYISS----IVFVSSM---CSTPLVVSHFQWqFGAIAVFA---SWVNFLIYLQRFESYGIYIVMFWE-ILRTLLRIVF 899
Cdd:cd22193 379 QSSFSDSyfeiLFFVQAVlviLSVVLYLFAYKE-YLACLVLAlalGWANMLYYTRGFQSMGIYSVMIQKvILRDLLRFLF 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 900 LffflilafglsFYVFLY---------------------PQMTFSRPYFALMQsFTMMLGDIDYQEgflkpllddQIQFP 958
Cdd:cd22193 458 V-----------YLLFLFgfavalvsliekcssdkkdcsSYGSFSDAVLELFK-LTIGMGDLEFQE---------NSTYP 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1951993450 959 FFTFIHLIMFTLLIPILLMNLLIGLAVGDIAEVQRNAclKRIAMQVSLHTSL--EKKLPFWFLKR 1021
Cdd:cd22193 517 AVFLILLLTYVILTFVLLLNMLIALMGETVNNVSKES--KRIWKLQRAITILefEKSFPECMRKA 579
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
238-285 |
4.69e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 4.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1951993450 238 INFTNNEKSSPLHLAVQNGNIDVVKACISYGAKIDLRQSDNATALHFA 285
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
517-574 |
5.05e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 5.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1951993450 517 DHHGWTALHYAALNGYTRTIRTLLETSIGlIDKTDKENNTAIHLAGREGHAKAVSLLL 574
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGAD-PTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
316-430 |
5.07e-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: 44.36 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 316 ETPLHKSVLFDHVELAEYLISAGANINSEDKE--------------SRTPLLLATSCSAWKSVNLLLAKGAD-VKLKDNF 380
Cdd:cd22194 142 QTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTdITSQDSR 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1951993450 381 GRNFLHLMVLQPGGLKNlNNDF--------LQMENIKQLVTDEDCEGCTPLHYACRHG 430
Cdd:cd22194 222 GNTVLHALVTVAEDSKT-QNDFvkrmydmiLLKSENKNLETIRNNEGLTPLQLAAKMG 278
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
244-273 |
7.27e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.95 E-value: 7.27e-04
10 20 30
....*....|....*....|....*....|
gi 1951993450 244 EKSSPLHLAVQNGNIDVVKACISYGAKIDL 273
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
447-504 |
7.74e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.73 E-value: 7.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1951993450 447 SKSKNKRSPLHFAACYGRFNTCQRLLRFMSDARLLndgDEKGLTPLHLAAENGHEKIV 504
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL---DKDGKTPLELAEENGFREVV 164
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
61-167 |
8.28e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.35 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 61 SLAARDDSEATPLHHAAKLGSMD-----LLLMIINESAKEG--------------INALDSQGNTPLHWAVEKNKVDCLK 121
Cdd:PTZ00322 53 ALEATENKDATPDHNLTTEEVIDpvvahMLTVELCQLAASGdavgarilltggadPNCRDYDGRTPLHIACANGHVQVVR 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1951993450 122 VLLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGTTDINLE 167
Cdd:PTZ00322 133 VLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
308-355 |
1.43e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 1.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1951993450 308 VDLPDGNDETPLHKSVLFDHVELAEYLISAGANINSEDKESRTPLLLA 355
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
554-602 |
2.55e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 2.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1951993450 554 NNTAIHLAGREGHAKAVSLLLENGASI-MLNANGASFIHEAIRYGKKDAV 602
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVL 50
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
314-503 |
2.65e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 41.52 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 314 NDETPLHKSVLFDHVELAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLLAKGADVKLKDNFGRNFLHLMVLQpG 393
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEE-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 394 GLKNLNNDFLQMENIKQLVTDedcEGCTPLHYACRHGVPNSVNNLLGLNMSLYSKSKNKRSPLHFAACYGRFNTCQRLLR 473
Cdd:PHA02875 80 DVKAVEELLDLGKFADDVFYK---DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
|
170 180 190
....*....|....*....|....*....|
gi 1951993450 474 FMSdarLLNDGDEKGLTPLHLAAENGHEKI 503
Cdd:PHA02875 157 HKA---CLDIEDCCGCTPLIIAMAKGDIAI 183
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
314-342 |
2.82e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.41 E-value: 2.82e-03
10 20
....*....|....*....|....*....
gi 1951993450 314 NDETPLHKSVLFDHVELAEYLISAGANIN 342
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
90-215 |
3.38e-03 |
|
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: 41.32 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 90 NESAKEGINA--LDS--QGNTPLHWAVEKNKVDCLKVLLCRGADPNIPN--------------YYRLTPLHLAIQLFHNT 151
Cdd:cd22193 58 TDNLKRFINAeyTDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 152 IVETLILHGTTDINLEG--DLGNTpVMQAC------YKDNHEALI----LLLSRGAKLCKKNKL-------GCYPIHMTA 212
Cdd:cd22193 138 IVQYLLENEHQPADIEAqdSRGNT-VLHALvtvadnTKENTKFVTrmydMILIRGAKLCPTVELeeirnndGLTPLQLAA 216
|
...
gi 1951993450 213 FMG 215
Cdd:cd22193 217 KMG 219
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
314-346 |
3.67e-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: 3.67e-03
10 20 30
....*....|....*....|....*....|....
gi 1951993450 314 NDETPLHKSVL-FDHVELAEYLISAGANINSEDK 346
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
92-329 |
3.99e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.41 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 92 SAKEGINAlDSQGNTPLHWAVEKNKVDCLKVLLCRGADPNI-PNYYrltPLHLAIQLFHNTIVETLILHGTTDINLEgDL 170
Cdd:PHA02791 19 SSKDAFKA-DVHGHSALYYAIADNNVRLVCTLLNAGALKNLlENEF---PLHQAATLEDTKIVKILLFSGMDDSQFD-DK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 171 GNTPVMQACYKDNHEALILLLSRGAKLCKKNKLGCYPIHMTAFMgsLKCMDIVLNKGEESGCTIDHQINFtnneksSPLH 250
Cdd:PHA02791 94 GNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWKTSFYHAVM--LNDVSIVSYFLSEIPSTFDLAILL------SCIH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 251 LAVQNGNIDVVKACISYGAKIDLRQS-----DNATALHFAATQGATEIVKFMVSSYNGDNKIVDLpdgnDETPLHKSVLF 325
Cdd:PHA02791 166 ITIKNGHVDMMILLLDYMTSTNTNNSllfipDIKLAIDNKDLEMLQALFKYDINIYSVNLENVLL----DDAEIAKMIIE 241
|
....
gi 1951993450 326 DHVE 329
Cdd:PHA02791 242 KHVE 245
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
123-175 |
4.65e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.56 E-value: 4.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1951993450 123 LLCRGADPNIPNYYRLTPLHLAIQLFHNTIVETLILHGtTDINLEGDLGNTPV 175
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTAL 53
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
75-198 |
5.18e-03 |
|
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: 40.83 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 75 HAAKLGSMDLLLMIIN---ESAKEGIN---ALDSQGN------TPLHWAVEKNKVDCLKVLLCRGADPNIPN-------- 134
Cdd:TIGR00870 87 HAISLEYVDAVEAILLhllAAFRKSGPlelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARAcgdffvks 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1951993450 135 ------YYRLTPLHLAIQLFHNTIVETLILHGtTDINLEGDLGNT----PVMQACYKDNHEALI-----LLLSRGAKLC 198
Cdd:TIGR00870 167 qgvdsfYHGESPLNAAACLGSPSIVALLSEDP-ADILTADSLGNTllhlLVMENEFKAEYEELScqmynFALSLLDKLR 244
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
148-252 |
5.33e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 40.35 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 148 FHNTIVETLILHGTTDINLEGDLG----NTPVMQACYKDNHEALILLLSRGAKLCK-KNKLGCYPIHMTAFMGSLKCMDI 222
Cdd:PHA02884 43 FHYTDIIDAILKLGADPEAPFPLSenskTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEI 122
|
90 100 110
....*....|....*....|....*....|
gi 1951993450 223 VLNKGEEsgctidhqINFTNNEKSSPLHLA 252
Cdd:PHA02884 123 LLSYGAD--------INIQTNDMVTPIELA 144
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
247-272 |
6.09e-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: 35.31 E-value: 6.09e-03
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
317-368 |
7.83e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 35.71 E-value: 7.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1951993450 317 TPLHKSVLFDHVELAEYLISAGANINSEDKESRTPLLLATSCSAWKSVNLLL 368
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
442-495 |
8.57e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 8.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1951993450 442 NMSLYSKSKNKRSPLHFAACYGRFNTCQRLLRFMSDARLLndgDEKGLTPLHLA 495
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK---DEEGLTALDLA 56
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
834-994 |
8.90e-03 |
|
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: 40.17 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 834 YISSIVFVSSMCSTPLVVSHF--QWQFGAIAVFA---SWVNFLIYLQRFESYGIYIVMFWE-ILRTLLR----------- 896
Cdd:cd22196 403 YCEILFFVQSLFLLASTVLYFcgRNEYVAFMVISlalGWANVLYYTRGFQQMGIYSVMIQKmILRDICRflfvylvflfg 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 897 --------IVFLFFFLILAFGLSFYVFLYPQMTFSRPYFALMQ--SFTMMLGDIDYQEGF-LKPLlddqiqfpfFTFIhL 965
Cdd:cd22196 483 fsaalvtlIEDGPPKGDVNTSQKECVCKSGYNSYNSLYSTCLElfKFTIGMGDLEFTENYkFKEV---------FIFL-L 552
|
170 180 190
....*....|....*....|....*....|..
gi 1951993450 966 IMFTLLIPILLMNLLIGL---AVGDIAEVQRN 994
Cdd:cd22196 553 ISYVILTYILLLNMLIALmgeTVSKIAQESKN 584
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
230-390 |
9.34e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.03 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 230 SGCTIDHQINFTNNEKSSPLHLAVQNGNIDVVKACISYgakIDLRQSDNATALHFAATQ--GATEIVKFMVSSYNGDNKI 307
Cdd:PHA02859 6 SEYDYNDFTDYLFYRYCNPLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIFSCLEKdkVNVEILKFLIENGADVNFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 308 VDlpdGNDETPLHKSVLFD---HVELAEYLISAGANINSEDKESRTPL-LLATSCSA-WKSVNLLLAKGADVKLKDNFGR 382
Cdd:PHA02859 83 TR---DNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLhMYMCNFNVrINVIKLLIDSGVSFLNKDFDNN 159
|
....*...
gi 1951993450 383 NFLHLMVL 390
Cdd:PHA02859 160 NILYSYIL 167
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
116-355 |
9.68e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 39.72 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 116 KVDCLKVLLCRGADPNIPNYYRlTPLHLAIQLFHNT------IVETLILHGTtDINLEGDLGNTPVMQACYK---DNHEA 186
Cdd:PHA02989 49 KIKIVKLLIDNGADVNYKGYIE-TPLCAVLRNREITsnkikkIVKLLLKFGA-DINLKTFNGVSPIVCFIYNsniNNCDM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 187 LILLLSRGAKLCK-KNKLGCYPIHM--TAFMGSLKCMDIVLNKGEESgctidhqINFTNNEKSSPLHLAVQNG----NID 259
Cdd:PHA02989 127 LRFLLSKGINVNDvKNSRGYNLLHMylESFSVKKDVIKILLSFGVNL-------FEKTSLYGLTPMNIYLRNDidviSIK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951993450 260 VVKACISYGAKIDLRQSDNATAL------HFAATQGATEIVKFMVSSYNGDNKivdlpDGNDETPLHKSVLFDHVELAEY 333
Cdd:PHA02989 200 VIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKYIKINKK-----DKKGFNPLLISAKVDNYEAFNY 274
|
250 260
....*....|....*....|..
gi 1951993450 334 LISAGANINSEDKESRTPLLLA 355
Cdd:PHA02989 275 LLKLGDDIYNVSKDGDTVLTYA 296
|
|
| |
